|
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: 735.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 10 SAVLTLLLAGYLAQQYLPLPTPKVIGIDLGTTYCSVGVFFPGTGKVKVIPDENGHISIPSMVSFTDN-DVYVGYESVELA 88
Cdd:cd10237 1 SGILALLLAGYLGQQYLPPPKPKIVGIDLGTTYSCVGVYHAVTGEVEVIPDDDGHKSIPSVVAFTPDgGVLVGYDALAQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 89 DSNPQNTIYDAKRFIGKIFTAEELEAEIGRYPFKVLNKN-GMVEFSVTSN-ETITVSPEYVGSRLLLKLKEMAEAYLGMP 166
Cdd:cd10237 81 EHNPSNTIYDAKRFIGKTFTKEELEEEAKRYPFKVVNDNiGSAFFEVPLNgSTLVVSPEDIGSLILLKLKKAAEAYLGVP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 167 VANAVISVPAEFDLKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLHKA-DVFHVLVIDLGGGTLDVSLLNKQGGMFLT 245
Cdd:cd10237 161 VAKAVISVPAEFDEKQRNATRKAANLAGLEVLRVINEPTAAAMAYGLHKKsDVNNVLVVDLGGGTLDVSLLNVQGGMFLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 246 RAMSGNNKLGGQDFNQRLLQYLYKQIYQTYGFVPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLltveeqdrkephssd 325
Cdd:cd10237 241 RAMAGNNHLGGQDFNQRLFQYLIDRIAKKFGKTLTDKEDIQRLRQAVEEVKLNLTNHNSASLSLP--------------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 326 telpkdklssaddhrvnsgfgrgLSDKKSGESQVLFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLV 405
Cdd:cd10237 306 -----------------------LQISLPSAFKVKFKEEITRDLFETLNEDLFQRVLEPIRQVLAEVELGKEDVDEIVLV 362
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 48928056 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 |
3.18e-174 |
|
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: 493.57 E-value: 3.18e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFFpgTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEEL 112
Cdd:cd24028 1 AIGIDLGTTYSCVAVWR--NGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 EAEIGRYPFKVLNKN-GMVEFSVT-SNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAA 190
Cdd:cd24028 79 QSDIKHWPFKVVEDEdGKPKIEVTyKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 191 NLAGLKILRVINEPTAAAMAYGLHK--ADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLY 268
Cdd:cd24028 159 TIAGLNVLRIINEPTAAALAYGLDKksSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 269 KQIYQTYGF-VPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDrkephssdtelpkdklssaddhrvnsgfgr 347
Cdd:cd24028 239 EEFKKKHGKdLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGID------------------------------ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 348 glsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDP 426
Cdd:cd24028 289 -------------FETTITRAKFEELCEDLFKKCLEPVEKVLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKEL 355
|
410 420
....*....|....*....|
gi 48928056 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 |
4.07e-130 |
|
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: 381.56 E-value: 4.07e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEEL 112
Cdd:cd10241 3 VIGIDLGTTYSCVGVF--KNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 EAEIGRYPFKVLNKNG--MVEFSVtSNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAA 190
Cdd:cd10241 81 QKDIKLLPFKIVNKNGkpYIQVEV-KGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 191 NLAGLKILRVINEPTAAAMAYGLHKADVFH-VLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYK 269
Cdd:cd10241 160 TIAGLNVLRIINEPTAAAIAYGLDKKGGEKnILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 270 QIYQTYGFVPSR-KEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDRKEPhssdtelpkdklssaddhrvnsgfgrg 348
Cdd:cd10241 240 LFKKKTGKDISKdKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSET--------------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 349 lsdkksgesqvlfeteISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDPN 427
Cdd:cd10241 293 ----------------LTRAKFEELNMDLFRKTLKPVQKVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFFnGKEPS 356
|
410
....*....|....*....
gi 48928056 428 TSVDPDLAVVTGVAIQAGI 446
Cdd:cd10241 357 RGINPDEAVAYGAAVQAGI 375
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
33-446 |
2.16e-119 |
|
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: 361.96 E-value: 2.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEEL 112
Cdd:pfam00012 1 VIGIDLGTTNSCVAVM--EGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 EAEIGRYPFKV---LNKNGMVEFSVTSNetiTVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEA 189
Cdd:pfam00012 79 QRDIKHLPYKVvklPNGDAGVEVRYLGE---TFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 190 ANLAGLKILRVINEPTAAAMAYGLHKADVFH-VLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLY 268
Cdd:pfam00012 156 GQIAGLNVLRIVNEPTAAALAYGLDKTDKERnIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 269 KQIYQTYGF-VPSRKEEIHRLRQAVEMVKLNLtlhqSAQlsvlltveeqdrkephSSDTELPKDKLSSADDHrvnsgfgr 347
Cdd:pfam00012 236 EEFKKKYGIdLSKDKRALQRLREAAEKAKIEL----SSN----------------QTNINLPFITAMADGKD-------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 348 glsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPN 427
Cdd:pfam00012 288 -------------VSGTLTRAKFEELVADLFERTLEPVEKALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPS 354
|
410
....*....|....*....
gi 48928056 428 TSVDPDLAVVTGVAIQAGI 446
Cdd:pfam00012 355 KGVNPDEAVAIGAAVQAGV 373
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
34-446 |
6.89e-119 |
|
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: 352.70 E-value: 6.89e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVFFpgTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEELE 113
Cdd:cd10233 2 IGIDLGTTYSCVGVWQ--NDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 114 AEIGRYPFKVLNKNGMVEFSVT-SNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANL 192
Cdd:cd10233 80 SDMKHWPFKVVSGGDKPKIQVEyKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 193 AGLKILRVINEPTAAAMAYGLHKADV--FHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQ 270
Cdd:cd10233 160 AGLNVLRIINEPTAAAIAYGLDKKGKgeRNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 271 IYQTY-GFVPSRKEEIHRLRQAVEMVKlnLTLHQSAQLSVlltveeqdrkephssdtELpkDKLSSADDhrvnsgfgrgl 349
Cdd:cd10233 240 FKRKHkKDISGNPRALRRLRTACERAK--RTLSSSTQASI-----------------EI--DSLFEGID----------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 350 sdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDPNT 428
Cdd:cd10233 288 -----------FYTSITRARFEELCADLFRSTLEPVEKVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNK 356
|
410
....*....|....*...
gi 48928056 429 SVDPDLAVVTGVAIQAGI 446
Cdd:cd10233 357 SINPDEAVAYGAAVQAAI 374
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
33-449 |
2.09e-112 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 339.88 E-value: 2.09e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEE 111
Cdd:COG0443 1 AIGIDLGTTNSVVAVV--EGGEPQVIPNAEGRRTLPSVVAFPkDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 112 LEAEIGRYpfkvlnkngmvefsvtsnetitvSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAAN 191
Cdd:COG0443 79 TEVGGKRY-----------------------SPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAAR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 192 LAGLKILRVINEPTAAAMAYGLHKADVFH-VLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQ 270
Cdd:COG0443 136 IAGLEVLRLLNEPTAAALAYGLDKGKEEEtILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 271 IYQTYGFVPSR-KEEIHRLRQAVEMVKlnltlhqsaqlsvlltvEEqdrkephssdtelpkdkLSSADDHRVNSGFGRGL 349
Cdd:COG0443 216 FGKEEGIDLRLdPAALQRLREAAEKAK-----------------IE-----------------LSSADEAEINLPFSGGK 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 350 SdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTS 429
Cdd:COG0443 262 H----------LDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPAVRERVKELFGKEPLKG 331
|
410 420
....*....|....*....|
gi 48928056 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 |
2.49e-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: 2.49e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEE 111
Cdd:cd10234 1 IIGIDLGTTNSCVAVM--EGGKPTVIPNAEGGRTTPSVVAFTkDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 112 LEAEIGRYPFkVLNKNGMVEFSVTSNEtitVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAAN 191
Cdd:cd10234 79 VERKQVPYPV-VSAGNGDAWVEIGGKE---YTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 192 LAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQI 271
Cdd:cd10234 155 IAGLEVLRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 272 YQTYGFVPSR-KEEIHRLRQAVEMVKLNLTLHQSAQLSVlltveeqdrkePH-SSDTELPKdklssaddHrvnsgfgrgl 349
Cdd:cd10234 235 KKEEGIDLSKdKMALQRLKEAAEKAKIELSSVLETEINL-----------PFiTADASGPK--------H---------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 350 sdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTS 429
Cdd:cd10234 286 -----------LEMKLTRAKFEELTEDLVERTIEPVEQALKDAKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKG 354
|
410
....*....|....*..
gi 48928056 430 VDPDLAVVTGVAIQAGI 446
Cdd:cd10234 355 VNPDEVVAIGAAIQGGV 371
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
34-446 |
7.14e-108 |
|
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: 324.63 E-value: 7.14e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVFfpgTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEELE 113
Cdd:cd24093 2 IGIDLGTTYSCVATY---ESSVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 114 AEIGRYPFKVLNKNGMVEFSVTS-NETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANL 192
Cdd:cd24093 79 KDMKTWPFKVIDVNGNPVIEVQYlGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 193 AGLKILRVINEPTAAAMAYGLHKADV---FHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYK 269
Cdd:cd24093 159 AGLNVLRIINEPTAAAIAYGLGAGKSekeRHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 270 QIYQTYGF-VPSRKEEIHRLRQAVEMVKlnLTLHQSAQLSVLLtveeqdrkephssdtelpkDKLSSADDhrvnsgfgrg 348
Cdd:cd24093 239 EFKKKTGLdISDDARALRRLRTAAERAK--RTLSSVTQTTVEV-------------------DSLFDGED---------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 349 lsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDPN 427
Cdd:cd24093 288 ------------FESSITRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLE 355
|
410
....*....|....*....
gi 48928056 428 TSVDPDLAVVTGVAIQAGI 446
Cdd:cd24093 356 KSINPDEAVAYGAAVQGAI 374
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
33-446 |
2.79e-106 |
|
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: 320.32 E-value: 2.79e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDND-VYVGYESVELADSNPQNTIYDAKRFIGKifTAEE 111
Cdd:cd10236 4 AVGIDLGTTNSLVATV--RSGQPEVLPDEKGEALLPSVVHYGEDGkITVGEKAKENAITDPENTISSVKRLMGR--SLAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 112 LEAEIGRYPFKVLNKNGMVEFSVTSNETITvsPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAAN 191
Cdd:cd10236 80 VKEELPLLPYRLVGDENELPRFRTGAGNLT--PVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 192 LAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQI 271
Cdd:cd10236 158 LAGLNVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADWILKQI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 272 YQTygfVPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDRkephssdtelpkdklssaddhrvnsgfgrglsd 351
Cdd:cd10236 238 GID---ARLDPAVQQALLQAARRAKEALSDADSASIEVEVEGKDWER--------------------------------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 352 kksgesqvlfetEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVD 431
Cdd:cd10236 282 ------------EITREEFEELIQPLVKRTLEPCRRALKDAGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSIN 349
|
410
....*....|....*
gi 48928056 432 PDLAVVTGVAIQAGI 446
Cdd:cd10236 350 PDEVVALGAAIQADI 364
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
32-449 |
1.42e-103 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 321.67 E-value: 1.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 32 KVIGIDLGTTYCSVGVFfPGtGKVKVIPDENGHISIPSMVSFTDN-DVYVGyesvELAD----SNPQNTIYDAKRFIGKi 106
Cdd:PRK00290 3 KIIGIDLGTTNSCVAVM-EG-GEPKVIENAEGARTTPSVVAFTKDgERLVG----QPAKrqavTNPENTIFSIKRLMGR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 107 fTAEELEAEIGRYPFKVLN-KNGMVEFSVTSNEtitVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNS 185
Cdd:PRK00290 76 -RDEEVQKDIKLVPYKIVKaDNGDAWVEIDGKK---YTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 186 TIEAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQ 265
Cdd:PRK00290 152 TKDAGKIAGLEVLRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIID 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 266 YLYKQIYQTYGFVPSR-KEEIHRLRQAVEMVKLNLTLHQSAQLSVlltveeqdrkePH-SSDTELPKdklssaddHrvns 343
Cdd:PRK00290 232 YLADEFKKENGIDLRKdKMALQRLKEAAEKAKIELSSAQQTEINL-----------PFiTADASGPK--------H---- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 344 gfgrglsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFG 423
Cdd:PRK00290 289 -----------------LEIKLTRAKFEELTEDLVERTIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFG 351
|
410 420
....*....|....*....|....*.
gi 48928056 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 |
6.03e-101 |
|
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: 306.04 E-value: 6.03e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYcSVGVFFPGTGKVKVIPDENGHISIPSMVSFTDND-VYVGYESVELADSNPQNTIYDAKRFIGKiftaeel 112
Cdd:cd24029 1 VGIDLGTTN-SAVAYWDGNGAEVIIENSEGKRTTPSVVYFDKDGeVLVGEEAKNQALLDPENTIYSVKRLMGR------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 eaeigrypfkvlnkngmVEFSVTSNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANL 192
Cdd:cd24029 73 -----------------DTKDKEEIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 193 AGLKILRVINEPTAAAMAYGLHKADVFH-VLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQI 271
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDGtILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 272 YQTYGFVPSRKEEI--HRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDrkephssdtelpkdklssaddhrvnsgfgrgl 349
Cdd:cd24029 216 GIETGILDDKEDERarARLREAAEEAKIELSSSDSTDILILDDGKGGE-------------------------------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 350 sdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTS 429
Cdd:cd24029 264 -----------LEIEITREEFEELIAPLIERTIDLLEKALKDAKLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISS 332
|
410
....*....|....*..
gi 48928056 430 VDPDLAVVTGVAIQAGI 446
Cdd:cd24029 333 VDPDEAVAKGAAIYAAS 349
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
32-449 |
4.48e-99 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 310.92 E-value: 4.48e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 32 KVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DNDVYVGYESVELADSNPQNTIYDAKRFIGKIFtaE 110
Cdd:PRK13411 3 KVIGIDLGTTNSCVAVL--EGGKPIVIPNSEGGRTTPSIVGFGkSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRW--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAEIGRYPFK-VLNKNGMVEFSVTSNetiTVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEA 189
Cdd:PRK13411 79 DTEEERSRVPYTcVKGRDDTVNVQIRGR---NYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 190 ANLAGLKILRVINEPTAAAMAYGLHKADVFH-VLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLY 268
Cdd:PRK13411 156 GTIAGLEVLRIINEPTAAALAYGLDKQDQEQlILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 269 KQIYQTYGFVPSR-KEEIHRLRQAVEMVKLnltlhqsaQLSVLLTveeqdrkephsSDTELPkdkLSSADDhrvnsgfgr 347
Cdd:PRK13411 236 ENFQQQEGIDLSQdKMALQRLREAAEKAKI--------ELSSMLT-----------TSINLP---FITADE--------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 348 glSDKKSgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFF-GKDP 426
Cdd:PRK13411 285 --TGPKH------LEMELTRAKFEELTKDLVEATIEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQP 356
|
410 420
....*....|....*....|...
gi 48928056 427 NTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:PRK13411 357 DRSVNPDEAVALGAAIQAGVLGG 379
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
34-458 |
7.11e-98 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 307.88 E-value: 7.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEELE 113
Cdd:PTZ00009 7 IGIDLGTTYSCVGVW--KNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDSVVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 114 AEIGRYPFKVLNKNG---MVEFSVtSNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAA 190
Cdd:PTZ00009 85 SDMKHWPFKVTTGGDdkpMIEVTY-QGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 191 NLAGLKILRVINEPTAAAMAYGLHKADV--FHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYL- 267
Cdd:PTZ00009 164 TIAGLNVLRIINEPTAAAIAYGLDKKGDgeKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCv 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 268 --YKQIYQTYGfVPSRKEEIHRLRQAVEMVKlnLTLHQSAQLSVLLtveeqdrkephssdtelpkDKLSSADDhrvnsgf 345
Cdd:PTZ00009 244 qdFKRKNRGKD-LSSNQRALRRLRTQCERAK--RTLSSSTQATIEI-------------------DSLFEGID------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 346 grglsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFF-GK 424
Cdd:PTZ00009 295 ---------------YNVTISRARFEELCGDYFRNTLQPVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGK 359
|
410 420 430
....*....|....*....|....*....|....
gi 48928056 425 DPNTSVDPDLAVVTGVAIQAGIDGGSWPLQVSAL 458
Cdd:PTZ00009 360 EPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDL 393
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
33-446 |
1.46e-97 |
|
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: 298.41 E-value: 1.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFfpgTGKV-KVIPDENGHISIPSMVSFT-DNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAE 110
Cdd:cd11733 3 VIGIDLGTTNSCVAVM---EGKTpKVIENAEGARTTPSVVAFTaDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAEIGRYPFKVLN-KNGMVEFSVTSNEtitVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEA 189
Cdd:cd11733 80 EVQKDIKMVPYKIVKaSNGDAWVEAHGKK---YSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 190 ANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYK 269
Cdd:cd11733 157 GQIAGLNVLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 270 QIYQTYGF-VPSRKEEIHRLRQAVEMVKLNLTlhQSAQLSVLLtveeqdrkePH-SSDTELPKdklssaddHrvnsgfgr 347
Cdd:cd11733 237 EFKKEQGIdLSKDNLALQRLREAAEKAKIELS--SSLQTDINL---------PFiTADASGPK--------H-------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 348 glsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPN 427
Cdd:cd11733 290 -------------LNMKLTRAKFESLVGDLIKRTVEPCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPS 356
|
410
....*....|....*....
gi 48928056 428 TSVDPDLAVVTGVAIQAGI 446
Cdd:cd11733 357 KGVNPDEAVAMGAAIQGGV 375
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
32-449 |
8.43e-94 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 297.69 E-value: 8.43e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 32 KVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFT-DNDVYVGYESVELADSNPQNTIYDAKRFIGKIFtaE 110
Cdd:PRK13410 3 RIVGIDLGTTNSVVAVM--EGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRY--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAEIGRYPFKV-LNKNGMVEFS--VTSNEtitVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTI 187
Cdd:PRK13410 79 ELDPESKRVPYTIrRNEQGNVRIKcpRLERE---FAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 188 EAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYL 267
Cdd:PRK13410 156 DAGRIAGLEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 268 YKQIYQTYGfVPSRKEE--IHRLRQAVEMVKLnltlhqsaQLSVLLTveeqdrkephsSDTELPkdklssaddhrvnsgF 345
Cdd:PRK13410 236 AEQFLEKEG-IDLRRDRqaLQRLTEAAEKAKI--------ELSGVSV-----------TDISLP---------------F 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 346 grgLSDKKSGESQVlfETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKD 425
Cdd:PRK13410 281 ---ITATEDGPKHI--ETRLDRKQFESLCGDLLDRLLRPVKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPRE 355
|
410 420
....*....|....*....|....
gi 48928056 426 PNTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:PRK13410 356 PNQNVNPDEVVAVGAAIQAGILAG 379
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
32-449 |
1.29e-92 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 293.17 E-value: 1.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 32 KVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDN-DVYVGYESVELADSNPQNTIYDAKRFIGKIFtaE 110
Cdd:CHL00094 3 KVVGIDLGTTNSVVAVM--EGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKF--S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAEIGRYPFKVL---NKNGMVEFSVTSNEtitVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTI 187
Cdd:CHL00094 79 EISEEAKQVSYKVKtdsNGNIKIECPALNKD---FSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 188 EAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYL 267
Cdd:CHL00094 156 DAGKIAGLEVLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 268 YKQIYQTYGF-VPSRKEEIHRLRQAVEMVKLNLTlhqsaqlsvllTVEEQDRKEPH-SSDTELPKdklssaddHrvnsgf 345
Cdd:CHL00094 236 IKEFKKKEGIdLSKDRQALQRLTEAAEKAKIELS-----------NLTQTEINLPFiTATQTGPK--------H------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 346 grglsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKD 425
Cdd:CHL00094 291 ---------------IEKTLTRAKFEELCSDLINRCRIPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKK 355
|
410 420
....*....|....*....|....
gi 48928056 426 PNTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:CHL00094 356 PNQSVNPDEVVAIGAAVQAGVLAG 379
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
34-449 |
1.55e-92 |
|
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: 284.14 E-value: 1.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDND-VYVGYESVELADSNPQNTIYDAKRFIG-------- 104
Cdd:cd10235 1 IGIDLGTTNSLVAVW--RDGGAELIPNALGEYLTPSVVSVDEDGsILVGRAAKERLVTHPDRTAASFKRFMGtdkqyrlg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 105 -KIFTAEELeaeigrypfkvlnkngmvefsvtsnetitvspeyvgSRLLLK-LKEMAEAYLGMPVANAVISVPAEFDLKQ 182
Cdd:cd10235 79 nHTFRAEEL------------------------------------SALVLKsLKEDAEAYLGEPVTEAVISVPAYFNDEQ 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 183 RNSTIEAANLAGLKILRVINEPTAAAMAYGLHK-ADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQ 261
Cdd:cd10235 123 RKATKDAGELAGLKVERLINEPTAAALAYGLHKrEDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTH 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 262 RLLQYLYKQiYQTYGFVPSRkEEIHRLRQAVEMVKLNLTLHQSAQLSVlltveeqdrkepHSSDTElpkdklssaddhrv 341
Cdd:cd10235 203 ALADYFLKK-HRLDFTSLSP-SELAALRKRAEQAKRQLSSQDSAEIRL------------TYRGEE-------------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 342 nsgfgrglsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEF 421
Cdd:cd10235 255 -------------------LEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAVILVGGATRMPLVRQLIARL 315
|
410 420
....*....|....*....|....*...
gi 48928056 422 FGKDPNTSVDPDLAVVTGVAIQAGIDGG 449
Cdd:cd10235 316 FGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
33-449 |
3.33e-90 |
|
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: 279.33 E-value: 3.33e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFfpgTGKV-KVIPDENGHISIPSMVSFT-DNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAE 110
Cdd:cd11734 3 VIGIDLGTTNSCVAVM---EGKTpRVIENAEGARTTPSVVAFTkDGERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAEIGRYPFKVL-NKNGMVEFSVTSNetiTVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEA 189
Cdd:cd11734 80 EVQRDIKEVPYKIVkHSNGDAWVEARGQ---KYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 190 ANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYK 269
Cdd:cd11734 157 GQIAGLNVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 270 QIYQTYGF-VPSRKEEIHRLRQAVEMVKLNLtlhqSAQLsvlltveeqdrkephSSDTELPkdkLSSADdhrvnsgfgrg 348
Cdd:cd11734 237 EFKKESGIdLSKDRMAIQRIREAAEKAKIEL----SSTL---------------QTDINLP---FITAD----------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 349 lsdkKSGESQVlfETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNT 428
Cdd:cd11734 284 ----ASGPKHI--NMKLTRAQFESLVKPLVDRTVEPCKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSK 357
|
410 420
....*....|....*....|.
gi 48928056 429 SVDPDLAVVTGVAIQAGIDGG 449
Cdd:cd11734 358 GVNPDEAVAIGAAIQGGVLSG 378
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
34-446 |
5.02e-90 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 286.30 E-value: 5.02e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVFFpgTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKifTAEELE 113
Cdd:PRK05183 22 VGIDLGTTNSLVATVR--SGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGR--SLADIQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 114 AEIGRYPFK-VLNKNGMVEFSVTSNEtitVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANL 192
Cdd:PRK05183 98 QRYPHLPYQfVASENGMPLIRTAQGL---KSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 193 AGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYKQiy 272
Cdd:PRK05183 175 AGLNVLRLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQ-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 273 qtygfvpsrkeeihrlrqavemvkLNLTLHQSAQLSVLLTVEEQDRKEphssdtelpkdKLSSADDHRVNSgfgrglsdk 352
Cdd:PRK05183 253 ------------------------AGLSPRLDPEDQRLLLDAARAAKE-----------ALSDADSVEVSV--------- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 353 ksgesqVLFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVDP 432
Cdd:PRK05183 289 ------ALWQGEITREQFNALIAPLVKRTLLACRRALRDAGVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDP 362
|
410
....*....|....
gi 48928056 433 DLAVVTGVAIQAGI 446
Cdd:PRK05183 363 DKVVAIGAAIQADI 376
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
33-446 |
8.92e-89 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 284.41 E-value: 8.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFFPGTGKVkvIPDENGHISIPSMVSFT-DNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEE 111
Cdd:PTZ00400 43 IVGIDLGTTNSCVAIMEGSQPKV--IENSEGMRTTPSVVAFTeDGQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 112 LEAEIGRYPFKVL---NKNGMVEfsvTSNETitVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIE 188
Cdd:PTZ00400 121 TKKEQKILPYKIVrasNGDAWIE---AQGKK--YSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 189 AANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLY 268
Cdd:PTZ00400 196 AGKIAGLDVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 269 KQIYQTYGFVPSR-KEEIHRLRQAVEMVKLnltlhqsaqlsvlltveeqdrkephssdtelpkdKLSSADDHRVNSGFgr 347
Cdd:PTZ00400 276 AEFKKQQGIDLKKdKLALQRLREAAETAKI----------------------------------ELSSKTQTEINLPF-- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 348 gLSDKKSGESQVLFetEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPN 427
Cdd:PTZ00400 320 -ITADQSGPKHLQI--KLSRAKLEELTHDLLKKTIEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPS 396
|
410
....*....|....*....
gi 48928056 428 TSVDPDLAVVTGVAIQAGI 446
Cdd:PTZ00400 397 KGVNPDEAVAMGAAIQAGV 415
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
7-446 |
3.96e-84 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 271.94 E-value: 3.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 7 ILGSAVLTlllAGYLAQQYLPLPTPKVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVE 86
Cdd:PTZ00186 6 VCGSAAAS---AARLARHESQKVQGDVIGVDLGTTYSCVATM--DGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 87 LADSNPQNTIYDAKRFIGKIFTAEELEAEIGRYPFKVLnKNGMVEFSVTSNETITVSPEYVGSRLLLKLKEMAEAYLGMP 166
Cdd:PTZ00186 81 QAITNPQSTFYAVKRLIGRRFEDEHIQKDIKNVPYKIV-RAGNGDAWVQDGNGKQYSPSQIGAFVLEKMKETAENFLGHK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 167 VANAVISVPAEFDLKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTR 246
Cdd:PTZ00186 160 VSNAVVTCPAYFNDAQRQATKDAGTIAGLNVIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAGGVFEVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 247 AMSGNNKLGGQDFNQRLLQYLYKQIYQTYGFVPSRKE-EIHRLRQAVEMVKLnltlhqsaqlsvlltveeqdrkephssd 325
Cdd:PTZ00186 240 ATNGDTHLGGEDFDLALSDYILEEFRKTSGIDLSKERmALQRVREAAEKAKC---------------------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 326 telpkdKLSSADDHRVNSGFgrgLSDKKSGESQVlfETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLV 405
Cdd:PTZ00186 292 ------ELSSAMETEVNLPF---ITANADGAQHI--QMHISRSKFEGITQRLIERSIAPCKQCMKDAGVELKEINDVVLV 360
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 48928056 406 GGSTRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAIQAGI 446
Cdd:PTZ00186 361 GGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGV 401
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
33-446 |
1.02e-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: 254.86 E-value: 1.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEEL 112
Cdd:cd10238 2 AFGVHFGNTNACVAVY--KDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 EAEIGRYPFKVLNKNGMVEFSVTSNETI-TVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAAN 191
Cdd:cd10238 80 QELKKESKCKIIEKDGKPGYEIELEEKKkLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 192 LAGLKILRVINEPTAAAMAYGL---HKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYL- 267
Cdd:cd10238 160 KAGFNVLRVISEPSAAALAYGIgqdDPTENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLa 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 268 ------YKQIyqtygfVPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVlltveeqdrkephssdtelpkDKLSSADDhrv 341
Cdd:cd10238 240 sefkrqWKQD------VRENKRAMAKLMNAAEVCKHVLSTLNTATCSV---------------------ESLYDGMD--- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 342 nsgfgrglsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEF 421
Cdd:cd10238 290 -------------------FQCNVSRARFESLCSSLFQQCLEPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDL 350
|
410 420
....*....|....*....|....*.
gi 48928056 422 F-GKDPNTSVDPDLAVVTGVAIQAGI 446
Cdd:cd10238 351 FpSAEVLSSIPPDEVIAIGAAKQAGL 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 |
2.35e-79 |
|
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: 251.32 E-value: 2.35e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEELE 113
Cdd:cd11732 1 VGIDFGNQNSVVAA--ARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 114 AEIGRYPFK-VLNKNGMVEFSVT-SNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAAN 191
Cdd:cd11732 79 KEIKLLPFKlVELEDGKVGIEVSyNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 192 LAGLKILRVINEPTAAAMAYGLHKADVF-------HVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLL 264
Cdd:cd11732 159 IAGLNCLRLINETTAAALDYGIYKSDLLeseekprIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 265 QYLYKQIYQTYGFVP-SRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDrkephssdtelpkdklssaddhrvns 343
Cdd:cd11732 239 EHFAEEFKKKYKIDPlENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDID-------------------------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 344 gfgrglsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFG 423
Cdd:cd11732 293 -----------------FSGQIKREEFEELIQPLLARLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFG 355
|
410 420
....*....|....*....|.
gi 48928056 424 KDPNTSVDPDLAVVTGVAIQA 444
Cdd:cd11732 356 KDLSTTLNADEAVARGCALQA 376
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
32-449 |
4.84e-76 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 251.31 E-value: 4.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 32 KVIGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDN-DVYVGYESVELADSNPQNTIYDAKRFIGKifTAE 110
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAM--EGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGR--KMS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAEIGRYPFKVL-NKNGMVEFSvTSNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEA 189
Cdd:PLN03184 116 EVDEESKQVSYRVVrDENGNVKLD-CPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 190 ANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLYK 269
Cdd:PLN03184 195 GRIAGLEVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLAS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 270 QIYQTYGF-VPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDRkephssdtelPKdklssaddHrvnsgfgrg 348
Cdd:PLN03184 275 NFKKDEGIdLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADG----------PK--------H--------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 349 lsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNT 428
Cdd:PLN03184 328 ------------IDTTLTRAKFEELCSDLLDRCKTPVENALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNV 395
|
410 420
....*....|....*....|.
gi 48928056 429 SVDPDLAVVTGVAIQAGIDGG 449
Cdd:PLN03184 396 TVNPDEVVALGAAVQAGVLAG 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 |
9.03e-75 |
|
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: 239.90 E-value: 9.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEEL 112
Cdd:cd24095 3 VVGIDFGNENCVVAV--ARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 EAEIGRYPFKVLN-KNGMVEFSVT-SNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAA 190
Cdd:cd24095 81 QRDLKLFPFKVTEgPDGEIGINVNyLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 191 NLAGLKILRVINEPTAAAMAYGLHKADVF-----HVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQ 265
Cdd:cd24095 161 QIAGLNCLRLMNETTATALAYGIYKTDLPetdptNVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 266 YLYKQIYQTYGF-VPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSVLLTVEEQDrkephssdtelpkdklssaddhrvnsg 344
Cdd:cd24095 241 HFAAEFKEKYKIdVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKD--------------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 345 fgrglsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGK 424
Cdd:cd24095 294 ----------------VKGMITREEFEELAAPLLERLLEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGK 357
|
410
....*....|....*....
gi 48928056 425 DPNTSVDPDLAVVTGVAIQ 443
Cdd:cd24095 358 EPSRTMNASECVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
34-444 |
5.19e-71 |
|
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: 229.85 E-value: 5.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEELE 113
Cdd:cd10228 1 VGFDFGNLSCYIAV--ARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 114 AEIGRYPFKVLN-KNGMVEFSVT-SNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAAN 191
Cdd:cd10228 79 KELKHLPYKVVKlPNGSVGIKVQyLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 192 LAGLKILRVINEPTAAAMAYGLHKADVF-------HVLVIDLGGGTLDVSL--LNKQGGMFLTRAMSGNnkLGGQDFNQR 262
Cdd:cd10228 159 IAGLNCLRLLNDTTAVALAYGIYKQDLPaeeekprNVVFVDMGHSSLQVSVcaFNKGKLKVLATAADPN--LGGRDFDEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 263 LLQYLYKQIYQTYGF-VPSRKEEIHRLRQAVEMVKlnltlhqsaqlsvlltveeqdrKEPHSSDTELPKDKLSSADDHRV 341
Cdd:cd10228 237 LVEHFAEEFKTKYKIdVKSKPRALLRLLTECEKLK----------------------KLMSANATELPLNIECFMDDKDV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 342 nSGFgrglsdkksgesqvlfeteISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEF 421
Cdd:cd10228 295 -SGK-------------------MKRAEFEELCAPLFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKV 354
|
410 420
....*....|....*....|...
gi 48928056 422 FGKDPNTSVDPDLAVVTGVAIQA 444
Cdd:cd10228 355 FGKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
33-446 |
7.11e-64 |
|
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: 210.30 E-value: 7.11e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGvFFPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGK-IFTAEE 111
Cdd:cd10232 2 VIGISFGNSNSSIA-IINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLGTtTLTVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 112 leaeigrypfkvlnkngmvefsvtsnetitvspeyVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAAN 191
Cdd:cd10232 81 -----------------------------------VTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 192 LAGLKILRVINEPTAAAMAYGLHKADVFH------VLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQ 265
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGDtikdktVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 266 YLYKQIYQTYGFVPSR-KEEIHRLRQAVEMVKLNLTLHQSAQLSVlltveeqdrkephssdtelpkDKLSSADDhrvnsg 344
Cdd:cd10232 206 HFAKEFKKKTKTDPRKnARSLAKLRNAAEITKRALSQGTSAPCSV---------------------ESLADGID------ 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 345 fgrglsdkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGK 424
Cdd:cd10232 259 ----------------FHSSINRTRYELLASKVFQQFADLVTDAIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPE 322
|
410 420
....*....|....*....|....*.
gi 48928056 425 D----PNTSVDPDLAVVTGVAIQAGI 446
Cdd:cd10232 323 StiirAPTQINPDELIARGAALQASL 348
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
33-444 |
4.45e-62 |
|
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: 205.81 E-value: 4.45e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVFFPGTgKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGkiFTAEEL 112
Cdd:cd10230 2 VLGIDLGSEFIKVALVKPGV-PFEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG--YSVEEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 eaeigrypfkvlnkNGMVefsvtsnetitvspeyvgsrlLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANL 192
Cdd:cd10230 79 --------------VAMI---------------------LEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 193 AGLKILRVINEPTAAAMAYGLHKA----DVFHVLVIDLGGGTLDVSLL------------NKQGGMFLTRAMSGNNKLGG 256
Cdd:cd10230 124 AGLNVLSLINDNTAAALNYGIDRRfennEPQNVLFYDMGASSTSATVVefssvkekdkgkNKTVPQVEVLGVGWDRTLGG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 257 QDFNQRLLQYLYKQIYQTYGF---VPSRKEEIHRLRQAVEMVKLNLtlhqSAQLSVLLTVEeqdrkephssdtelpkdkl 333
Cdd:cd10230 204 LEFDLRLADHLADEFNEKHKKdkdVRTNPRAMAKLLKEANRVKEVL----SANTEAPASIE------------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 334 SSADDHrvnsgfgrglsDkksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPR 413
Cdd:cd10230 261 SLYDDI-----------D---------FRTKITREEFEELCADLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPK 320
|
410 420 430
....*....|....*....|....*....|..
gi 48928056 414 IRQVIQEFFGKDP-NTSVDPDLAVVTGVAIQA 444
Cdd:cd10230 321 VQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
34-446 |
3.39e-59 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and similar proteins; The subgroup includes two Saccharomyces cerevisiae heat shock protein homologs, Sse1 and Sse2. They may have calcium-dependent calmodulin-binding activities. Both Sse1 and Sse2 belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466944 [Multi-domain] Cd Length: 385 Bit Score: 199.14 E-value: 3.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEELE 113
Cdd:cd24094 1 VGLDLGNLNSVIAV--ARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 114 AEIGRYPFKVLNKNGMVEFSVT-SNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANL 192
Cdd:cd24094 79 EEEKYFTAKLVDANGEVGAEVNyLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 193 AGLKILRVINEPTAAAMAYGLHKADV-------FHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQ 265
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKTDLpepeekpRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 266 YLYKQIYQTYGF-VPSRKEEIHRLRQAVEMVKLNLTLHQSAQLSvlltVEeqdrkephssdtelpkdklSSADDHRVNSg 344
Cdd:cd24094 239 HFADEFKEKYKIdVRSNPKAYFRLLAAAEKLKKVLSANAQAPLN----VE-------------------SLMNDIDVSS- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 345 fgrglsdkksgesqvlfetEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFFGK 424
Cdd:cd24094 295 -------------------MLKREEFEELIAPLLERVTAPLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGK 355
|
410 420
....*....|....*....|..
gi 48928056 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 |
1.82e-55 |
|
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: 189.38 E-value: 1.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEEL 112
Cdd:cd11737 2 VVGFDLGFQSCYVAV--ARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 EAEIGRYPFKVLN-KNGMVEFSVT-SNETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAA 190
Cdd:cd11737 80 QAEKPSLAYELVQlPTGTTGIKVMyMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 191 NLAGLKILRVINEPTAAAMAYGLHKADV-------FHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRL 263
Cdd:cd11737 160 QIAGLNCLRLMNETTAVALAYGIYKQDLpapeekpRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 264 LQYLYKQIYQTYGF-VPSRKEEIHRLRQAVEMVKlnltlhqsaqlsvlltveeqdrKEPHSSDTELPKDKLSSADDHRVN 342
Cdd:cd11737 240 VNHFCEEFGKKYKLdIKSKIRALLRLFQECEKLK----------------------KLMSANASDLPLNIECFMNDIDVS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 343 SGFGRGlsdkksgesqvlfeteisrkLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFF 422
Cdd:cd11737 298 GTMNRG--------------------QFEEMCADLLARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF 357
|
410 420
....*....|....*....|....
gi 48928056 423 GKDPNTSVDPDLAVVTGVAIQAGI 446
Cdd:cd11737 358 GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
33-443 |
2.60e-50 |
|
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: 175.43 E-value: 2.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEEL 112
Cdd:cd11739 2 VVGFDVGFQNCYIAV--ARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 EAEIGRYPFK-VLNKNGMVEFSVTS-NETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAA 190
Cdd:cd11739 80 QKEKENLSYDlVPLKNGGVGVKVMYlDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 191 NLAGLKILRVINEPTAAAMAYGLHKADVFH-------VLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRL 263
Cdd:cd11739 160 QIVGLNCLRLMNDMTAVALNYGIYKQDLPApdekpriVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 264 LQYLYKQIYQTYGF-VPSRKEEIHRLRQAVEMVKlnltlhqsaqlsvlltveeqdrKEPHSSDTELPKDKLSSADDHRVN 342
Cdd:cd11739 240 VEHFCAEFKTKYKLdVKSKIRALLRLYQECEKLK----------------------KLMSSNSTDLPLNIECFMNDKDVS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 343 sgfGRglsdkksgesqvlfeteISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEFF 422
Cdd:cd11739 298 ---GK-----------------MNRSQFEELCADLLQRIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF 357
|
410 420
....*....|....*....|.
gi 48928056 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 |
6.62e-49 |
|
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: 172.02 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGYESVELADSNPQNTIYDAKRFIGKIFTAEEL 112
Cdd:cd11738 2 VVGIDVGFQNCYIAV--ARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 113 EAEIGRYPFKvLNK--NGMVEFSVTS-NETITVSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEA 189
Cdd:cd11738 80 QAEKIKLPYE-LQKmpNGSTGVKVRYlDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 190 ANLAGLKILRVINEPTAAAMAYGLHKADV-------FHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQR 262
Cdd:cd11738 159 AQIAGLNCLRLMNETTAVALAYGIYKQDLpaleekpRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 263 LLQYLYKQIYQTYgfvpsrkeeihrlrqavemvKLNLTLHQSAQLSvlLTVE-EQDRKEPHSSDTELPKDKLSSADDHRV 341
Cdd:cd11738 239 LVDYFCEEFKTKY--------------------KLNVKENIRALLR--LYQEcEKLKKLMSANASDLPLNIECFMNDIDV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 342 NSgfgrglsdkksgesqvlfetEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKTEIDEVVLVGGSTRIPRIRQVIQEF 421
Cdd:cd11738 297 SS--------------------KMNRAQFEELCASLLARVEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKF 356
|
410 420
....*....|....*....|....*
gi 48928056 422 FGKDPNTSVDPDLAVVTGVAIQAGI 446
Cdd:cd11738 357 FGKDISTTLNADEAVARGCALQCAI 381
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
33-444 |
1.12e-48 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 175.81 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVGVffPGTGKVKVIPDENGHISIPSMVSFTDNDVYVGyesveladSNpqNTIYDAKRFIGK----IFT 108
Cdd:PRK01433 21 AVGIDFGTTNSLIAI--ATNRKVKVIKSIDDKELIPTTIDFTSNNFTIG--------NN--KGLRSIKRLFGKtlkeILN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 109 AEELEAEIGRYpfkvLNKNGMVEFSVTSNETItvSPEYVGSRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIE 188
Cdd:PRK01433 89 TPALFSLVKDY----LDVNSSELKLNFANKQL--RIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 189 AANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGGMFLTRAMSGNNKLGGQDFNQRLLQYLY 268
Cdd:PRK01433 163 AAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 269 KqiyqtygfvpsrkeeihrlrqavemvKLNLtlhqsaqlsvlltveeqdrkePHSSDT-ELPKdklsSADDHrvnsgfgr 347
Cdd:PRK01433 243 N--------------------------KFDL---------------------PNSIDTlQLAK----KAKET-------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 348 gLSDKKSGESQVLfetEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEKteIDEVVLVGGSTRIPRIRQVIQEFFGKDPN 427
Cdd:PRK01433 264 -LTYKDSFNNDNI---SINKQTLEQLILPLVERTINIAQECLEQAGNPN--IDGVILVGGATRIPLIKDELYKAFKVDIL 337
|
410
....*....|....*..
gi 48928056 428 TSVDPDLAVVTGVAIQA 444
Cdd:PRK01433 338 SDIDPDKAVVWGAALQA 354
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
34-442 |
8.34e-47 |
|
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: 164.97 E-value: 8.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVFFPGTGKVKVI-------PDENGHISIPSMVsftdnDVYVgyesveladsnpqntiydakRFIGKI 106
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLVvlqlpwpGGDGGSSKVPSVL-----EVVA--------------------DFLRAL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 107 FtaEELEAEIGRYPFKVLNKNgmVEFsvtsnetitvspeyvgsrlllklkemaeaylgmpvanaVISVPAEFDLKQRNST 186
Cdd:cd10170 56 L--EHAKAELGDRIWELEKAP--IEV--------------------------------------VITVPAGWSDAAREAL 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 187 IEAANLAGLK----ILRVINEPTAAAMAYGLHKADVFH------VLVIDLGGGTLDVSLLNKQGGMFL---TRAMSGNNK 253
Cdd:cd10170 94 REAARAAGFGsdsdNVRLVSEPEAAALYALEDKGDLLPlkpgdvVLVCDAGGGTVDLSLYEVTSGSPLlleEVAPGGGAL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 254 LGGQDFNQRLLQYLYKQIYQTYGFVP-SRKEEIHRLRQAVEmvklnltlhqsaqlsvlltveeqDRKEPHSSDtelpkdk 332
Cdd:cd10170 174 LGGTDIDEAFEKLLREKLGDKGKDLGrSDADALAKLLREFE-----------------------EAKKRFSGG------- 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 333 lsSADDHRVNSGFGRGLSDKksgesqvlFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHLEK--TEIDEVVLVGGSTR 410
Cdd:cd10170 224 --EEDERLVPSLLGGGLPEL--------GLEKGTLLLTEEEIRDLFDPVIDKILELIEEQLEAKsgTPPDAVVLVGGFSR 293
|
410 420 430
....*....|....*....|....*....|....*.
gi 48928056 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 |
7.80e-27 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.
Pssm-ID: 466829 [Multi-domain] Cd Length: 409 Bit Score: 111.60 E-value: 7.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVFFpgTGKVKVIPDENGHISIPSMVSFTDNDVyvgyesveladsnpqntIYDAKRFIGKIFTAEELE 113
Cdd:cd10231 1 IGLDFGTSNSSLAVAD--DGKTDLVPFEGDSPTLPSLLYFPRREE-----------------EGAESIYFGNDAIDAYLN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 114 -AEIGRY---PFKVLNKNGMVE-FSVTSNETITvspEYVGSrLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRN---- 184
Cdd:cd10231 62 dPEEGRLiksVKSFLGSSLFDEtTIFGRRYPFE---DLVAA-ILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEddaq 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 185 --STIE-AANLAGLKILRVINEPTAAAMAY--GLHKADVfhVLVIDLGGGTLDVSLLNKQGGMFLTR----AMSGNnKLG 255
Cdd:cd10231 138 aeSRLRdAARRAGFRNVEFQYEPIAAALDYeqRLDREEL--VLVVDFGGGTSDFSVLRLGPNRTDRRadilATSGV-GIG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 256 GQDFNQRL-----LQYL-YKQIYQTYG---FVP-------SRKEEIHRLRQAVEMVKLNLTLHQSAQ---LSVLLTVeeQ 316
Cdd:cd10231 215 GDDFDRELalkkvMPHLgRGSTYVSGDkglPVPawlyadlSNWHAISLLYTKKTLRLLLDLRRDAADpekIERLLSL--V 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 317 DRKEPHS--SDTELPKDKLSSADDHRVN-SGFGRGLsdkksgesqvlfETEISRKLFDTLNEDLFQKILVPIQQVLKEGH 393
Cdd:cd10231 293 EDQLGHRlfRAVEQAKIALSSADEATLSfDFIEISI------------KVTITRDEFETAIAFPLARILEALERTLNDAG 360
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 48928056 394 LEKTEIDEVVLVGGSTRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVA 441
Cdd:cd10231 361 VKPSDVDRVFLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
33-442 |
3.35e-16 |
|
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: 80.01 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 33 VIGIDLGTTYCSVG-VFFPGTGKVKVI----PDENGHIS--IPSMVSFTDNDVYV--GYESVELADSNpQNTIYDAKRFI 103
Cdd:cd10229 2 VVAIDFGTTYSGYAySFITDPGDIHTMynwwGAPTGVSSpkTPTCLLLNPDGEFHsfGYEAREKYSDL-AEDEEHQWLYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 104 GKIFTAEELEAEIGRyPFKVLNKNGMvefSVTSNETITVSPEYVGSRLLLKLKEMAEAYLgmPVANA--VISVPAEFDLK 181
Cdd:cd10229 81 FKFKMMLLSEKELTR-DTKVKAVNGK---SMPALEVFAEALRYLKDHALKELRDRSGSSL--DEDDIrwVLTVPAIWSDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 182 QRNSTIEAANLAGLKI------LRVINEPTAAAMAYGLHKA----------DVFhvLVIDLGGGTLDVS---LLNKQGGM 242
Cdd:cd10229 155 AKQFMREAAVKAGLISeenseqLIIALEPEAAALYCQKLLAegeekelkpgDKY--LVVDCGGGTVDITvheVLEDGKLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 243 FLTRAmSGNNkLGGQDFNQRLLQYLYK----QIYQtyGFVPSRKEEIHRLRQAVEMVKLNLTLhqsaqlsvlltveeqdr 318
Cdd:cd10229 233 ELLKA-SGGP-WGSTSVDEEFEELLEEifgdDFME--AFKQKYPSDYLDLLQAFERKKRSFKL----------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 319 kephssdtELPKDKLssaddhrvnsgfgrglsdkksgesqvlfeteisRKLFDtlneDLFQKILVPIQQVLKEGHLEKte 398
Cdd:cd10229 292 --------RLSPELM---------------------------------KSLFD----PVVKKIIEHIKELLEKPELKG-- 324
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 48928056 399 IDEVVLVGGSTRIPRIRQVIQEFFGKDPN--TSVDPDLAVVTGVAI 442
Cdd:cd10229 325 VDYIFLVGGFAESPYLQKAVKEAFSTKVKiiIPPEPGLAVVKGAVL 370
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
34-270 |
2.07e-14 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 74.05 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVffPGTGKVkvipdenghISIPSMVSFTDND---VYVGYEsveladsnpqntiydAKRFIGKifTAE 110
Cdd:cd10225 2 IGIDLGTANTLVYV--KGKGIV---------LNEPSVVAVDKNTgkvLAVGEE---------------AKKMLGR--TPG 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAEigrYPFKvlnkNG-MVEFSVTsnetitvspeyvgsRLLLK-LKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIE 188
Cdd:cd10225 54 NIVAI---RPLR----DGvIADFEAT--------------EAMLRyFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKE 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 189 AANLAGLKILRVINEPTAAAMAYGLhkaDVFH---VLVIDLGGGTLDVSLLNkQGGMFLTRAMsgnnKLGGQDFNQRLLQ 265
Cdd:cd10225 113 AAEHAGAREVYLIEEPMAAAIGAGL---PIEEprgSMVVDIGGGTTEIAVIS-LGGIVTSRSV----RVAGDEMDEAIIN 184
|
....*
gi 48928056 266 YLYKQ 270
Cdd:cd10225 185 YVRRK 189
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
32-442 |
2.41e-11 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 64.77 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 32 KVIGIDLGTTycSVGVFFPGTGkvkVIPDEnghisiPSMVSF---TDNDVYVGYEsveladsnpqntiydAKRFIGKifT 108
Cdd:PRK13930 9 KDIGIDLGTA--NTLVYVKGKG---IVLNE------PSVVAIdtkTGKVLAVGEE---------------AKEMLGR--T 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 109 AEELEAeIgrYPFKvlnkNGMVE-FSVTSnetitvspeyvgsRLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTI 187
Cdd:PRK13930 61 PGNIEA-I--RPLK----DGVIAdFEATE-------------AMLRYFIKKARGRRFFRKPRIVICVPSGITEVERRAVR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 188 EAANLAGLKILRVINEPTAAAMAYGLhkaDVFHV---LVIDLGGGTLDV---SLlnkqGGMFLTRAMsgnnKLGGQDFNQ 261
Cdd:PRK13930 121 EAAEHAGAREVYLIEEPMAAAIGAGL---PVTEPvgnMVVDIGGGTTEVaviSL----GGIVYSESI----RVAGDEMDE 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 262 RLLQYLykqiyqtygfvpsRKEeiHRLR---QAVEMVKLNLTlhqSAqlsvlLTVEEQDRKEPHSSD--TELPK-DKLSS 335
Cdd:PRK13930 190 AIVQYV-------------RRK--YNLLigeRTAEEIKIEIG---SA-----YPLDEEESMEVRGRDlvTGLPKtIEISS 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 336 AddhrvnsgfgrglsdkksgesqvlfetEISRKLFDTLNEdlfqkILVPIQQVlkeghLEKT--E-----IDE-VVLVGG 407
Cdd:PRK13930 247 E---------------------------EVREALAEPLQQ-----IVEAVKSV-----LEKTppElaadiIDRgIVLTGG 289
|
410 420 430
....*....|....*....|....*....|....*
gi 48928056 408 STRIPRIRQVIQEFFGKDPNTSVDPDLAVVTGVAI 442
Cdd:PRK13930 290 GALLRGLDKLLSEETGLPVHIAEDPLTCVARGTGK 324
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
34-439 |
8.34e-11 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 63.73 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTYCSVGVFfpGTGKVKVIPDENGHISIPSMVSFTDND-----VYVGYESVELADSNPQ--NTIYDAKR----- 101
Cdd:PRK11678 3 IGFDYGTANCSVAVM--RDGKPRLLPLENDSTYLPSTLCAPTREavsewLYRHLDVPAYDDERQAllRRAIRYNReedid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 102 ------FIGKIFTAEELEA-EIGRY---PFKVLNKNGMVEFSVTSNETITVSpeyvgsrLLLKLKEMAEAYLGMPVANAV 171
Cdd:PRK11678 81 vtaqsvFFGLAALAQYLEDpEEVYFvksPKSFLGASGLKPQQVALFEDLVCA-------MMLHIKQQAEAQLQAAITQAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 172 ISVPAEF------DLKQRNSTI--EAANLAGLKILRVINEPTAAAMAY--GLHKADVfhVLVIDLGGGTLDVSLLnKQGG 241
Cdd:PRK11678 154 IGRPVNFqglggeEANRQAEGIleRAAKRAGFKDVEFQFEPVAAGLDFeaTLTEEKR--VLVVDIGGGTTDCSML-LMGP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 242 MFLTR--------AMSGnNKLGGQDFNQRLlqyLYKQIYQTYGF-----------------------VP---------SR 281
Cdd:PRK11678 231 SWRGRadrsasllGHSG-QRIGGNDLDIAL---AFKQLMPLLGMgsetekgialpslpfwnavaindVPaqsdfyslaNG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 282 K--EEIHRLRQAVEMVKLNLTLHQSaQLSVLL--TVEEQdrkephssdtelpKDKLSSADDHRVNSGFgrgLSDkksges 357
Cdd:PRK11678 307 RllNDLIRDAREPEKVARLLKVWRQ-RLSYRLvrSAEEA-------------KIALSDQAETRASLDF---ISD------ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 358 qvLFETEISRKLFDTLNEDLFQKILVPIQQVLKEGHlekTEIDEVVLVGGSTRIPRIRQVIQEFFgkdpntsvdPDLAVV 437
Cdd:PRK11678 364 --GLATEISQQGLEEAISQPLARILELVQLALDQAQ---VKPDVIYLTGGSARSPLIRAALAQQL---------PGIPIV 429
|
..
gi 48928056 438 TG 439
Cdd:PRK11678 430 GG 431
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
123-254 |
5.62e-09 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 56.51 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 123 VLNKNGMV-----EFSVTSNETITVspEYVG-SRLLLKLKEMAEAYLGMPVANAVISVP---AEFDLKQRNSTIEAAnla 193
Cdd:cd24047 16 VVDEEGQPvagalERADVVRDGIVV--DYIGaIRIVRKLKETLEKKLGVELTSAATAFPpgtGERDARAIRNVLEGA--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 48928056 194 GLKILRVINEPTAAAMAYGLHKAdvfhvLVIDLGGGTLDVSLL-NKQ---------GGMFLTRAMSGNNKL 254
Cdd:cd24047 91 GLEVSNVVDEPTAANAVLGIRDG-----AVVDIGGGTTGIAVLkDGKvvytadeptGGTHLSLVLAGNYGI 156
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
144-427 |
1.21e-07 |
|
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: 53.07 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 144 PEYVgSRLLLKLKEMAEAYLGMPVANAVISVPaefdlKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLV 223
Cdd:cd24004 45 ISKV-AESIKELLKELEEKLGSKLKDVVIAIA-----KVVESLLNVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLNIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 224 IDLGGGTLDVSLLNKqGGMFLTRamsgNNKLGGQDFNQRLLQylykqiyqtyGFVPSRKEeihrlrqaVEMVKLNLTLHq 303
Cdd:cd24004 119 VDIGAGTTDIALIRN-GGIEAYR----MVPLGGDDFTKAIAE----------GFLISFEE--------AEKIKRTYGIF- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 304 saqlsvlLTVEEQDRKEPhssdtELPKDKLSSADDHRVNsgfgrglsdkksgesqvlfetEISRKLFDTLnEDLFQKILV 383
Cdd:cd24004 175 -------LLIEAKDQLGF-----TINKKEVYDIIKPVLE---------------------ELASGIANAI-EEYNGKFKL 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 48928056 384 PiqqvlkeghlekteiDEVVLVGGSTRIPRIRQVIQEFFGKDPN 427
Cdd:cd24004 221 P---------------DAVYLVGGGSKLPGLNEALAEKLGLPVE 249
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
146-240 |
2.07e-07 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 52.14 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 146 YVGS-RLLLKLKEMAEAYLGMPVANAVISVPAEFDLKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLHKAdvfhvLVI 224
Cdd:PRK15080 66 FIGAvTIVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG-----AVV 140
|
90
....*....|....*.
gi 48928056 225 DLGGGTLDVSLLnKQG 240
Cdd:PRK15080 141 DIGGGTTGISIL-KDG 155
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
157-270 |
3.41e-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: 51.79 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 157 EMAEAYL-----------GMPVANAVISVPAEFDLKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVID 225
Cdd:pfam06723 72 EVTEAMLkyfikkvhgrrSFSKPRVVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGNMVVD 151
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 48928056 226 LGGGTLDVSLLNkQGGMFLTRAMsgnnKLGGQDFNQRLLQYLYKQ 270
Cdd:pfam06723 152 IGGGTTEVAVIS-LGGIVTSKSV----RVAGDEFDEAIIKYIRKK 191
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
171-270 |
6.37e-07 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 51.06 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 171 VISVPAEFDLKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLhkaDVFHV---LVIDLGGGTLDVSLLNkQGGMFLTRA 247
Cdd:PRK13928 99 MICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGL---DISQPsgnMVVDIGGGTTDIAVLS-LGGIVTSSS 174
|
90 100
....*....|....*....|...
gi 48928056 248 MsgnnKLGGQDFNQRLLQYLYKQ 270
Cdd:PRK13928 175 I----KVAGDKFDEAIIRYIRKK 193
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
34-270 |
1.65e-06 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 50.08 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTTycSVGVFFPGTGKVkvipdenghISIPSMVSF--TDNDVY-VGYEsveladsnpqntiydAKRFIGKifTAE 110
Cdd:COG1077 10 IGIDLGTA--NTLVYVKGKGIV---------LNEPSVVAIdkKTGKVLaVGEE---------------AKEMLGR--TPG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAeigRYPFKvlnkNGmvefsVTSNETITvspeyvgsRLLLKL---KEMAEAYLGMPvaNAVISVPAEFDLKQRNSTI 187
Cdd:COG1077 62 NIVA---IRPLK----DG-----VIADFEVT--------EAMLKYfikKVHGRRSFFRP--RVVICVPSGITEVERRAVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 188 EAANLAGLKILRVINEPTAAAMAYGLhkaDVFH---VLVIDLGGGTLDV---SLlnkqGGMFLTRAMsgnnKLGGQDFNQ 261
Cdd:COG1077 120 DAAEQAGAREVYLIEEPMAAAIGAGL---PIEEptgNMVVDIGGGTTEVaviSL----GGIVVSRSI----RVAGDELDE 188
|
....*....
gi 48928056 262 RLLQYLYKQ 270
Cdd:COG1077 189 AIIQYVRKK 197
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
111-331 |
7.98e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 44.51 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAEIGRYPFKVLN----KNGMV-EFSVTSNetitvspeyvgsrLLLKLKEMAEAYLGMPV--ANAVISVPAEFDLKQR 183
Cdd:PRK13929 48 EAKNMIGKTPGKIVAvrpmKDGVIaDYDMTTD-------------LLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVER 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 184 NSTIEAANLAGLKILRVINEPTAAAMAYGLHKADVFHVLVIDLGGGTLDVSLLNKQGgmfltrAMSGNN-KLGGQDFNQR 262
Cdd:PRK13929 115 RAISDAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTEVAIISFGG------VVSCHSiRIGGDQLDED 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 263 LLQYLYK------------QIYQTYGFVPSRKEEIH---RLRQAVEMVKLNLTLH----QSAQLSVLLTVEEQDRKEPHS 323
Cdd:PRK13929 189 IVSFVRKkynlligertaeQVKMEIGYALIEHEPETmevRGRDLVTGLPKTITLEskeiQGAMRESLLHILEAIRATLED 268
|
....*...
gi 48928056 324 SDTELPKD 331
Cdd:PRK13929 269 CPPELSGD 276
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
34-233 |
8.43e-05 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 44.51 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 34 IGIDLGTtYCSVgvffpgtgkvkvIPDENGH-ISIPSmvsftdndvYVGYesveladsnPQNTIydAKRFIGK--IFTAE 110
Cdd:cd24009 4 IGIDLGT-SRSA------------VVTSRGKrFSFRS---------VVGY---------PKDII--ARKLLGKevLFGDE 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 111 ELEAEIG---RYPFKvlnkNGMVEFSVTSNETITVspEYVgSRLL--LKLKEMAEAYlgmpvanAVISVPAEFDLKQRNS 185
Cdd:cd24009 51 ALENRLAldlRRPLE----DGVIKEGDDRDLEAAR--ELL-QHLIelALPGPDDEIY-------AVIGVPARASAENKQA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 48928056 186 TIEAANLAGLKILrVINEPTAAAmaYGLHKADvfHVLVIDLGGGTLDV 233
Cdd:cd24009 117 LLEIARELVDGVM-VVSEPFAVA--YGLDRLD--NSLIVDIGAGTTDL 159
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
171-270 |
2.63e-04 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 43.15 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 171 VISVPAEFDLKQRNSTIEAANLAGLKILRVINEPTAAAMAYGLhkaDVFH---VLVIDLGGGTLDV---SLlnkqGGMFL 244
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGL---PVTEptgSMVVDIGGGTTEVaviSL----GGIVY 172
|
90 100
....*....|....*....|....*.
gi 48928056 245 TRAMsgnnKLGGQDFNQRLLQYLYKQ 270
Cdd:PRK13927 173 SKSV----RVGGDKFDEAIINYVRRN 194
|
|
| ASKHA_NBD_ParM_R1-like |
cd24022 |
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
221-295 |
7.76e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.
Pssm-ID: 466872 [Multi-domain] Cd Length: 324 Bit Score: 38.41 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48928056 221 VLVIDLGGGTLDVSLLNkqGGMFLTRAMSGNNKLGGQDFNQRLLQYLYK-------------QIYQTYGFVPSRKEEI-- 285
Cdd:cd24022 176 VAVIDIGGTTTDIAVVS--GGLSIDHARSGTIELGVLDVRDALKDALKKrfglssisdaeldRALRTGKFRLNGGKEVdv 253
|
90
....*....|.
gi 48928056 286 -HRLRQAVEMV 295
Cdd:cd24022 254 sDLVNEAIAEV 264
|
|
| |
