|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
1-450 |
0e+00 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 938.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 1 MFIGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLCAPTREAVSEWLYRHHDVPADDDETQALLRRAIRYNREEDID 80
Cdd:PRK11678 1 MFIGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREAVSEWLYRHLDVPAYDDERQALLRRAIRYNREEDID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 81 VTAKSVQFGLSSLAQYIDDPEEVWFVKSPKSFLGASGLKPQQVALFEDLVCAMMLHIRQQAQAQLPEAITQAVIGRPINF 160
Cdd:PRK11678 81 VTAQSVFFGLAALAQYLEDPEEVYFVKSPKSFLGASGLKPQQVALFEDLVCAMMLHIKQQAEAQLQAAITQAVIGRPVNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 161 QGLGGDEANTQAQGILERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLLMGPQWRSRLDREA 240
Cdd:PRK11678 161 QGLGGEEANRQAEGILERAAKRAGFKDVEFQFEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSMLLMGPSWRGRADRSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 241 SLLGHSGCRIGGNDLDIALAFKNLMPLLGMGGETEKGIALPILPWWNAVAINDVPAQSDFYSSANGRLLNDLVRDAREPE 320
Cdd:PRK11678 241 SLLGHSGQRIGGNDLDIALAFKQLMPLLGMGSETEKGIALPSLPFWNAVAINDVPAQSDFYSLANGRLLNDLIRDAREPE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 321 KVALLQKVWRQRLSYRLVRSAEESKIALSSVAETRASLPFISDELATLISQQGLESALSQPLARILEQVQLALDNAQEKP 400
Cdd:PRK11678 321 KVARLLKVWRQRLSYRLVRSAEEAKIALSDQAETRASLDFISDGLATEISQQGLEEAISQPLARILELVQLALDQAQVKP 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446391885 401 DVIYLTGGSARSPLIKKALTEQLPGIPIAGGDDFGSVTAGLARWAEVVFR 450
Cdd:PRK11678 401 DVIYLTGGSARSPLIRAALAQQLPGIPIVGGDDFGSVTAGLARWAQVVFR 450
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
3-443 |
7.79e-174 |
|
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: 492.94 E-value: 7.79e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLCAPTREAVSewlyrhhdvpadddetqallrrairynreedidvt 82
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEG----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 83 AKSVQFGLSSLAQYIDDPEEVWFVKSPKSFLGASGLKPQ----QVALFEDLVCAMMLHIRQQAQAQLPEAITQAVIGRPI 158
Cdd:cd10231 46 AESIYFGNDAIDAYLNDPEEGRLIKSVKSFLGSSLFDETtifgRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 159 NFQGlGGDEANTQAQGILERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLLMGPQWrsrLDR 238
Cdd:cd10231 126 HFSG-VGAEDDAQAESRLRDAARRAGFRNVEFQYEPIAAALDYEQRLDREELVLVVDFGGGTSDFSVLRLGPNR---TDR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 239 EASLLGHSGCRIGGNDLDIALAFKNLMPLLGMGGETEKGIALPILPWWNAVAINDVPAQSDFYSSANGRLLNDLVRDARE 318
Cdd:cd10231 202 RADILATSGVGIGGDDFDRELALKKVMPHLGRGSTYVSGDKGLPVPAWLYADLSNWHAISLLYTKKTLRLLLDLRRDAAD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 319 PEKVALLQKVWRQRLSYRLVRSAEESKIALSSVAETRASLPFISDELATLISQQGLESALSQPLARILEQVQLALDNAQE 398
Cdd:cd10231 282 PEKIERLLSLVEDQLGHRLFRAVEQAKIALSSADEATLSFDFIEISIKVTITRDEFETAIAFPLARILEALERTLNDAGV 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446391885 399 KP---DVIYLTGGSARSPLIKKALTEQLPGIPIAGGDDFGSVTAGLAR 443
Cdd:cd10231 362 KPsdvDRVFLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLAL 409
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
3-449 |
5.83e-70 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 229.32 E-value: 5.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSmlcaptreavsewlyrhhdvpadddetqallrrAIRYNREEDIDVt 82
Cdd:COG0443 2 IGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPS---------------------------------VVAFPKDGEVLV- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 83 aksvqfGLSSLAQYIDDPEevWFVKSPKSFLGaSGLKPQQVAL------FEDLVCAMMLHIRQQAQAQLPEAITQAVIGR 156
Cdd:COG0443 48 ------GEAAKRQAVTNPG--RTIRSIKRLLG-RSLFDEATEVggkrysPEEISALILRKLKADAEAYLGEPVTRAVITV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 157 PINFqglggDEANTQAqgiLERAAKRAGFKDVVFQYEPVAAGLDYEATL-QEEKRVLVVDIGGGTTDCSLLLMGPQwrsR 235
Cdd:COG0443 119 PAYF-----DDAQRQA---TKDAARIAGLEVLRLLNEPTAAALAYGLDKgKEEETILVYDLGGGTFDVSILRLGDG---V 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 236 LDReaslLGHSGC-RIGGNDLDIALAfKNLMPLLGMggetEKGIalpilpwwnavaindvpaqsdfyssangrllnDLVR 314
Cdd:COG0443 188 FEV----LATGGDtHLGGDDFDQALA-DYVAPEFGK----EEGI--------------------------------DLRL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 315 DARepekvALlqkvwrqrlsYRLVRSAEESKIALSSVAETRASLPFISD-ELATLISQQGLESALSQPLARILEQVQLAL 393
Cdd:COG0443 227 DPA-----AL----------QRLREAAEKAKIELSSADEAEINLPFSGGkHLDVELTRAEFEELIAPLVERTLDPVRQAL 291
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446391885 394 DNAQEKP---DVIYLTGGSARSPLIKKALTEQLPGIPIAGGDDFGSVTAGLARWAEVVF 449
Cdd:COG0443 292 ADAGLSPsdiDAVLLVGGSTRMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLA 350
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
91-428 |
4.92e-27 |
|
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: 110.66 E-value: 4.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 91 SSLAQYIDDPEEVWFVKSPKSFLGASGLK---PQQVALFEDLVCAMMLHIRQQAQAQ---LPEAITQAVIGRPINFqglg 164
Cdd:cd10170 10 SGVAYALLGPGEPPLVVLQLPWPGGDGGSskvPSVLEVVADFLRALLEHAKAELGDRiweLEKAPIEVVITVPAGW---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 165 gdeaNTQAQGILERAAKRAGFK----DVVFQYEPVAAGLDY------EATLQEEKRVLVVDIGGGTTDCSLLLMGPQWRS 234
Cdd:cd10170 86 ----SDAAREALREAARAAGFGsdsdNVRLVSEPEAAALYAledkgdLLPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 235 RLDREASllgHSGCRIGGNDLDIALAfknlmpllgmggetekgialpilpwwnavaindvpaqsdfyssangRLLNDLVR 314
Cdd:cd10170 162 LLEEVAP---GGGALLGGTDIDEAFE----------------------------------------------KLLREKLG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 315 DAREPEKVAllqkvwRQRLSYRLVRSAEESKIALSSVAETRASLPFI---------SDELATLISQQGLESALSQPLARI 385
Cdd:cd10170 193 DKGKDLGRS------DADALAKLLREFEEAKKRFSGGEEDERLVPSLlggglpelgLEKGTLLLTEEEIRDLFDPVIDKI 266
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446391885 386 LEQVQLALDNAQ-EKPDVIYLTGGSARSPLIKKALTEQLPGIPI 428
Cdd:cd10170 267 LELIEEQLEAKSgTPPDAVVLVGGFSRSPYLRERLRERFGSAGI 310
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
3-425 |
1.86e-23 |
|
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: 101.43 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLC---------APTREAVSEWLY-----------RHHDVPADDDE 62
Cdd:cd24028 2 IGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAftdgerlvgEAAKNQAASNPEntifdvkrligRKFDDPSVQSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 63 TQALLRRAIRYNREE-DIDVTAKSVQFGLSslaqyiddPEEVwfvkspksflgasglkpqqvalfedlvCAMML-HIRQQ 140
Cdd:cd24028 82 IKHWPFKVVEDEDGKpKIEVTYKGEEKTFS--------PEEI---------------------------SAMILkKLKEI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 141 AQAQLPEAITQAVIGRPINFqglggDEANTQAqgiLERAAKRAGFKdvVFQY--EPVAAGLDY--EATLQEEKRVLVVDI 216
Cdd:cd24028 127 AEAYLGRPVTKAVITVPAYF-----NDAQRQA---TKDAATIAGLN--VLRIinEPTAAALAYglDKKSSGERNVLVFDL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 217 GGGTTDCSLLLMgpqwrsrldreasllghsgcriggndldialaFKNLMPLLGMGGETEKGialpilpwwnavaindvpa 296
Cdd:cd24028 197 GGGTFDVSLLSI--------------------------------DNGVFEVKATAGDTHLG------------------- 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 297 QSDFyssaNGRLLNDLVRDAREPEKVALlqkVWRQRLSYRLVRSAEESKIALSSVAETRASLPFISD--ELATLISQQGL 374
Cdd:cd24028 226 GEDF----DNRLVEYLVEEFKKKHGKDL---RENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDgiDFETTITRAKF 298
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446391885 375 ESaLSQPL-ARILEQVQLALDNAQEKP----DVIyLTGGSARSPLIKKALTEQLPG 425
Cdd:cd24028 299 EE-LCEDLfKKCLEPVEKVLKDAKLSKddidEVV-LVGGSTRIPKIQELLSEFFGG 352
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
3-428 |
1.59e-20 |
|
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: 92.25 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLL-KMENDSTLLPSmlcaptreavsewlyrhhdvpadddetqallrrAIRYNREEDIDV 81
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIiENSEGKRTTPS---------------------------------VVYFDKDGEVLV 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 82 --TAKSvqfglsslaQYIDDPEEVwfVKSPKSFLGASG----------LKPQQVAlfedlvcAMML-HIRQQAQAQLPEA 148
Cdd:cd24029 48 geEAKN---------QALLDPENT--IYSVKRLMGRDTkdkeeiggkeYTPEEIS-------AEILkKLKEDAEEQLGGE 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 149 ITQAVIGRPINFqglgGDEantQAQGILeRAAKRAGFKDVVFQYEPVAAGLDY-EATLQEEKRVLVVDIGGGTTDCSLLl 227
Cdd:cd24029 110 VKGAVITVPAYF----NDK---QRKATK-KAAELAGLNVLRLINEPTAAALAYgLDKEGKDGTILVYDLGGGTFDVSIL- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 228 mgpqwrsRLDREA-SLLGHSG-CRIGGNDLDIALAfkNLMpllgmggETEKGIALPILPwwnavaindvpaqSDFYSSAN 305
Cdd:cd24029 181 -------EIENGKfEVLATGGdNFLGGDDFDEAIA--ELI-------LEKIGIETGILD-------------DKEDERAR 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 306 GRLLNdlvrdarepekvallqkvwrqrlsyrlvrSAEESKIALSSVAETRASLPFISD--ELATLISQQGLESALSQPLA 383
Cdd:cd24029 232 ARLRE-----------------------------AAEEAKIELSSSDSTDILILDDGKggELEIEITREEFEELIAPLIE 282
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446391885 384 RILEQVQLALDNAQEKP---DVIYLTGGSARSPLIKKALTEQLPGIPI 428
Cdd:cd24029 283 RTIDLLEKALKDAKLSPediDRVLLVGGSSRIPLVREMLEEYFGREPI 330
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
3-421 |
5.31e-20 |
|
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: 92.71 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLC-APTREAVSEWLYRHhdVPADDDETQALLRRAI-RYNREEDID 80
Cdd:pfam00012 2 IGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAfTPKERLVGQAAKNQ--AVTNPKNTVFSVKRLIgRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 81 VTAKSVQFGLSSLAQyiDDPE-EVwfvkspkSFLGASgLKPQQVAlfedlvcAMML-HIRQQAQAQLPEAITQAVIGRPI 158
Cdd:pfam00012 80 RDIKHLPYKVVKLPN--GDAGvEV-------RYLGET-FTPEQIS-------AMILqKLKETAEAYLGKPVTDAVITVPA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 159 NFqglggDEAntQAQGILErAAKRAGFKDVVFQYEPVAAGLDY--EATlQEEKRVLVVDIGGGTTDCSLLlmgpqwrsrl 236
Cdd:pfam00012 143 YF-----NDA--QRQATKD-AGQIAGLNVLRIVNEPTAAALAYglDKT-DKERNIAVYDLGGGTFDVSIL---------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 237 dreasllghsgcRIGGNDLDIalafknlmplLGMGGETEKGialpilpwwnavaindvpaQSDFyssaNGRLLNDLVRDA 316
Cdd:pfam00012 204 ------------EIGRGVFEV----------KATNGDTHLG-------------------GEDF----DLRLVDHLAEEF 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 317 REPEKVALL--QKVWRqrlsyRLVRSAEESKIALSSVaETRASLPFIS-----DELATLISQQGLESaLSQPL-ARILEQ 388
Cdd:pfam00012 239 KKKYGIDLSkdKRALQ-----RLREAAEKAKIELSSN-QTNINLPFITamadgKDVSGTLTRAKFEE-LVADLfERTLEP 311
|
410 420 430
....*....|....*....|....*....|....*.
gi 446391885 389 VQLALDNAQEKPDVIY---LTGGSARSPLIKKALTE 421
Cdd:pfam00012 312 VEKALKDAGLSKSEIDevvLVGGSTRIPAVQELVKE 347
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
3-425 |
1.49e-18 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 88.27 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLC-----------APTREAVS---------------EWlyrhhdv 56
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGfgksgdrlvgqLAKRQAVTnaentvysikrfigrRW------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 57 paDDDETQallRRAIRYN----REEDIDVTAKSVQFglsslaqyiddpeevwfvkspksflgasglKPQQVAlfedlvcA 132
Cdd:PRK13411 78 --DDTEEE---RSRVPYTcvkgRDDTVNVQIRGRNY------------------------------TPQEIS-------A 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 133 MMLH-IRQQAQAQLPEAITQAVIGRPINFQglggdEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQ-EEKR 210
Cdd:PRK13411 116 MILQkLKQDAEAYLGEPVTQAVITVPAYFT-----DAQRQAT---KDAGTIAGLEVLRIINEPTAAALAYGLDKQdQEQL 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 211 VLVVDIGGGTTDCSLLLMGpqwrsrlDREASLLGHSG-CRIGGNDLDIAlafknlmpllgmggetekgialpILPWwnav 289
Cdd:PRK13411 188 ILVFDLGGGTFDVSILQLG-------DGVFEVKATAGnNHLGGDDFDNC-----------------------IVDW---- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 290 aindvpaqsdfyssangrllndLVRDAREPEKVALLQ-KVWRQRLSyrlvRSAEESKIALSSVAETRASLPFI-SDE--- 364
Cdd:PRK13411 234 ----------------------LVENFQQQEGIDLSQdKMALQRLR----EAAEKAKIELSSMLTTSINLPFItADEtgp 287
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446391885 365 --LATLISQQGLESALSQPLARILEQVQLALDNAQEKP---DVIYLTGGSARSPLIKKALTEQLPG 425
Cdd:PRK13411 288 khLEMELTRAKFEELTKDLVEATIEPMQQALKDAGLKPediDRVILVGGSTRIPAVQEAIQKFFGG 353
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
3-416 |
1.93e-18 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 88.15 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLC-APTREAVSEWLYRHHDV--PADddeTQALLRRAI--RYNree 77
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGfTKDGELLVGQLARRQLVlnPQN---TFYNLKRFIgrRYD--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 78 DIDVTAKSVQFGLSSlaqyiDDPEEVWfVKSP---KSFlgasglKPqqvalfEDLVCAMMLHIRQQAQAQLPEAITQAVI 154
Cdd:PRK13410 79 ELDPESKRVPYTIRR-----NEQGNVR-IKCPrleREF------AP------EELSAMILRKLADDASRYLGEPVTGAVI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 155 GRPINFqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLLMGpqwRS 234
Cdd:PRK13410 141 TVPAYF-----NDSQRQAT---RDAGRIAGLEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVG---NG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 235 RLDREASllghSG-CRIGGNDLDialafKNLMPLLGMGGETEKGIalpilpwwnavaindvpaqsdfyssangrllnDLV 313
Cdd:PRK13410 210 VFEVKAT----SGdTQLGGNDFD-----KRIVDWLAEQFLEKEGI--------------------------------DLR 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 314 RDarepekvallqkvwRQRLSyRLVRSAEESKIALSSVAETRASLPFISdelATLISQQGLESALSQP---------LAR 384
Cdd:PRK13410 249 RD--------------RQALQ-RLTEAAEKAKIELSGVSVTDISLPFIT---ATEDGPKHIETRLDRKqfeslcgdlLDR 310
|
410 420 430
....*....|....*....|....*....|....*
gi 446391885 385 ILEQVQLALDNAQEKPDVI---YLTGGSARSPLIK 416
Cdd:PRK13410 311 LLRPVKRALKDAGLSPEDIdevVLVGGSTRMPMVQ 345
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
3-421 |
1.38e-17 |
|
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: 83.80 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSmlcaptreavsewlyrhhdvpadddetqallrrAIRYNREEDIDVt 82
Cdd:cd10236 5 VGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPS---------------------------------VVHYGEDGKITV- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 83 aksvqfGLSSLAQYIDDPEEVwfVKSPKSFLGAS--------GLKP-------QQVALFE----DL----VCAMML-HIR 138
Cdd:cd10236 51 ------GEKAKENAITDPENT--ISSVKRLMGRSladvkeelPLLPyrlvgdeNELPRFRtgagNLtpveISAEILkELK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 139 QQAQAQLPEAITQAVIGRPINFqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGG 218
Cdd:cd10236 123 QRAEETLGGELTGAVITVPAYF-----DDAQRQAT---KDAARLAGLNVLRLLNEPTAAALAYGLDQKKEGTIAVYDLGG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 219 GTTDCSLLlmgpqwrsRLDREA----SLLGHSgcRIGGNDLDIALAfknlmpllgmggetekgialpilpwwnavaindv 294
Cdd:cd10236 195 GTFDISIL--------RLSDGVfevlATGGDT--ALGGDDFDHLLA---------------------------------- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 295 paqSDFYSSANgrllndlVRDAREPEKVAllqkvwrqrlsyRLVRSAEESKIALSSVAETRASLPFISDELATLISQQGL 374
Cdd:cd10236 231 ---DWILKQIG-------IDARLDPAVQQ------------ALLQAARRAKEALSDADSASIEVEVEGKDWEREITREEF 288
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446391885 375 ESaLSQPL-ARILEQVQLALDNAQEKPDVI---YLTGGSARSPLIKKALTE 421
Cdd:cd10236 289 EE-LIQPLvKRTLEPCRRALKDAGLEPADIdevVLVGGSTRIPLVRQRVAE 338
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
3-421 |
3.19e-15 |
|
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: 76.75 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLkmEND--STLLPSMLcAPTreavsewlyrhhdvpaDDDET---QALLRRAIRyNREE 77
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVI--PNAegGRTTPSVV-AFT----------------KDGERlvgQPAKRQAVT-NPEN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 78 DI---------DVTAKSVQFGLSSLAQYIDDPEEVWFVKSPKSFlgasglKPQQVAlfedlvcAMML-HIRQQAQAQLPE 147
Cdd:cd10234 62 TIfsikrfmgrRYKEVEVERKQVPYPVVSAGNGDAWVEIGGKEY------TPEEIS-------AFILqKLKKDAEAYLGE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 148 AITQAVIGRPINFqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLL 227
Cdd:cd10234 129 KVTKAVITVPAYF-----NDSQRQAT---KDAGKIAGLEVLRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 228 MGpqwrsrlDREASLLGHSG-CRIGGNDLD------IALAFKNlmpllgmggetEKGIalpilpwwnavaindvpaqsdf 300
Cdd:cd10234 201 IG-------DGVFEVLSTNGdTHLGGDDFDqriidyLADEFKK-----------EEGI---------------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 301 yssangrllnDLVRDarepeKVALlqkvwrQRLSyrlvRSAEESKIALSSVAETRASLPFIS-DE-----LATLISQQGL 374
Cdd:cd10234 241 ----------DLSKD-----KMAL------QRLK----EAAEKAKIELSSVLETEINLPFITaDAsgpkhLEMKLTRAKF 295
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446391885 375 ESaLSQPL-ARILEQVQLALDNAQEKP----DVIyLTGGSARSPLIKKALTE 421
Cdd:cd10234 296 EE-LTEDLvERTIEPVEQALKDAKLSPsdidEVI-LVGGSTRMPAVQELVKE 345
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
141-424 |
7.07e-15 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 76.69 E-value: 7.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 141 AQAQLPEAITQAVIGRPINFQglggdeaNTQAQGILErAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGT 220
Cdd:CHL00094 127 ASKYLGETVTQAVITVPAYFN-------DSQRQATKD-AGKIAGLEVLRIINEPTAASLAYGLDKKNNETILVFDLGGGT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 221 TDCSLLLMGpqwrsrlDREASLLGHSG-CRIGGNDLDialafKNLMPLLGMGGETEKGIalpilpwwnavaindvpaqsd 299
Cdd:CHL00094 199 FDVSILEVG-------DGVFEVLSTSGdTHLGGDDFD-----KKIVNWLIKEFKKKEGI--------------------- 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 300 fyssangrllnDLVRDarepekvallqkvwRQRLSyRLVRSAEESKIALSSVAETRASLPFIS------DELATLISQQG 373
Cdd:CHL00094 246 -----------DLSKD--------------RQALQ-RLTEAAEKAKIELSNLTQTEINLPFITatqtgpKHIEKTLTRAK 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446391885 374 LESALSQPLARILEQVQLALDNAQ---EKPDVIYLTGGSARSPLIK---KALTEQLP 424
Cdd:CHL00094 300 FEELCSDLINRCRIPVENALKDAKldkSDIDEVVLVGGSTRIPAIQelvKKLLGKKP 356
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-421 |
2.56e-13 |
|
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: 71.22 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMR--DGKPQLLKMENDSTLLPSMLCAPTREAVsewLYRHHDVPADDDETQALL---RRAI--RYNR 75
Cdd:cd10237 25 VGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGV---LVGYDALAQAEHNPSNTIydaKRFIgkTFTK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 76 EEdIDVTAKSVQFglsslaqyiddpeEVWFVKSPKSFLGASGLKPQQVALFEDLVCAMMLHIRQQAQAQLPEAITQAVIG 155
Cdd:cd10237 102 EE-LEEEAKRYPF-------------KVVNDNIGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVIS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 156 RPINFqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEA-TLQEEKRVLVVDIGGGTTDCSLLlmgpqwrs 234
Cdd:cd10237 168 VPAEF-----DEKQRNAT---RKAANLAGLEVLRVINEPTAAAMAYGLhKKSDVNNVLVVDLGGGTLDVSLL-------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 235 rldreasllghsgcRI-GGNDLDIALAFKNlmpllGMGGEtekgialpilpwwnavaindvpaqsDFyssaNGRLLNDLV 313
Cdd:cd10237 232 --------------NVqGGMFLTRAMAGNN-----HLGGQ-------------------------DF----NQRLFQYLI 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 314 RDAREPEKVALLQKVWRQRLsyRLvrSAEESKIALSSVAETRASLPFISD-------ELATLISQQGLEsALSQPL-ARI 385
Cdd:cd10237 264 DRIAKKFGKTLTDKEDIQRL--RQ--AVEEVKLNLTNHNSASLSLPLQISlpsafkvKFKEEITRDLFE-TLNEDLfQRV 338
|
410 420 430
....*....|....*....|....*....|....*....
gi 446391885 386 LEQVQLALDNAQ---EKPDVIYLTGGSARSPLIKKALTE 421
Cdd:cd10237 339 LEPIRQVLAEVElgkEDVDEIVLVGGSTRIPRVRQLVRE 377
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-428 |
1.28e-12 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 69.88 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLcAPTREA---VSEWLYRHHDVpaDDDETQALLRRAIRyNREEDI 79
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVV-AYTKNGdrlVGQIAKRQAVV--NPENTFFSVKRFIG-RKMSEV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 80 DVTAKSVQFGLSSlaqyiddpEEVWFVKspksfLGASGLKPQQVAlfEDLVCAMMLHIRQQAQAQLPEAITQAVIGRPIN 159
Cdd:PLN03184 118 DEESKQVSYRVVR--------DENGNVK-----LDCPAIGKQFAA--EEISAQVLRKLVDDASKFLNDKVTKAVITVPAY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 160 FqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLLMGpqwrsrlDRE 239
Cdd:PLN03184 183 F-----NDSQRTAT---KDAGRIAGLEVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEVG-------DGV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 240 ASLLGHSG-CRIGGNDLDialafKNLMPLLGMGGETEKGIalpilpwwnavaindvpaqsdfyssangrllnDLVRDare 318
Cdd:PLN03184 248 FEVLSTSGdTHLGGDDFD-----KRIVDWLASNFKKDEGI--------------------------------DLLKD--- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 319 pekvallqkvwRQRLSyRLVRSAEESKIALSSVAETRASLPFIS------DELATLISQQGLESALSQPLARILEQVQLA 392
Cdd:PLN03184 288 -----------KQALQ-RLTEAAEKAKIELSSLTQTSISLPFITatadgpKHIDTTLTRAKFEELCSDLLDRCKTPVENA 355
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446391885 393 LDNAQ---EKPDVIYLTGGSARSPLIK---KALTEQLPGIPI 428
Cdd:PLN03184 356 LRDAKlsfKDIDEVILVGGSTRIPAVQelvKKLTGKDPNVTV 397
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
3-421 |
1.46e-12 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 69.75 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMlcaptreaVSewlYrhhdvpADDDET---QALLRRAI-------- 71
Cdd:PRK00290 5 IGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSV--------VA---F------TKDGERlvgQPAKRQAVtnpentif 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 72 ---RY--NREEDIDVTAKSVQFGLSSlaqyiDDPEEVWFVKSPKSFlgasglKPQQVAlfedlvcAMML-HIRQQAQAQL 145
Cdd:PRK00290 68 sikRLmgRRDEEVQKDIKLVPYKIVK-----ADNGDAWVEIDGKKY------TPQEIS-------AMILqKLKKDAEDYL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 146 PEAITQAVIGRPINFqglggDEANTQAQgilERAAKRAGFkDVV-FQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCS 224
Cdd:PRK00290 130 GEKVTEAVITVPAYF-----NDAQRQAT---KDAGKIAGL-EVLrIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 225 LLLMGpqwrsrlDREASLLGHSG-CRIGGNDLD------IALAFKNlmpllgmggetEKGIalpilpwwnavaindvpaq 297
Cdd:PRK00290 201 ILEIG-------DGVFEVLSTNGdTHLGGDDFDqriidyLADEFKK-----------ENGI------------------- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 298 sdfyssangrllnDLVRDarepeKVALlqkvwrQRLSyrlvRSAEESKIALSSVAETRASLPFIS-DE-----LATLISQ 371
Cdd:PRK00290 244 -------------DLRKD-----KMAL------QRLK----EAAEKAKIELSSAQQTEINLPFITaDAsgpkhLEIKLTR 295
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446391885 372 QGLESaLSQPL-ARILEQVQLALDNAQEKP----DVIyLTGGSARSPLIKKALTE 421
Cdd:PRK00290 296 AKFEE-LTEDLvERTIEPCKQALKDAGLSVsdidEVI-LVGGSTRMPAVQELVKE 348
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
176-443 |
5.26e-12 |
|
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: 66.34 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 176 LERAAKRAGFKDVVFQYEPVAA----GLDyeatLQEEKRVLVVDIGGGTTDCSLLLMGpqwrsrldreaSLLGHSGCRIG 251
Cdd:cd10225 110 VKEAAEHAGAREVYLIEEPMAAaigaGLP----IEEPRGSMVVDIGGGTTEIAVISLG-----------GIVTSRSVRVA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 252 GNDLDIALAfknlmpllgmggetekgialpilpwwnavaindvpaqsdfyssangrllnDLVRdaREpekvallqkvwrq 331
Cdd:cd10225 175 GDEMDEAII--------------------------------------------------NYVR--RK------------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 332 rlsYRLV---RSAEESKIALSSVAETRASLPF-------ISDELATL-ISQQGLESALSQPLARILEQVQLALDNAqeKP 400
Cdd:cd10225 190 ---YNLLigeRTAERIKIEIGSAYPLDEELSMevrgrdlVTGLPRTIeITSEEVREALEEPVNAIVEAVRSTLERT--PP 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446391885 401 DV--------IYLTGGSARSPLIKKALTEQLpGIPIAGGDDFGSVTA-GLAR 443
Cdd:cd10225 265 ELaadivdrgIVLTGGGALLRGLDELLREET-GLPVHVADDPLTCVAkGAGK 315
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
3-226 |
1.06e-11 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 66.80 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLCaptreavsewlYRHHDVPADDDETQALLRRAIRYNREEDIDVT 82
Cdd:PRK01433 22 VGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTID-----------FTSNNFTIGNNKGLRSIKRLFGKTLKEILNTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 83 AKsvqfgLSSLAQYIDDPEEVwfvksPKSFLGASGLKPQQVAlfedlvCAMMLHIRQQAQAQLPEAITQAVIGRPINFqg 162
Cdd:PRK01433 91 AL-----FSLVKDYLDVNSSE-----LKLNFANKQLRIPEIA------AEIFIYLKNQAEEQLKTNITKAVITVPAHF-- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446391885 163 lggdeaNTQAQGILERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLL 226
Cdd:PRK01433 153 ------NDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSIL 210
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
3-432 |
3.93e-11 |
|
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: 64.19 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSmlcaptreavsewlyrhhdVPADDDETQALLRRAIRYNREEDIDVT 82
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPS-------------------VVSVDEDGSILVGRAAKERLVTHPDRT 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 83 AKSVQFGLSSLAQYIddpeevwfvkspksfLGASGLKPqqvalfEDLVCAMMLHIRQQAQAQLPEAITQAVIGRPINFqg 162
Cdd:cd10235 62 AASFKRFMGTDKQYR---------------LGNHTFRA------EELSALVLKSLKEDAEAYLGEPVTEAVISVPAYF-- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 163 lggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYE-ATLQEEKRVLVVDIGGGTTDCSLLLMgpqWRSRLDREAS 241
Cdd:cd10235 119 ---NDEQRKAT---KDAGELAGLKVERLINEPTAAALAYGlHKREDETRFLVFDLGGGTFDVSVLEL---FEGVIEVHAS 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 242 llghSG-CRIGGNDLDIALAfknlmpllgmggetekgialpilpwwNAVAindvpaqsdfyssangrllnDLVRDAREPE 320
Cdd:cd10235 190 ----AGdNFLGGEDFTHALA--------------------------DYFL--------------------KKHRLDFTSL 219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 321 KVALLQKVWRQrlsyrlvrsAEESKIALSSVAETRASLPFISDELATLISQQGLESALSQPLARILEQVQLALDNAQEKP 400
Cdd:cd10235 220 SPSELAALRKR---------AEQAKRQLSSQDSAEIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAGLKP 290
|
410 420 430
....*....|....*....|....*....|....*
gi 446391885 401 ---DVIYLTGGSARSPLIKKALTEQLPGIPIAGGD 432
Cdd:cd10235 291 sdiDAVILVGGATRMPLVRQLIARLFGRLPLSSLD 325
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
113-429 |
7.56e-11 |
|
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: 63.28 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 113 LGASGLKPQQVALF---------EDLVcAMML-HIRQQAQAQLPEAITQAVIGRPINFqglggdeanTQAQGI-LERAAK 181
Cdd:cd10230 53 LALATRFPENTFSYlkdllgysvEELV-AMILeYAKSLAESFAGEPIKDAVITVPPFF---------TQAQRQaLLDAAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 182 RAGFKdvVFQY--EPVAAGLDY----EATLQEEKRVLVVDIGGGTTDCSLLLMGP-----QWRSRLDREASLLGHSGCR- 249
Cdd:cd10230 123 IAGLN--VLSLinDNTAAALNYgidrRFENNEPQNVLFYDMGASSTSATVVEFSSvkekdKGKNKTVPQVEVLGVGWDRt 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 250 IGGNDLDIALA--FKNLMpllgmggETEKGIALPIlpwwnavaindvpaqsdfysSANGRLLNdlvrdarepekvallqk 327
Cdd:cd10230 201 LGGLEFDLRLAdhLADEF-------NEKHKKDKDV--------------------RTNPRAMA----------------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 328 vwrqrlsyRLVRSAEESKIALSSVAETRASLPFISDE--LATLISQQGLESALSQPLARILEQVQLALDNAQEKPDVIY- 404
Cdd:cd10230 237 --------KLLKEANRVKEVLSANTEAPASIESLYDDidFRTKITREEFEELCADLFERVVAPIEEALEKAGLTLDDIDs 308
|
330 340
....*....|....*....|....*..
gi 446391885 405 --LTGGSARSPLIKKALTEQLPGIPIA 429
Cdd:cd10230 309 veLIGGGTRVPKVQEALKEALGRKELG 335
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
102-425 |
4.62e-10 |
|
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: 61.15 E-value: 4.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 102 EVWFVKSPKSFlgasglKPQQVAlfedlvcAMML-HIRQQAQAQLPEAITQAVIGRPINFqglggDEANTQAQgilERAA 180
Cdd:cd24093 98 EVQYLGETKTF------SPQEIS-------AMVLtKMKEIAEAKIGKKVEKAVITVPAYF-----NDAQRQAT---KDAG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 181 KRAGFKDVVFQYEPVAAGLDY---EATLQEEKRVLVVDIGGGTTDCSLL-LMGPQWrsrldreaSLLGHSG-CRIGGNDL 255
Cdd:cd24093 157 AIAGLNVLRIINEPTAAAIAYglgAGKSEKERHVLIFDLGGGTFDVSLLhIAGGVY--------TVKSTSGnTHLGGQDF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 256 DIALAfknlmpllgmggetekgialpilpwwnavaindvpaqSDFYSSANGRLLNDLVRDARepekvALlqkvwrqrlsY 335
Cdd:cd24093 229 DTNLL-------------------------------------EHFKAEFKKKTGLDISDDAR-----AL----------R 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 336 RLVRSAEESKIALSSVAETRASLPFISD--ELATLISQQGLESALSQPLARILEQVQLALDNAQ-EKPDV--IYLTGGSA 410
Cdd:cd24093 257 RLRTAAERAKRTLSSVTQTTVEVDSLFDgeDFESSITRARFEDLNAALFKSTLEPVEQVLKDAKiSKSQIdeVVLVGGST 336
|
330
....*....|....*
gi 446391885 411 RSPLIKKALTEQLPG 425
Cdd:cd24093 337 RIPKVQKLLSDFFDG 351
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
3-442 |
4.80e-10 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 61.62 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLCAPTREAVSEWLYRHHDVPADDDETQALLRRAIRYNREEDIDVT 82
Cdd:PTZ00186 30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 83 AKSVQFGLSSLAQyiddpEEVWFVKSpksflGASGLKPQQVALFedlvcaMMLHIRQQAQAQLPEAITQAVIGRPINFqg 162
Cdd:PTZ00186 110 IKNVPYKIVRAGN-----GDAWVQDG-----NGKQYSPSQIGAF------VLEKMKETAENFLGHKVSNAVVTCPAYF-- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 163 lggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLLMGPqwrSRLDREASl 242
Cdd:PTZ00186 172 ---NDAQRQAT---KDAGTIAGLNVIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEIAG---GVFEVKAT- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 243 lgHSGCRIGGNDLDIALafknlmpllgmggetekgialpilpwwnavaindvpaqSDFyssangrllndLVRDAREPEKV 322
Cdd:PTZ00186 242 --NGDTHLGGEDFDLAL--------------------------------------SDY-----------ILEEFRKTSGI 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 323 ALLqkvwRQRLSYRLVR-SAEESKIALSSVAETRASLPFIS------DELATLISQQGLESALSQPLARILEQVQLALDN 395
Cdd:PTZ00186 271 DLS----KERMALQRVReAAEKAKCELSSAMETEVNLPFITanadgaQHIQMHISRSKFEGITQRLIERSIAPCKQCMKD 346
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446391885 396 A----QEKPDVIyLTGGSARSPLIKKALTEQLPGIPIAGGDDFGSVTAGLA 442
Cdd:PTZ00186 347 AgvelKEINDVV-LVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAA 396
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
3-413 |
6.98e-10 |
|
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: 60.54 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLcAPTREAvsEWLYrhhDVPADddetqallRRAIrYNREEDIDVT 82
Cdd:cd11734 4 IGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVV-AFTKDG--ERLV---GVPAK--------RQAV-VNPENTLFAT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 83 AKSVQFGLSSlAQYIDDPEEVWFVKSPKS----FLGASGLK--PQQVALFedlVCAMMlhiRQQAQAQLPEAITQAVIGR 156
Cdd:cd11734 69 KRLIGRKFDD-AEVQRDIKEVPYKIVKHSngdaWVEARGQKysPSQIGAF---VLGKM---KETAEGYLGKPVKNAVVTV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 157 PINFqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLLMgpqwRSRL 236
Cdd:cd11734 142 PAYF-----NDSQRQAT---KDAGQIAGLNVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEI----QKGV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 237 DREASLLGHSgcRIGGNDLDIALA------FKNlmpllgmggetEKGIALpilpwwnavaindvpaqsdfyssANGRLLN 310
Cdd:cd11734 210 FEVKSTNGDT--HLGGEDFDIALVrhivseFKK-----------ESGIDL-----------------------SKDRMAI 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 311 DLVRDArepekvallqkvwrqrlsyrlvrsAEESKIALSSVAETRASLPFISDE------LATLISQQGLESaLSQPLA- 383
Cdd:cd11734 254 QRIREA------------------------AEKAKIELSSTLQTDINLPFITADasgpkhINMKLTRAQFES-LVKPLVd 308
|
410 420 430
....*....|....*....|....*....|....
gi 446391885 384 RILEQVQLALDNAQEKP----DVIyLTGGSARSP 413
Cdd:cd11734 309 RTVEPCKKALKDAGVKTseinEVI-LVGGMSRMP 341
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
3-413 |
7.50e-10 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 60.99 E-value: 7.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLkmENDStllpSMLCAPTREAVSEWLYRHHDVPA------DDDETQALLRRAIryNRE 76
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVI--ENSE----GMRTTPSVVAFTEDGQRLVGIVAkrqavtNPENTVFATKRLI--GRR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 77 EDIDVTAKSVQfglsSLAQYI--DDPEEVWFVKSPKSFlgasglKPQQVALFedlvcaMMLHIRQQAQAQLPEAITQAVI 154
Cdd:PTZ00400 116 YDEDATKKEQK----ILPYKIvrASNGDAWIEAQGKKY------SPSQIGAF------VLEKMKETAESYLGRKVKQAVI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 155 GRPINFqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLlmgpqwrs 234
Cdd:PTZ00400 180 TVPAYF-----NDSQRQAT---KDAGKIAGLDVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISIL-------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 235 rldreasllghsgcRIGGNDLDIALAFKNlmplLGMGGEtekgialpilpwwnavaindvpaqsDFyssaNGRLLNDLVR 314
Cdd:PTZ00400 244 --------------EILGGVFEVKATNGN----TSLGGE-------------------------DF----DQRILNYLIA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 315 DAREPEKVALLQ-KVWRQRLSyrlvRSAEESKIALSSVAETRASLPFISDE------LATLISQQGLESALSQPLARILE 387
Cdd:PTZ00400 277 EFKKQQGIDLKKdKLALQRLR----EAAETAKIELSSKTQTEINLPFITADqsgpkhLQIKLSRAKLEELTHDLLKKTIE 352
|
410 420 430
....*....|....*....|....*....|
gi 446391885 388 QVQLALDNA----QEKPDVIyLTGGSARSP 413
Cdd:PTZ00400 353 PCEKCIKDAgvkkDELNDVI-LVGGMTRMP 381
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
176-428 |
2.62e-09 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 58.55 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 176 LERAAKRAGFKDVVFQYEPVAA----GLDyeatLQEEKRVLVVDIGGGTTDCSLLLMGpqwrsrldreaSLLGHSGCRIG 251
Cdd:COG1077 118 VRDAAEQAGAREVYLIEEPMAAaigaGLP----IEEPTGNMVVDIGGGTTEVAVISLG-----------GIVVSRSIRVA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 252 GNDLDialafknlmpllgmggetekgialpilpwwnavaindvpaqsdfyssangrllndlvrdarepekVALLQKVWRQ 331
Cdd:COG1077 183 GDELD-----------------------------------------------------------------EAIIQYVRKK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 332 rlsYRLV---RSAEESKIALSSVAETRASLPF-IS--DeLAT------LISQQGLESALSQPLARILEQVQLALDNAqeK 399
Cdd:COG1077 198 ---YNLLigeRTAEEIKIEIGSAYPLEEELTMeVRgrD-LVTglpktiTITSEEIREALEEPLNAIVEAIKSVLEKT--P 271
|
250 260 270
....*....|....*....|....*....|....*..
gi 446391885 400 PDV--------IYLTGGSARSPLIKKALTEQLpGIPI 428
Cdd:COG1077 272 PELaadivdrgIVLTGGGALLRGLDKLLSEET-GLPV 307
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
3-421 |
7.20e-09 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 57.88 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSmlcaptreavsewlyrhhdvpadddetqallrrAIRYnreedidvT 82
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPS---------------------------------VVRY--------L 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 83 AKSVQFGLSSLAQYIDDPEEVwfVKSPKSFLGAS-----GLKPQQVALFEDLVCAMML-------------------HIR 138
Cdd:PRK05183 61 EDGIEVGYEARANAAQDPKNT--ISSVKRFMGRSladiqQRYPHLPYQFVASENGMPLirtaqglkspvevsaeilkALR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 139 QQAQAQLPEAITQAVIGRPINFqglggDEAntQAQGILErAAKRAGFKDVVFQYEPVAA----GLDYEAtlqeEKRVLVV 214
Cdd:PRK05183 139 QRAEETLGGELDGAVITVPAYF-----DDA--QRQATKD-AARLAGLNVLRLLNEPTAAaiayGLDSGQ----EGVIAVY 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 215 DIGGGTTDCSLLlmgpqwrsRLDR---EA-SLLGHSGcrIGGNDLDIALAfKNLMPLLGMGgetekgialpilpwwnava 290
Cdd:PRK05183 207 DLGGGTFDISIL--------RLSKgvfEVlATGGDSA--LGGDDFDHLLA-DWILEQAGLS------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 291 indvPAQSDFyssangrllndlvrDAREpekvaLLQKvwrqrlsyrlvrsAEESKIALSSVAETRASLPFISDElatlIS 370
Cdd:PRK05183 257 ----PRLDPE--------------DQRL-----LLDA-------------ARAAKEALSDADSVEVSVALWQGE----IT 296
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446391885 371 QQGLEsALSQPL-ARILEQVQLALDNAQEKPD----VIyLTGGSARSPLIKKALTE 421
Cdd:PRK05183 297 REQFN-ALIAPLvKRTLLACRRALRDAGVEADevkeVV-MVGGSTRVPLVREAVGE 350
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
2-226 |
1.07e-08 |
|
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: 56.60 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 2 FIGFDYGTANCSVAVMR-DGKPQLLKMENDSTLLPSMLCAptreavsewlyrhhdvpADDDE---TQALlrrairynree 77
Cdd:cd10232 2 VIGISFGNSNSSIAIINkDGRAEVIANEDGDRQIPSILAY-----------------HGDEEyhgSQAK----------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 78 didvtaksvqfglsslAQYIDDPEEVwfVKSPKSFLGASGLKPQqvalfeDLVCAMMLHIRQQAQAQLPEAITQAVIGRP 157
Cdd:cd10232 54 ----------------AQLVRNPKNT--VANFRDLLGTTTLTVS------EVTTRYLRRLKESAEDYLGKKVTGAVLSVP 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446391885 158 INFQglggdEANTQAqgiLERAAKRAGFKDVVFQYEPVAAGLDYEATLQ------EEKRVLVVDIGGGTTDCSLL 226
Cdd:cd10232 110 TDFT-----EKQKAA---LVAAAAAAGLEVLQLIPEPAAAALAYDLRAEtsgdtiKDKTVVVADLGGTRSDVTVV 176
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
3-413 |
2.27e-08 |
|
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: 55.73 E-value: 2.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLC----------APT-REAV---SEWLY-------RHHDvpadDD 61
Cdd:cd11733 4 IGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAftadgerlvgMPAkRQAVtnpENTLYatkrligRRFD----DP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 62 ETQallrrairynreEDIdvtaKSVQFGLsslaqyiddpeevwfVKSPK--SFLGASGLK--PQQVALFedlvcaMMLHI 137
Cdd:cd11733 80 EVQ------------KDI----KMVPYKI---------------VKASNgdAWVEAHGKKysPSQIGAF------VLTKM 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 138 RQQAQAQLPEAITQAVIGRPINFqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIG 217
Cdd:cd11733 123 KETAESYLGRPVKNAVITVPAYF-----NDSQRQAT---KDAGQIAGLNVLRIINEPTAAALAYGLDKKDDKIIAVYDLG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 218 GGTTDCSLL-LMGPQWRSRLDREASLLghsgcriGGNDLDIAL------AFKNlmpllgmggetEKGIalpilpwwnava 290
Cdd:cd11733 195 GGTFDISILeIQKGVFEVKATNGDTFL-------GGEDFDNALlnylvaEFKK-----------EQGI------------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 291 indvpaqsdfyssangrllnDLVRDarepeKVALlqkvwrQRLSyrlvRSAEESKIALSSVAETRASLPFIS------DE 364
Cdd:cd11733 245 --------------------DLSKD-----NLAL------QRLR----EAAEKAKIELSSSLQTDINLPFITadasgpKH 289
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446391885 365 LATLISQQGLESALSQPLARILEQVQLALDNAQEKP----DVIyLTGGSARSP 413
Cdd:cd11733 290 LNMKLTRAKFESLVGDLIKRTVEPCKKCLKDAGVSKsdigEVL-LVGGMTRMP 341
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
176-262 |
2.07e-07 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 52.83 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 176 LERAAKRAGFK--DVVFqyEPVAAGldyEATL-QEEKR--VLVVDIGGGTTDCSLLlmgpqwrsrldREASLLgHSGC-R 249
Cdd:COG0849 167 LVKCVERAGLEveDLVL--SPLASA---EAVLtEDEKElgVALVDIGGGTTDIAVF-----------KDGALR-HTAViP 229
|
90
....*....|....*
gi 446391885 250 IGGNDL--DIALAFK 262
Cdd:COG0849 230 VGGDHItnDIAIGLR 244
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
3-421 |
2.85e-07 |
|
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: 52.18 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLC----------APTREAVSEW----------LYRHHDVPADDDE 62
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGftekerligeAAKSQQKSNYkntirnfkrlIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 63 TQALLRRAIRYnreEDIDVTAKsvqfglsslAQYIDdpEEVWFVkspksflgasglkPQQVAlfedlvcAMML-HIRQQA 141
Cdd:cd11732 81 IKLLPFKLVEL---EDGKVGIE---------VSYNG--EEVVFS-------------PEQVL-------AMLLgKLKEIA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 142 QAQLPEAITQAVIGRPINFQglggdeaNTQAQGILErAAKRAGFKDVVFQYEPVAAGLDY------EATLQEEKR-VLVV 214
Cdd:cd11732 127 EAANKGEVKDCVISVPGYYT-------DAQRRALLD-AAEIAGLNCLRLINETTAAALDYgiyksdLLESEEKPRiVAFV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 215 DIGGGTTDCSLLLMgpqWRSRLDreasLLGHSG-CRIGGNDLDIALAFKnlmpllgMGGETEK--GIalpilpwwnavai 291
Cdd:cd11732 199 DMGHSSTQVSIAAF---TKGKLK----VLSTAFdRNLGGRDFDRALVEH-------FAEEFKKkyKI------------- 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 292 ndvpaqsdfyssangrllndlvrDAREPEKVALlqkvwrqrlsyRLVRSAEESKIALSSVAETRASLPFISDE--LATLI 369
Cdd:cd11732 252 -----------------------DPLENPKARL-----------RLLDACEKLKKVLSANGEAPLNVECLMEDidFSGQI 297
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446391885 370 SQQGLESaLSQPL-ARILEQVQLALDNAQEKPDVIY---LTGGSARSPLIKKALTE 421
Cdd:cd11732 298 KREEFEE-LIQPLlARLEAPIKKALAQAGLTKEDLHsveIVGGGTRVPAVKEAIAE 352
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
3-428 |
4.55e-07 |
|
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: 51.86 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKmeNDS----TllPSML-CAPTREAVSewlyrhhdVPAdddeTQALLRRAirynree 77
Cdd:cd10238 3 FGVHFGNTNACVAVYKDGRTDVVA--NDAgdrvT--PAVVaFTDNEKIVG--------LAA----KQGLIRNA------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 78 DIDVTAKSVQFGLSSlaqyiDDPEEVWFVK-SPKSFLGASGL---------KPQQVALfEDLVCAMMLHIRQQAQAQLPE 147
Cdd:cd10238 60 SNTVVRVKQLLGRSF-----DDPAVQELKKeSKCKIIEKDGKpgyeieleeKKKLVSP-KEVAKLIFKKMKEIAQSHGGS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 148 AITQAVIGRPINFqglggDEANTQAqgiLERAAKRAGFKDVVFQYEPVAAGLDYE---ATLQEEKRVLVVDIGGGTTDCS 224
Cdd:cd10238 134 DVIDVVLTVPLDF-----DEDQRNA---LKEAAEKAGFNVLRVISEPSAAALAYGigqDDPTENSNVLVYRLGGTSLDVT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 225 LLlmgpQWRSRLDReasLLGHSGCR-IGGNDLDIALAfKNLMpllgmggetekgialpilpwwnavaindvpaqSDFyss 303
Cdd:cd10238 206 VL----SVNNGMYR---VLATRTDDnLGGDDFTEALA-EHLA--------------------------------SEF--- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 304 angrllndlvrdarepekvallQKVWRQ------RLSYRLVRSAEESKIALSSVAETRASLPFISD--ELATLISQQGLE 375
Cdd:cd10238 243 ----------------------KRQWKQdvrenkRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDgmDFQCNVSRARFE 300
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446391885 376 SALSQPLARILEQVQLALDNAQ-EKPDV--IYLTGGSARSPLIKKALTEQLPGIPI 428
Cdd:cd10238 301 SLCSSLFQQCLEPIQEVLNSAGlTKEDIdkVILCGGSSRIPKLQQLIKDLFPSAEV 356
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
132-421 |
1.49e-06 |
|
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: 50.07 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 132 AMMLH-IRQQAQAQLPEAITQAVIGRPINFqglggdeANTQAQGILErAAKRAGFKDVVFQYEPVAAGLDYEAT-----L 205
Cdd:cd24094 115 AMYLGkLKDTTQAELKAPVSDVVISVPGWF-------TDEQRRAILD-AAEIAGLNPLRLMNDTTAAALGYGITktdlpE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 206 QEEK--RVLVVDIGGGTTDCSLLlmgpqwrSRLDREASLLGHSGCR-IGGNDLDIALafknlmpllgmggetekgialpi 282
Cdd:cd24094 187 PEEKprIVAFVDIGHSSYTVSIV-------AFKKGQLTVKGTAYDRhFGGRDFDKAL----------------------- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 283 lpwwnavaindvpaqsdfyssangrlLNDLVRDAREPEKVALLQKvwrQRLSYRLVRSAEESKIALSSVAETRASLPFIS 362
Cdd:cd24094 237 --------------------------TDHFADEFKEKYKIDVRSN---PKAYFRLLAAAEKLKKVLSANAQAPLNVESLM 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446391885 363 DEL--ATLISQQGLESALSQPLARILEQVQLALDNAQEKPDVIY---LTGGSARSPLIKKALTE 421
Cdd:cd24094 288 NDIdvSSMLKREEFEELIAPLLERVTAPLEKALAQAGLTKDEIDfveLVGGTTRVPALKESISA 351
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
137-427 |
2.17e-06 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 49.21 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 137 IRQQAQAQLPEAITQAVIGRPINFQGLggdeantqaqgilERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDI 216
Cdd:cd24004 55 LLKELEEKLGSKLKDVVIAIAKVVESL-------------LNVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 217 GGGTTDCSLLlmgpqwrsrldREASLLGHSGCRIGGNDL--DIALAFKnlmpllgmggetekgialpiLPWWNavaindv 294
Cdd:cd24004 122 GAGTTDIALI-----------RNGGIEAYRMVPLGGDDFtkAIAEGFL--------------------ISFEE------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 295 paqsdfyssangrllndlvrdarepekvallqkvwrqrlsyrlvrsAEESKIALSsvaetRASLPFISDELATLISQQGL 374
Cdd:cd24004 164 ----------------------------------------------AEKIKRTYG-----IFLLIEAKDQLGFTINKKEV 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446391885 375 ESALSQPLARILEQVQLALD--NAQEK-PDVIYLTGGSARSPLIKKALTEQLpGIP 427
Cdd:cd24004 193 YDIIKPVLEELASGIANAIEeyNGKFKlPDAVYLVGGGSKLPGLNEALAEKL-GLP 247
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
3-421 |
3.01e-06 |
|
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: 49.23 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 3 IGFDYGTANCSVAVMRDGKPQLLKMENDSTLLPSMLCAPTRE-----AVSEWLYRHhdvPADddeTQALLRRAI--RYNR 75
Cdd:cd24095 4 VGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQrflgeAAAASILMN---PKN---TISQLKRLIgrKFDD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 76 EEdidvtaksVQFGLSSLA-QYIDDPE-----EVWFVKSPKSFlgasglKPQQVAlfedlvcAMML-HIRQQAQAQLPEA 148
Cdd:cd24095 78 PE--------VQRDLKLFPfKVTEGPDgeigiNVNYLGEQKVF------TPEQIL-------AMLLsNLKRIAEKNLKTP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 149 ITQAVIGRPINFqglggdeanTQAQ--GILErAAKRAGFKDVVFQYEPVAAGLDY--EATLQEE---KRVLVVDIGGGTT 221
Cdd:cd24095 137 VTDCVISVPVYF---------TDAQrrAMLD-AAQIAGLNCLRLMNETTATALAYgiYKTDLPEtdpTNVVFVDVGHSST 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 222 DCSLLlmgpqwrSRLDREASLLGHSGCR-IGGNDLDIALA------FKnlmpllgmggeTEKGIalpilpwwnavaindv 294
Cdd:cd24095 207 QVCVV-------AFKKGQLKVLSHAFDRnLGGRDFDEVLFdhfaaeFK-----------EKYKI---------------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 295 paqsDFYSSAngrllndlvrdarepekvallqkvwrqRLSYRLVRSAEESKIALSSVAETRASLPFISDE--LATLISQQ 372
Cdd:cd24095 253 ----DVKSNK---------------------------KASLRLRAACEKVKKILSANPEAPLNIECLMEDkdVKGMITRE 301
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446391885 373 GLEsALSQP-LARILEQVQLALDNAQEKPDVIY---LTGGSARSPLIKKALTE 421
Cdd:cd24095 302 EFE-ELAAPlLERLLEPLEKALADSGLTVDQIHsveVVGSGSRIPAILKILTK 353
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
176-262 |
3.02e-06 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; 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. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 49.07 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 176 LERAAKRAGFK--DVVFqyEPVAAGldyEATL-QEEKR--VLVVDIGGGTTDCSLLlmgpqwrsrldREASLLgHSGC-R 249
Cdd:cd24048 165 LIKCVERAGLEvdDIVL--SPLASA---EAVLtEDEKElgVALIDIGGGTTDIAVF-----------KNGSLR-YTAViP 227
|
90
....*....|....*
gi 446391885 250 IGGNDL--DIALAFK 262
Cdd:cd24048 228 VGGNHItnDIAIGLN 242
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
130-421 |
5.27e-06 |
|
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: 48.36 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 130 VCAMML-HIRQQAQAQLPEAITQAVIGRPINFqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAA----GLDYEat 204
Cdd:cd10241 116 ISAMVLtKMKETAEAYLGKKVTHAVVTVPAYF-----NDAQRQAT---KDAGTIAGLNVLRIINEPTAAaiayGLDKK-- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 205 lQEEKRVLVVDIGGGTTDCSLLLMGpqwrsrlDREASLLGHSG-CRIGGNDLDialafKNLMpllgmggetEKGIALpil 283
Cdd:cd10241 186 -GGEKNILVFDLGGGTFDVSLLTID-------NGVFEVLATNGdTHLGGEDFD-----QRVM---------DHFIKL--- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 284 pwwnavaindvpaqsdfYSSANGRllnDLVRDAREpekvalLQKvwrqrlsyrLVRSAEESKIALSSVAETRAslpfisd 363
Cdd:cd10241 241 -----------------FKKKTGK---DISKDKRA------VQK---------LRREVEKAKRALSSQHQARI------- 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446391885 364 ELATLIsqQGLEsaLSQPLAR-------------ILEQVQLALDNAQ-EKPDV--IYLTGGSARSPLIKKALTE 421
Cdd:cd10241 279 EIESLF--DGED--FSETLTRakfeelnmdlfrkTLKPVQKVLEDAGlKKSDIdeIVLVGGSTRIPKVQQLLKD 348
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
176-260 |
1.02e-05 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 47.44 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 176 LERAAKRAGFKDVVFQYEPVAA----GLD-YEATLQeekrvLVVDIGGGTTDCSLLLMGpqwrsrldreaSLLGHSGCRI 250
Cdd:PRK13930 119 VREAAEHAGAREVYLIEEPMAAaigaGLPvTEPVGN-----MVVDIGGGTTEVAVISLG-----------GIVYSESIRV 182
|
90
....*....|
gi 446391885 251 GGNDLDIALA 260
Cdd:PRK13930 183 AGDEMDEAIV 192
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
171-265 |
1.29e-05 |
|
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: 47.27 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 171 QAQGILERAAKRAGF------KDVVFQYEPVAAGLDY--------EATLQEEKRVLVVDIGGGTTDCSLLlmgpQWRSRL 236
Cdd:cd10229 154 AAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCqkllaegeEKELKPGDKYLVVDCGGGTVDITVH----EVLEDG 229
|
90 100
....*....|....*....|....*....
gi 446391885 237 DREASLLGhSGCRIGGNDLDiaLAFKNLM 265
Cdd:cd10229 230 KLEELLKA-SGGPWGSTSVD--EEFEELL 255
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
179-258 |
4.49e-05 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 45.47 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 179 AAKRAGFKDVVFQYEPVAA----GLDyeatLQEEKRVLVVDIGGGTTDCSLLlmgpqwrsrldreaSLLG--HSGC-RIG 251
Cdd:PRK13927 118 SALGAGAREVYLIEEPMAAaigaGLP----VTEPTGSMVVDIGGGTTEVAVI--------------SLGGivYSKSvRVG 179
|
....*..
gi 446391885 252 GNDLDIA 258
Cdd:PRK13927 180 GDKFDEA 186
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
170-259 |
5.18e-05 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 45.28 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 170 TQAQGILERA----AKRAGFKDVVFQYEPVAA----GLD-YEATLQeekrvLVVDIGGGTTDCSLLLMGpqwrsrldrea 240
Cdd:PRK13928 104 TGITSVEKRAvreaAEQAGAKKVYLIEEPLAAaigaGLDiSQPSGN-----MVVDIGGGTTDIAVLSLG----------- 167
|
90
....*....|....*....
gi 446391885 241 SLLGHSGCRIGGNDLDIAL 259
Cdd:PRK13928 168 GIVTSSSIKVAGDKFDEAI 186
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
176-262 |
6.16e-05 |
|
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division]
Pssm-ID: 273483 [Multi-domain] Cd Length: 371 Bit Score: 44.93 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 176 LERAAKRAGFK--DVVFQyePVAAGldyEATLQEEKR---VLVVDIGGGTTDCSLLLMGPqwrsrldreaslLGHSGC-R 249
Cdd:TIGR01174 163 LVKCVERCGLEvdNIVLS--GLASA---IAVLTEDEKelgVCLIDIGGGTTDIAVYTGGS------------IRYTKViP 225
|
90
....*....|....*
gi 446391885 250 IGGND--LDIALAFK 262
Cdd:TIGR01174 226 IGGNHitKDIAKALR 240
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
176-256 |
7.86e-05 |
|
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: 44.47 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 176 LERAAKRAGFKDVVFQYEPVAA----GLDYEatlqEEKRVLVVDIGGGTTDCSLLLMGPQWRSRldreaSLlghsgcRIG 251
Cdd:pfam06723 112 VKEAAKNAGAREVFLIEEPMAAaigaGLPVE----EPTGNMVVDIGGGTTEVAVISLGGIVTSK-----SV------RVA 176
|
....*
gi 446391885 252 GNDLD 256
Cdd:pfam06723 177 GDEFD 181
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
176-259 |
1.38e-04 |
|
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also called envB) and the paralogous pair MreB and Mrl of Bacillus subtilis have all been shown to help determine cell shape. This protein is present in a wide variety of bacteria, including spirochetes, but is missing from the Mycoplasmas and from Gram-positive cocci. Most completed bacterial genomes have a single member of this family. In some species it is an essential gene. A close homolog is found in the Archaeon Methanobacterium thermoautotrophicum, and a more distant homolog in Archaeoglobus fulgidus. The family is related to cell division protein FtsA and heat shock protein DnaK. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129982 [Multi-domain] Cd Length: 333 Bit Score: 43.94 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 176 LERAAKRAGFKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLlmgpqwrsrldreaSLLG---HSGCRIGG 252
Cdd:TIGR00904 117 VKESALSAGAREVYLIEEPMAAAIGAGLPVEEPTGSMVVDIGGGTTEVAVI--------------SLGGivvSRSIRVGG 182
|
....*..
gi 446391885 253 NDLDIAL 259
Cdd:TIGR00904 183 DEFDEAI 189
|
|
| ASKHA_NBD_ParM_R1-like |
cd24022 |
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
193-231 |
1.75e-04 |
|
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: 43.41 E-value: 1.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446391885 193 EPVAAGLDY--------EATLQEEKRVLVVDIGGGTTDCSLLLMGPQ 231
Cdd:cd24022 150 EGVAAYFDYlldedgngTDEEEEEGPVAVIDIGGTTTDIAVVSGGLS 196
|
|
| AnmK |
COG2377 |
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis]; |
387-435 |
4.22e-04 |
|
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441944 Cd Length: 363 Bit Score: 42.36 E-value: 4.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 446391885 387 EQVQLALDNAQEKPDVIYLTGGSARSPLIKKALTEQLPGIPIAGGDDFG 435
Cdd:COG2377 275 ASIADAIRRLPPPPDRVLVCGGGAHNPTLMERLQALLPGVPVVTTDELG 323
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
107-259 |
4.33e-04 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 42.20 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 107 KSPKSFLGASGLKPQQVALFeDLVCAMMLHIRQQAQAQLPEAITQ--AVIGRPinfqglGGDEAnTQAQGILErAAKRAG 184
Cdd:PRK13929 55 KTPGKIVAVRPMKDGVIADY-DMTTDLLKQIMKKAGKNIGMTFRKpnVVVCTP------SGSTA-VERRAISD-AVKNCG 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446391885 185 FKDVVFQYEPVAAGLDYEATLQEEKRVLVVDIGGGTTDCSLLLMGpqwrsrldreaSLLGHSGCRIGGNDLDIAL 259
Cdd:PRK13929 126 AKNVHLIEEPVAAAIGADLPVDEPVANVVVDIGGGTTEVAIISFG-----------GVVSCHSIRIGGDQLDEDI 189
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
185-222 |
5.21e-04 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 41.74 E-value: 5.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446391885 185 FKDVVFQYEPVAAGLDYEATLQE--EKRVLVVDIGGGTTD 222
Cdd:cd10227 137 INDVKVLPEGAGAYLDYLLDDDEleDGNVLVIDIGGGTTD 176
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
130-226 |
5.37e-04 |
|
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: 42.23 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 130 VCAMML-HIRQQAQAQLPEAITQAVIGRPINFqglggDEANTQAQgilERAAKRAGFKDVVFQYEPVAAGLDY--EATLQ 206
Cdd:cd10233 114 ISSMVLtKMKEIAEAYLGKKVKNAVITVPAYF-----NDSQRQAT---KDAGTIAGLNVLRIINEPTAAAIAYglDKKGK 185
|
90 100
....*....|....*....|
gi 446391885 207 EEKRVLVVDIGGGTTDCSLL 226
Cdd:cd10233 186 GERNVLIFDLGGGTFDVSLL 205
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
127-226 |
1.24e-03 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 41.32 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446391885 127 EDLVCAMMLHIRQQAQAQLPEAITQAVIGRPINFQglggdeaNTQAQGIlERAAKRAGFKDVVFQYEPVAA----GLDYE 202
Cdd:PTZ00009 118 EEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFN-------DSQRQAT-KDAGTIAGLNVLRIINEPTAAaiayGLDKK 189
|
90 100
....*....|....*....|....
gi 446391885 203 ATlqEEKRVLVVDIGGGTTDCSLL 226
Cdd:PTZ00009 190 GD--GEKNVLIFDLGGGTFDVSLL 211
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
374-442 |
1.72e-03 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 40.34 E-value: 1.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446391885 374 LESALSQPLARILEQVQLALD-----NAQEKPDVIYLTGGSARSPLIKKALTEQLpGIPIAGGDDFGSVTAGLA 442
Cdd:cd24049 247 VAEALRPVLERLVSEIRRSLDyyrsqNGGEPIDKIYLTGGGSLLPGLDEYLSERL-GIPVEILNPFSNIESKKS 319
|
|
| ASKHA_NBD_ParM_Alp7A-like |
cd24023 |
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar ... |
200-226 |
4.29e-03 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis actin-like protein Alp7A and similar proteins from the ParM domain family; The family corresponds to a group of uncharacterized proteins similar to Bacillus subtilis actin-like protein Alp7A, a plasmid partitioning protein that functions in plasmid segregation. The subfamily also includes Bacillus thuringiensis ParM hybrid fusion protein.
Pssm-ID: 466873 [Multi-domain] Cd Length: 368 Bit Score: 39.24 E-value: 4.29e-03
10 20
....*....|....*....|....*..
gi 446391885 200 DYEATLQEEKRVLVVDIGGGTTDCSLL 226
Cdd:cd24023 199 DTEDEDLKEKNILIIDIGGGTTDVAVF 225
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