|
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: 923.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 1 MFIGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLCAPTREAVSEWLFRHHQVPATAAETQALLRRAVSFNREEDID 80
Cdd:PRK11678 1 MFIGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREAVSEWLYRHLDVPAYDDERQALLRRAIRYNREEDID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 81 VTPSSVQFGLSSLGQYIEDPEEVYFVKSPKSFLGASGLKPQQVAMFEDLVCAMMLHIRNQAQSQVPDAITQAVIGRPINF 160
Cdd:PRK11678 81 VTAQSVFFGLAALAQYLEDPEEVYFVKSPKSFLGASGLKPQQVALFEDLVCAMMLHIKQQAEAQLQAAITQAVIGRPVNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 161 QGLGGDEANQQAQGILERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSLLLMGPQWHHRRDREN 240
Cdd:PRK11678 161 QGLGGEEANRQAEGILERAAKRAGFKDVEFQFEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSMLLMGPSWRGRADRSA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 241 SLLGHSGCRVGGNDLDIALAFKSLMPLLGMGGQTEKGIALPILPWWNAIAINDVPAQSDFYSTANGRLLNDLVRDAQDAE 320
Cdd:PRK11678 241 SLLGHSGQRIGGNDLDIALAFKQLMPLLGMGSETEKGIALPSLPFWNAVAINDVPAQSDFYSLANGRLLNDLIRDAREPE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 321 KVALLYKVWRQRLSYRVVRTAEESKIALSDRPEHAVTLPFISDDLATAITQEGLEMALAQPLQRILEQVQLALENGKEKP 400
Cdd:PRK11678 321 KVARLLKVWRQRLSYRLVRSAEEAKIALSDQAETRASLDFISDGLATEISQQGLEEAISQPLARILELVQLALDQAQVKP 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 550733447 401 DVIYLTGGSARSPLIKKALAEQLPGIPIAGGDDFGSVTAGLARWAQVVFS 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 |
7.11e-162 |
|
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: 462.90 E-value: 7.11e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLCAPTREAVSewlfrhhqvpataaetqallrravsfnreedidvt 82
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEG----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 83 PSSVQFGLSSLGQYIEDPEEVYFVKSPKSFLGASGLKPQ----QVAMFEDLVCAMMLHIRNQAQSQVPDAITQAVIGRPI 158
Cdd:cd10231 46 AESIYFGNDAIDAYLNDPEEGRLIKSVKSFLGSSLFDETtifgRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 159 NFQGlGGDEANQQAQGILERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSLLLMGPQWhhrRDR 238
Cdd:cd10231 126 HFSG-VGAEDDAQAESRLRDAARRAGFRNVEFQYEPIAAALDYEQRLDREELVLVVDFGGGTSDFSVLRLGPNR---TDR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 239 ENSLLGHSGCRVGGNDLDIALAFKSLMPLLGMGGQTEKGIALPILPWWNAIAINDVPAQSDFYSTANGRLLNDLVRDAQD 318
Cdd:cd10231 202 RADILATSGVGIGGDDFDRELALKKVMPHLGRGSTYVSGDKGLPVPAWLYADLSNWHAISLLYTKKTLRLLLDLRRDAAD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 319 AEKVALLYKVWRQRLSYRVVRTAEESKIALSDRPEHAVTLPFISDDLATAITQEGLEMALAQPLQRILEQVQLALENGKE 398
Cdd:cd10231 282 PEKIERLLSLVEDQLGHRLFRAVEQAKIALSSADEATLSFDFIEISIKVTITRDEFETAIAFPLARILEALERTLNDAGV 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 550733447 399 KP---DVIYLTGGSARSPLIKKALAEQLPGIPIAGGDDFGSVTAGLAR 443
Cdd:cd10231 362 KPsdvDRVFLTGGSSQSPAVRQALASLFGQARLVEGDEFGSVAAGLAL 409
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
3-449 |
6.36e-68 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 223.93 E-value: 6.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSmlcaptreavsewlfrhhqvpataaetqallrrAVSFNREEDIDVt 82
Cdd:COG0443 2 IGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPS---------------------------------VVAFPKDGEVLV- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 83 pssvqfGLSSLGQYIEDPEEvyFVKSPKSFLGaSGLKPQQVAM------FEDLVCAMMLHIRNQAQSQVPDAITQAVIGR 156
Cdd:COG0443 48 ------GEAAKRQAVTNPGR--TIRSIKRLLG-RSLFDEATEVggkrysPEEISALILRKLKADAEAYLGEPVTRAVITV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 157 PINFqglggDEANQQAqgiLERAAHRAGFRDVVFQYEPVAAGLDFEATL-TEEKRVLVVDIGGGTTDCSLLLMGPQWHHR 235
Cdd:COG0443 119 PAYF-----DDAQRQA---TKDAARIAGLEVLRLLNEPTAAALAYGLDKgKEEETILVYDLGGGTFDVSILRLGDGVFEV 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 236 rdrenslLGHSGC-RVGGNDLDIALAfKSLMPLLGMggqtEKGIalpilpwwnaiaindvpaqsdfystangrllnDLVR 314
Cdd:COG0443 191 -------LATGGDtHLGGDDFDQALA-DYVAPEFGK----EEGI--------------------------------DLRL 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 315 DAQDaekvallykvwRQRLsyrvVRTAEESKIALSDRPEHAVTLPFISD-DLATAITQEGLEMALAQPLQRILEQVQLAL 393
Cdd:COG0443 227 DPAA-----------LQRL----REAAEKAKIELSSADEAEINLPFSGGkHLDVELTRAEFEELIAPLVERTLDPVRQAL 291
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 550733447 394 ENGKEKP---DVIYLTGGSARSPLIKKALAEQLPGIPIAGGDDFGSVTAGLARWAQVVF 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 ... |
98-428 |
8.61e-25 |
|
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: 104.11 E-value: 8.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 98 EDPEEVYFVKSPKSFLGASGLKPQQVAMFEDLVCAMMLHIRNQAQSQV---PDAITQAVIGRPINFqglggdeaNQQAQG 174
Cdd:cd10170 20 GEPPLVVLQLPWPGGDGGSSKVPSVLEVVADFLRALLEHAKAELGDRIwelEKAPIEVVITVPAGW--------SDAARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 175 ILERAAHRAGF----RDVVFQYEPVAAGL------DFEATLTEEKRVLVVDIGGGTTDCSLLLMGPQWHHRRDRensLLG 244
Cdd:cd10170 92 ALREAARAAGFgsdsDNVRLVSEPEAAALyaledkGDLLPLKPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLEE---VAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 245 HSGCRVGGNDLDIALAfkslmpllgmggqtekgialpilpwwnaiaindvpaqsdfystangrllnDLVRDAQDAEKVAL 324
Cdd:cd10170 169 GGGALLGGTDIDEAFE--------------------------------------------------KLLREKLGDKGKDL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 325 LYKVWRQRlsYRVVRTAEESKIALSDRPEHAVTLPFI---------SDDLATAITQEGLEMALAQPLQRILEQVQLALE- 394
Cdd:cd10170 199 GRSDADAL--AKLLREFEEAKKRFSGGEEDERLVPSLlggglpelgLEKGTLLLTEEEIRDLFDPVIDKILELIEEQLEa 276
|
330 340 350
....*....|....*....|....*....|....
gi 550733447 395 NGKEKPDVIYLTGGSARSPLIKKALAEQLPGIPI 428
Cdd:cd10170 277 KSGTPPDAVVLVGGFSRSPYLRERLRERFGSAGI 310
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
3-428 |
1.92e-21 |
|
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: 94.95 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLL-KMENGSTLLPSmlcaptreavsewlfrhhqvpataaetqallrrAVSFNREEDIDV 81
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIiENSEGKRTTPS---------------------------------VVYFDKDGEVLV 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 82 tpssvqfGLSSLGQYIEDPEE-VYFVK-----SPKSFLGASG--LKPQQVAmfedlvcAMML-HIRNQAQSQVPDAITQA 152
Cdd:cd24029 48 -------GEEAKNQALLDPENtIYSVKrlmgrDTKDKEEIGGkeYTPEEIS-------AEILkKLKEDAEEQLGGEVKGA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 153 VIGRPINFqglgGDEANQQAQgileRAAHRAGFRDVVFQYEPVAA----GLDFEatlTEEKRVLVVDIGGGTTDCSLLlm 228
Cdd:cd24029 114 VITVPAYF----NDKQRKATK----KAAELAGLNVLRLINEPTAAalayGLDKE---GKDGTILVYDLGGGTFDVSIL-- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 229 gpqwhHRRDRENSLLGHSG-CRVGGNDLDIALAfkSLMpllgmggQTEKGIALPILPwwnaiaindvpaqSDFYSTANGR 307
Cdd:cd24029 181 -----EIENGKFEVLATGGdNFLGGDDFDEAIA--ELI-------LEKIGIETGILD-------------DKEDERARAR 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 308 LLNDlvrdaqdaekvallykvwrqrlsyrvvrtAEESKIALSDRPEHAVTLPFISD--DLATAITQEGLEmALAQPL-QR 384
Cdd:cd24029 234 LREA-----------------------------AEEAKIELSSSDSTDILILDDGKggELEIEITREEFE-ELIAPLiER 283
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 550733447 385 ILEQVQLALENGKEKP---DVIYLTGGSARSPLIKKALAEQLPGIPI 428
Cdd:cd24029 284 TIDLLEKALKDAKLSPediDRVLLVGGSSRIPLVREMLEEYFGREPI 330
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
3-425 |
8.05e-21 |
|
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: 93.73 E-value: 8.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMlcaptreavsewlfrhhqvpataaetqallrraVSFNREE----- 77
Cdd:cd24028 2 IGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSY---------------------------------VAFTDGErlvge 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 78 ----DIDVTPSSVQFGLSSL-GQYIEDPEEVYFVKS-PKSFLGASGLKPQQVAMF---------EDlVCAMML-HIRNQA 141
Cdd:cd24028 49 aaknQAASNPENTIFDVKRLiGRKFDDPSVQSDIKHwPFKVVEDEDGKPKIEVTYkgeektfspEE-ISAMILkKLKEIA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 142 QSQVPDAITQAVIGRPINFqglggDEANQQAqgiLERAAHRAGFRdvVFQY--EPVAAGLDF--EATLTEEKRVLVVDIG 217
Cdd:cd24028 128 EAYLGRPVTKAVITVPAYF-----NDAQRQA---TKDAATIAGLN--VLRIinEPTAAALAYglDKKSSGERNVLVFDLG 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 218 GGTTDCSLLLMgpqwhhrrdrensllghsgcrvggndldialaFKSLMPLLGMGGQTEKGialpilpwwnaiaindvpaQ 297
Cdd:cd24028 198 GGTFDVSLLSI--------------------------------DNGVFEVKATAGDTHLG-------------------G 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 298 SDFystaNGRLLNDLVRDAQDAEKVALlykVWRQRLSYRVVRTAEESKIALSDRPEHAVTLPFISD--DLATAITQEGLE 375
Cdd:cd24028 227 EDF----DNRLVEYLVEEFKKKHGKDL---RENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDgiDFETTITRAKFE 299
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 550733447 376 MaLAQPL-QRILEQVQLALENGKEKP----DVIyLTGGSARSPLIKKALAEQLPG 425
Cdd:cd24028 300 E-LCEDLfKKCLEPVEKVLKDAKLSKddidEVV-LVGGSTRIPKIQELLSEFFGG 352
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
3-421 |
6.00e-18 |
|
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: 86.16 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLC-APTREAVSEwlfrhhqvpatAAETQALL-------------- 67
Cdd:pfam00012 2 IGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAfTPKERLVGQ-----------AAKNQAVTnpkntvfsvkrlig 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 68 RRAVSFNREEDIDVTPSSVqfglsslgqyIEDPEEVYFVKSpkSFLGASgLKPQQVAmfedlvcAMML-HIRNQAQSQVP 146
Cdd:pfam00012 71 RKFSDPVVQRDIKHLPYKV----------VKLPNGDAGVEV--RYLGET-FTPEQIS-------AMILqKLKETAEAYLG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 147 DAITQAVIGRPINFqglggDEAnqQAQGILErAAHRAGFRDVVFQYEPVAA----GLDFEatlTEEKRVLVVDIGGGTTD 222
Cdd:pfam00012 131 KPVTDAVITVPAYF-----NDA--QRQATKD-AGQIAGLNVLRIVNEPTAAalayGLDKT---DKERNIAVYDLGGGTFD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 223 CSLLLMGpqwhhrrDRENSLLGHSG-CRVGGNDLDIALA------FKslmpllgmggqTEKGIalpilpwwnaiaindvp 295
Cdd:pfam00012 200 VSILEIG-------RGVFEVKATNGdTHLGGEDFDLRLVdhlaeeFK-----------KKYGI----------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 296 aqsdfystangrllnDLVRDaqdaeKVALlykvwrQRLSyrvvRTAEESKIALSDRpEHAVTLPFIS-----DDLATAIT 370
Cdd:pfam00012 245 ---------------DLSKD-----KRAL------QRLR----EAAEKAKIELSSN-QTNINLPFITamadgKDVSGTLT 293
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 550733447 371 QEGLEmALAQPL-QRILEQVQLALENGKEKPDVIY---LTGGSARSPLIKKALAE 421
Cdd:pfam00012 294 RAKFE-ELVADLfERTLEPVEKALKDAGLSKSEIDevvLVGGSTRIPAVQELVKE 347
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
3-421 |
8.80e-16 |
|
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: 78.41 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSML-CAPTREAVSEWlfrhhqvPATAAETQALLRRAVSFNREedIDV 81
Cdd:cd10236 5 VGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVhYGEDGKITVGE-------KAKENAITDPENTISSVKRL--MGR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 82 TPSSVQFGLSSLG-QYIEDPEEVYFVKspksfLGASGLKPQQVAmfedlvcAMML-HIRNQAQSQVPDAITQAVIGRPIN 159
Cdd:cd10236 76 SLADVKEELPLLPyRLVGDENELPRFR-----TGAGNLTPVEIS-------AEILkELKQRAEETLGGELTGAVITVPAY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 160 FqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAA----GLDFEAtlteEKRVLVVDIGGGTTDCSLLlmgpqwhhr 235
Cdd:cd10236 144 F-----DDAQRQAT---KDAARLAGLNVLRLLNEPTAAalayGLDQKK----EGTIAVYDLGGGTFDISIL--------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 236 rdREN-------SLLGHSgcRVGGNDLDIALAfkslmpllgmggqtekgialpilpwwnaiaindvpaqSDFYSTANGRL 308
Cdd:cd10236 203 --RLSdgvfevlATGGDT--ALGGDDFDHLLA-------------------------------------DWILKQIGIDA 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 309 LNDlvrdaqDAEKVALLykvwrqrlsyrvvRTAEESKIALSDRPEHAVTLPFISDDLATAITQEGLEmALAQPL-QRILE 387
Cdd:cd10236 242 RLD------PAVQQALL-------------QAARRAKEALSDADSASIEVEVEGKDWEREITREEFE-ELIQPLvKRTLE 301
|
410 420 430
....*....|....*....|....*....|....*..
gi 550733447 388 QVQLALENGKEKPDVI---YLTGGSARSPLIKKALAE 421
Cdd:cd10236 302 PCRRALKDAGLEPADIdevVLVGGSTRIPLVRQRVAE 338
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
3-425 |
8.48e-14 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 73.63 E-value: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLC-----------APTREAV--------SEWLFRHHQVPATAAEt 63
Cdd:PRK13411 5 IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGfgksgdrlvgqLAKRQAVtnaentvySIKRFIGRRWDDTEEE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 64 qallRRAVSFN----REEDIDVTpssvqfglsslgqyIEDpeEVYfvkspksflgasglKPQQVAmfedlvcAMMLH-IR 138
Cdd:PRK13411 84 ----RSRVPYTcvkgRDDTVNVQ--------------IRG--RNY--------------TPQEIS-------AMILQkLK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 139 NQAQSQVPDAITQAVIGRPINFQglggdEANQQAQgilERAAHRAGFRDVVFQYEPVAA----GLDfeaTLTEEKRVLVV 214
Cdd:PRK13411 123 QDAEAYLGEPVTQAVITVPAYFT-----DAQRQAT---KDAGTIAGLEVLRIINEPTAAalayGLD---KQDQEQLILVF 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 215 DIGGGTTDCSLLLMGpqwhhrrDRENSLLGHSG-CRVGGNDLDIAlafkslmpllgmggqtekgialpILPWwnaiaind 293
Cdd:PRK13411 192 DLGGGTFDVSILQLG-------DGVFEVKATAGnNHLGGDDFDNC-----------------------IVDW-------- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 294 vpaqsdfystangrllndLVRDAQDAEKVAL-LYKVWRQRLSyrvvRTAEESKIALSDRPEHAVTLPFISDD------LA 366
Cdd:PRK13411 234 ------------------LVENFQQQEGIDLsQDKMALQRLR----EAAEKAKIELSSMLTTSINLPFITADetgpkhLE 291
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550733447 367 TAITQEGLEMALAQPLQRILEQVQLALENGKEKP---DVIYLTGGSARSPLIKKALAEQLPG 425
Cdd:PRK13411 292 MELTRAKFEELTKDLVEATIEPMQQALKDAGLKPediDRVILVGGSTRIPAVQEAIQKFFGG 353
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
176-443 |
1.59e-13 |
|
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: 70.96 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 176 LERAAHRAGFRDVVFQYEPVAA----GLDfeatLTEEKRVLVVDIGGGTTDCSLLLMGpqwhhrrdrenSLLGHSGCRVG 251
Cdd:cd10225 110 VKEAAEHAGAREVYLIEEPMAAaigaGLP----IEEPRGSMVVDIGGGTTEIAVISLG-----------GIVTSRSVRVA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 252 GNDLDialafkslmpllgmggqtekgialpilpwwNAIAindvpaqsdfystangrllnDLVRdaqdaEKvallykvwrq 331
Cdd:cd10225 175 GDEMD------------------------------EAII--------------------NYVR-----RK---------- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 332 rlsYRVV---RTAEESKIALsdrpehAVTLPFISD--------DLAT------AITQEGLEMALAQPLQRILEQVQLALE 394
Cdd:cd10225 190 ---YNLLigeRTAERIKIEI------GSAYPLDEElsmevrgrDLVTglprtiEITSEEVREALEEPVNAIVEAVRSTLE 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 550733447 395 ngKEKPDV--------IYLTGGSARSPLIKKALAEQLpGIPIAGGDDFGSVTA-GLAR 443
Cdd:cd10225 261 --RTPPELaadivdrgIVLTGGGALLRGLDELLREET-GLPVHVADDPLTCVAkGAGK 315
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
3-416 |
1.84e-12 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 69.27 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLcAPTREavSEWLFrhhqvpATAAETQALLRRAVSF-------NR 75
Cdd:PRK13410 5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVV-GFTKD--GELLV------GQLARRQLVLNPQNTFynlkrfiGR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 76 EEDiDVTPSS--VQFGLSSlgqyieDPEEVYFVKSP---KSFlgasglKPqqvamfEDLVCAMMLHIRNQAQSQVPDAIT 150
Cdd:PRK13410 76 RYD-ELDPESkrVPYTIRR------NEQGNVRIKCPrleREF------AP------EELSAMILRKLADDASRYLGEPVT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 151 QAVIGRPINFqglggDEANQQAQgileRAAHR-AGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSLLLMG 229
Cdd:PRK13410 137 GAVITVPAYF-----NDSQRQAT----RDAGRiAGLEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEVG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 230 pqwhhrrdreNSLL---GHSG-CRVGGNDLDialafKSLMPLLGMGGQTEKGIalpilpwwnaiaindvpaqsdfystan 305
Cdd:PRK13410 208 ----------NGVFevkATSGdTQLGGNDFD-----KRIVDWLAEQFLEKEGI--------------------------- 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 306 grllnDLVRDAQdaekvALlykvwrQRLSyrvvRTAEESKIALSDRPEHAVTLPFIsddlatAITQEG---LEMALAQP- 381
Cdd:PRK13410 246 -----DLRRDRQ-----AL------QRLT----EAAEKAKIELSGVSVTDISLPFI------TATEDGpkhIETRLDRKq 299
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 550733447 382 --------LQRILEQVQLALENGKEKPDVI---YLTGGSARSPLIK 416
Cdd:PRK13410 300 feslcgdlLDRLLRPVKRALKDAGLSPEDIdevVLVGGSTRMPMVQ 345
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
3-421 |
1.10e-11 |
|
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: 65.96 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSmlcaptreavsewlfrhhqVPATAAETQALL-----RRAVSfNREE 77
Cdd:cd10234 2 IGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPS-------------------VVAFTKDGERLVgqpakRQAVT-NPEN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 78 didvTPSSVQfglSSLGQYIEDPEEVYFVKSPKSFLGASG----------LKPQQVAmfedlvcAMML-HIRNQAQSQVP 146
Cdd:cd10234 62 ----TIFSIK---RFMGRRYKEVEVERKQVPYPVVSAGNGdawveiggkeYTPEEIS-------AFILqKLKKDAEAYLG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 147 DAITQAVIGRPINFqglggDEANQQAQgileRAAHR-AGFrDVV-FQYEPVAA----GLDFEatltEEKRVLVVDIGGGT 220
Cdd:cd10234 128 EKVTKAVITVPAYF-----NDSQRQAT----KDAGKiAGL-EVLrIINEPTAAalayGLDKK----KDEKILVYDLGGGT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 221 TDCSLLLMGpqwhhrrDRENSLLGHSG-CRVGGNDLD------IALAFKSlmpllgmggqtEKGIalpilpwwnaiaind 293
Cdd:cd10234 194 FDVSILEIG-------DGVFEVLSTNGdTHLGGDDFDqriidyLADEFKK-----------EEGI--------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 294 vpaqsdfystangrllnDLVRDaqdaeKVALlykvwrQRLSyrvvRTAEESKIALSDRPEHAVTLPFISDD------LAT 367
Cdd:cd10234 241 -----------------DLSKD-----KMAL------QRLK----EAAEKAKIELSSVLETEINLPFITADasgpkhLEM 288
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 550733447 368 AITQEGLEmALAQPL-QRILEQVQLALENGKEKP----DVIyLTGGSARSPLIKKALAE 421
Cdd:cd10234 289 KLTRAKFE-ELTEDLvERTIEPVEQALKDAKLSPsdidEVI-LVGGSTRMPAVQELVKE 345
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
176-428 |
1.17e-11 |
|
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: 65.48 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 176 LERAAHRAGFRDVVFQYEPVAA----GLDfeatLTEEKRVLVVDIGGGTTDCSLLLMGpqwhhrrdrenSLLGHSGCRVG 251
Cdd:COG1077 118 VRDAAEQAGAREVYLIEEPMAAaigaGLP----IEEPTGNMVVDIGGGTTEVAVISLG-----------GIVVSRSIRVA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 252 GNDLDialafkslmpllgmggqtekgialpilpwwNAIAindvpaqsdfystangrllnDLVRDAqdaekvallykvwrq 331
Cdd:COG1077 183 GDELD------------------------------EAII--------------------QYVRKK--------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 332 rlsYRVV---RTAEESKIALSD--RPEHAVTLPFISDDLATA------ITQEGLEMALAQPLQRILEQVQLALEngKEKP 400
Cdd:COG1077 198 ---YNLLigeRTAEEIKIEIGSayPLEEELTMEVRGRDLVTGlpktitITSEEIREALEEPLNAIVEAIKSVLE--KTPP 272
|
250 260 270
....*....|....*....|....*....|....*.
gi 550733447 401 DV--------IYLTGGSARSPLIKKALAEQLpGIPI 428
Cdd:COG1077 273 ELaadivdrgIVLTGGGALLRGLDKLLSEET-GLPV 307
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-421 |
3.09e-11 |
|
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: 64.67 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQ--NGQPQLLKMENGSTLLPSMLCAPTREAVsewLFRHHQVPATAAETQALLRRAVSF------- 73
Cdd:cd10237 25 VGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGV---LVGYDALAQAEHNPSNTIYDAKRFigktftk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 74 -NREEDIDVTPSSVQFGLSSLGQYIEDPEEVYFVKSPksflgasglkpqqvamfEDLVCAMMLHIRNQAQSQVPDAITQA 152
Cdd:cd10237 102 eELEEEAKRYPFKVVNDNIGSAFFEVPLNGSTLVVSP-----------------EDIGSLILLKLKKAAEAYLGVPVAKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 153 VIGRPINFqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAAGLDF---EATLTEEkrVLVVDIGGGTTDCSLLlmg 229
Cdd:cd10237 165 VISVPAEF-----DEKQRNAT---RKAANLAGLEVLRVINEPTAAAMAYglhKKSDVNN--VLVVDLGGGTLDVSLL--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 230 pqWHHrrdrensllghsgcrvGGNDLDIALAfkslmpllG---MGGQtekgialpilpwwnaiaindvpaqsDFystaNG 306
Cdd:cd10237 232 --NVQ----------------GGMFLTRAMA--------GnnhLGGQ-------------------------DF----NQ 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 307 RLLNDLVRDAQDAEKVALLYKVWRQRLSYRVvrtaEESKIALSDRPEHAVTLPfISDDLATA--------ITQEGLEmAL 378
Cdd:cd10237 257 RLFQYLIDRIAKKFGKTLTDKEDIQRLRQAV----EEVKLNLTNHNSASLSLP-LQISLPSAfkvkfkeeITRDLFE-TL 330
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 550733447 379 AQPL-QRILEQVQLALENG---KEKPDVIYLTGGSARSPLIKKALAE 421
Cdd:cd10237 331 NEDLfQRVLEPIRQVLAEVelgKEDVDEIVLVGGSTRIPRVRQLVRE 377
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-425 |
4.59e-11 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 64.87 E-value: 4.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLcAPTREAvsewlfrhHQVPATAAETQALLRRAVSF--------N 74
Cdd:PLN03184 42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVV-AYTKNG--------DRLVGQIAKRQAVVNPENTFfsvkrfigR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 75 REEDIDVTPSSVQFglsslgQYIEDPEEVYFVKSPksflgASGlkpQQVAMfEDLVCAMMLHIRNQAQSQVPDAITQAVI 154
Cdd:PLN03184 113 KMSEVDEESKQVSY------RVVRDENGNVKLDCP-----AIG---KQFAA-EEISAQVLRKLVDDASKFLNDKVTKAVI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 155 GRPINFqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSLLLMGpqwhh 234
Cdd:PLN03184 178 TVPAYF-----NDSQRTAT---KDAGRIAGLEVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEVG----- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 235 rrDRENSLLGHSG-CRVGGNDLDialafKSLMPLLGMGGQTEKGIalpilpwwnaiaindvpaqsdfystangrllnDLV 313
Cdd:PLN03184 245 --DGVFEVLSTSGdTHLGGDDFD-----KRIVDWLASNFKKDEGI--------------------------------DLL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 314 RDAQdaekvALlykvwrQRLSyrvvRTAEESKIALSDRPEHAVTLPFISddlATAITQEGLEMALAQP---------LQR 384
Cdd:PLN03184 286 KDKQ-----AL------QRLT----EAAEKAKIELSSLTQTSISLPFIT---ATADGPKHIDTTLTRAkfeelcsdlLDR 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 550733447 385 ILEQVQLALENGK---EKPDVIYLTGGSARSPLIkKALAEQLPG 425
Cdd:PLN03184 348 CKTPVENALRDAKlsfKDIDEVILVGGSTRIPAV-QELVKKLTG 390
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
3-419 |
6.52e-11 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 64.49 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLCaptreavsewlFRHHQVPATAAETQALLRRAVSFNREEDIDvT 82
Cdd:PRK01433 22 VGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTID-----------FTSNNFTIGNNKGLRSIKRLFGKTLKEILN-T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 83 PSsvqfglssLGQYIEDpeevYFVKS---PKSFLGASGLKPQQVAmfedlvCAMMLHIRNQAQSQVPDAITQAVIGRPIN 159
Cdd:PRK01433 90 PA--------LFSLVKD----YLDVNsseLKLNFANKQLRIPEIA------AEIFIYLKNQAEEQLKTNITKAVITVPAH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 160 FqglggdeaNQQAQGILERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSLLLMgpqwhhrRDRE 239
Cdd:PRK01433 152 F--------NDAARGEVMLAAKIAGFEVLRLIAEPTAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNI-------QEGI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 240 NSLLGHSG-CRVGGNDLDIALAfkslmpllgmggqtekgialpilpwwnaiaindvpaqsDFYstANGRLLNDLVRDAQD 318
Cdd:PRK01433 217 FQVIATNGdNMLGGNDIDVVIT--------------------------------------QYL--CNKFDLPNSIDTLQL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 319 AEKVallykvwRQRLSYRvvRTAEESKIALSDRPEHAVTLPFISDDLatAITQEGLEmalaqplqrileqvqlalENGKE 398
Cdd:PRK01433 257 AKKA-------KETLTYK--DSFNNDNISINKQTLEQLILPLVERTI--NIAQECLE------------------QAGNP 307
|
410 420
....*....|....*....|.
gi 550733447 399 KPDVIYLTGGSARSPLIKKAL 419
Cdd:PRK01433 308 NIDGVILVGGATRIPLIKDEL 328
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
132-428 |
9.38e-11 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 62.84 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 132 AMMLHIRNQAQSQVPDAITQAVIGRPInfqglGGDEANQQAqgiLERAAHRAGFRDVVFQYEPVAA----GLD-FEATLT 206
Cdd:PRK13930 83 AMLRYFIKKARGRRFFRKPRIVICVPS-----GITEVERRA---VREAAEHAGAREVYLIEEPMAAaigaGLPvTEPVGN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 207 eekrvLVVDIGGGTTDCSLLLMGpqwhhrrdrenSLLGHSGCRVGGNDLDialafkslmpllgmggqtekgialpilpww 286
Cdd:PRK13930 155 -----MVVDIGGGTTEVAVISLG-----------GIVYSESIRVAGDEMD------------------------------ 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 287 NAIAindvpaqsdfystangrllnDLVRDAqdaekvallykvwrqrlsYRVV---RTAEESKIAL--SDRPEHAVTLPFI 361
Cdd:PRK13930 189 EAIV--------------------QYVRRK------------------YNLLigeRTAEEIKIEIgsAYPLDEEESMEVR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 362 SDDLAT------AITQEGLEMALAQPLQRILEQVQLALEngKEKPDV--------IYLTGGSARSPLIKKALAEQLpGIP 427
Cdd:PRK13930 231 GRDLVTglpktiEISSEEVREALAEPLQQIVEAVKSVLE--KTPPELaadiidrgIVLTGGGALLRGLDKLLSEET-GLP 307
|
.
gi 550733447 428 I 428
Cdd:PRK13930 308 V 308
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
3-425 |
6.78e-10 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 61.28 E-value: 6.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLcAPTReavsewlfrhhqvpataaeTQALL------RRAVsFNRE 76
Cdd:CHL00094 5 VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIV-AYTK-------------------KGDLLvgqiakRQAV-INPE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 77 EdidvTPSSVQ-FGLSSLGQYIEDPEEV-YFVKSPksflGASGLKPQQVAMFEDL----VCAMMLH-IRNQAQSQVPDAI 149
Cdd:CHL00094 64 N----TFYSVKrFIGRKFSEISEEAKQVsYKVKTD----SNGNIKIECPALNKDFspeeISAQVLRkLVEDASKYLGETV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 150 TQAVIGRPINFqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSLLLMG 229
Cdd:CHL00094 136 TQAVITVPAYF-----NDSQRQAT---KDAGKIAGLEVLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEVG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 230 pqwhhrrDRENSLLGHSG-CRVGGNDLDialafKSLMPLLGMGGQTEKGIalpilpwwnaiaindvpaqsdfystangrl 308
Cdd:CHL00094 208 -------DGVFEVLSTSGdTHLGGDDFD-----KKIVNWLIKEFKKKEGI------------------------------ 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 309 lnDLVRDAQdaekvALlykvwrQRLSyrvvRTAEESKIALSDRPEHAVTLPFISDD------LATAITQEGLEmalaQPL 382
Cdd:CHL00094 246 --DLSKDRQ-----AL------QRLT----EAAEKAKIELSNLTQTEINLPFITATqtgpkhIEKTLTRAKFE----ELC 304
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 550733447 383 QRILEQVQLALENG-------KEKPDVIYLTGGSARSPLIKKaLAEQLPG 425
Cdd:CHL00094 305 SDLINRCRIPVENAlkdakldKSDIDEVVLVGGSTRIPAIQE-LVKKLLG 353
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
3-413 |
6.93e-10 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 60.99 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLcaptreAVSEWLFRHHQVPATaaetqallRRAVSfNREEDIDVT 82
Cdd:PTZ00400 44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVV------AFTEDGQRLVGIVAK--------RQAVT-NPENTVFAT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 83 PSSVqfglsslGQYIEDPE--------EVYFVKSPK--SFLGASGLK--PQQVAMFedlvcaMMLHIRNQAQSQVPDAIT 150
Cdd:PTZ00400 109 KRLI-------GRRYDEDAtkkeqkilPYKIVRASNgdAWIEAQGKKysPSQIGAF------VLEKMKETAESYLGRKVK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 151 QAVIGRPINFqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSLL-LMG 229
Cdd:PTZ00400 176 QAVITVPAYF-----NDSQRQAT---KDAGKIAGLDVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILeILG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 230 PQWHHRRDRENSLLghsgcrvGGNDLDialafKSLMPLLGMGGQTEKGIalpilpwwnaiaindvpaqsdfystangrll 309
Cdd:PTZ00400 248 GVFEVKATNGNTSL-------GGEDFD-----QRILNYLIAEFKKQQGI------------------------------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 310 nDLVRDaqdaeKVALlykvwrQRLSyrvvRTAEESKIALSDRPEHAVTLPFISDD------LATAITQEGLEMALAQPLQ 383
Cdd:PTZ00400 285 -DLKKD-----KLAL------QRLR----EAAETAKIELSSKTQTEINLPFITADqsgpkhLQIKLSRAKLEELTHDLLK 348
|
410 420 430
....*....|....*....|....*....|....
gi 550733447 384 RILEQVQLALE----NGKEKPDVIyLTGGSARSP 413
Cdd:PTZ00400 349 KTIEPCEKCIKdagvKKDELNDVI-LVGGMTRMP 381
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
70-429 |
7.31e-10 |
|
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: 60.20 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 70 AVSFNREEDIdvtpssvqFGLSSLGQYIEDPEEVYFvkSPKSFLGASGlkpqqvamfEDLVcAMML-HIRNQAQSQVPDA 148
Cdd:cd10230 38 AVAFRNGERL--------FGDDALALATRFPENTFS--YLKDLLGYSV---------EELV-AMILeYAKSLAESFAGEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 149 ITQAVIGRPINFqglggdeaNQ-QAQGILeRAAHRAGFRdvVFQY--EPVAAGLDF----EATLTEEKRVLVVDIGGGTT 221
Cdd:cd10230 98 IKDAVITVPPFF--------TQaQRQALL-DAAEIAGLN--VLSLinDNTAAALNYgidrRFENNEPQNVLFYDMGASST 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 222 DCSLLLMGPQwHHRRDRENSLLGHS---GCR----VGGNDLDIALAfkslmpllgmggqtekgialpilpwwNAIAindv 294
Cdd:cd10230 167 SATVVEFSSV-KEKDKGKNKTVPQVevlGVGwdrtLGGLEFDLRLA--------------------------DHLA---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 295 paqSDFYSTANGrllNDLVRDAQDAekvalLYKVWRQrlsyrvvrtAEESKIALSDRPEHAVTLPFISD--DLATAITQE 372
Cdd:cd10230 216 ---DEFNEKHKK---DKDVRTNPRA-----MAKLLKE---------ANRVKEVLSANTEAPASIESLYDdiDFRTKITRE 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550733447 373 GLEMA-------LAQPLQRILEQVQLALENgkekPDVIYLTGGSARSPLIKKALAEQLPGIPIA 429
Cdd:cd10230 276 EFEELcadlferVVAPIEEALEKAGLTLDD----IDSVELIGGGTRVPKVQEALKEALGRKELG 335
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
3-413 |
2.50e-09 |
|
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: 58.61 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLcAPTREAvsEWLFrhhQVPATaaetqallRRAVsfnreedidVT 82
Cdd:cd11734 4 IGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVV-AFTKDG--ERLV---GVPAK--------RQAV---------VN 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 83 PSSVQFGLSSL-GQYIEDPE------EVYFVKSPKS----FLGASGLK--PQQVAMFedlVCAMMlhiRNQAQSQVPDAI 149
Cdd:cd11734 61 PENTLFATKRLiGRKFDDAEvqrdikEVPYKIVKHSngdaWVEARGQKysPSQIGAF---VLGKM---KETAEGYLGKPV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 150 TQAVIGRPINFqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSLLLMg 229
Cdd:cd11734 135 KNAVVTVPAYF-----NDSQRQAT---KDAGQIAGLNVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEI- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 230 pqwHHRRDRENSLLGHSgcRVGGNDLDIALAFKSLmpllgmggqtekgialpilpwwnaiaindvpaqSDFYSTANGRLL 309
Cdd:cd11734 206 ---QKGVFEVKSTNGDT--HLGGEDFDIALVRHIV---------------------------------SEFKKESGIDLS 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 310 NDlvrdaqdaeKVALlykvwrqrlsYRVVRTAEESKIALSDRPEHAVTLPFISDD------LATAITQEGLEmALAQPL- 382
Cdd:cd11734 248 KD---------RMAI----------QRIREAAEKAKIELSSTLQTDINLPFITADasgpkhINMKLTRAQFE-SLVKPLv 307
|
410 420 430
....*....|....*....|....*....|....*
gi 550733447 383 QRILEQVQLALENGKEKP----DVIyLTGGSARSP 413
Cdd:cd11734 308 DRTVEPCKKALKDAGVKTseinEVI-LVGGMSRMP 341
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
3-413 |
4.00e-09 |
|
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: 58.04 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSmlcaptreavsewlfrhhqVPATAAETQALL-----RRAVSfnree 77
Cdd:cd11733 4 IGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPS-------------------VVAFTADGERLVgmpakRQAVT----- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 78 didvTPSSVQFGLSSL-GQYIEDPE------EVYF--VKSPK--SFLGASGLK--PQQVAMFedlvcaMMLHIRNQAQSQ 144
Cdd:cd11733 60 ----NPENTLYATKRLiGRRFDDPEvqkdikMVPYkiVKASNgdAWVEAHGKKysPSQIGAF------VLTKMKETAESY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 145 VPDAITQAVIGRPINFqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCS 224
Cdd:cd11733 130 LGRPVKNAVITVPAYF-----NDSQRQAT---KDAGQIAGLNVLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDIS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 225 LL-LMGPQWHHRRDRENSLLghsgcrvGGNDLDIAL------AFKSlmpllgmggqtEKGIalpilpwwnaiaindvpaq 297
Cdd:cd11733 202 ILeIQKGVFEVKATNGDTFL-------GGEDFDNALlnylvaEFKK-----------EQGI------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 298 sdfystangrllnDLVRDaqdaeKVALlykvwrQRLSyrvvRTAEESKIALSDRPEHAVTLPFISDD------LATAITQ 371
Cdd:cd11733 245 -------------DLSKD-----NLAL------QRLR----EAAEKAKIELSSSLQTDINLPFITADasgpkhLNMKLTR 296
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 550733447 372 EGLEMALAQPLQRILEQVQLALEN-GKEKPDV--IYLTGGSARSP 413
Cdd:cd11733 297 AKFESLVGDLIKRTVEPCKKCLKDaGVSKSDIgeVLLVGGMTRMP 341
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
176-262 |
6.84e-09 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 57.45 E-value: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 176 LERAAHRAGFR--DVVFqyEPVAAGldfEATLTEEKR---VLVVDIGGGTTDCSLLlmgpqwhhrrdRENSLLgHSGC-R 249
Cdd:COG0849 167 LVKCVERAGLEveDLVL--SPLASA---EAVLTEDEKelgVALVDIGGGTTDIAVF-----------KDGALR-HTAViP 229
|
90
....*....|....*
gi 550733447 250 VGGNDL--DIALAFK 262
Cdd:COG0849 230 VGGDHItnDIAIGLR 244
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
176-262 |
1.76e-08 |
|
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: 56.00 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 176 LERAAHRAGFR--DVVFqyEPVAAGldfEATLTEEKR---VLVVDIGGGTTDCSLLlmgpqwhhrrdRENSLLgHSGC-R 249
Cdd:cd24048 165 LIKCVERAGLEvdDIVL--SPLASA---EAVLTEDEKelgVALIDIGGGTTDIAVF-----------KNGSLR-YTAViP 227
|
90
....*....|....*
gi 550733447 250 VGGNDL--DIALAFK 262
Cdd:cd24048 228 VGGNHItnDIAIGLN 242
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
3-425 |
2.03e-08 |
|
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: 55.76 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNgQPQLLKMENGSTLLPSMLC-APTREAVSEwlfrhhqvpatAAETQALLrravsfnreedidv 81
Cdd:cd24093 2 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAfTPEERLIGD-----------AAKNQAAL-------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 82 TPSSVQFGLSSL-GQYIEDPE---------------------EVYFVKSPKSFlgasglKPQQVAmfedlvcAMML-HIR 138
Cdd:cd24093 56 NPRNTVFDAKRLiGRRFDDESvqkdmktwpfkvidvngnpviEVQYLGETKTF------SPQEIS-------AMVLtKMK 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 139 NQAQSQVPDAITQAVIGRPINFqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAAGLDF---EATLTEEKRVLVVD 215
Cdd:cd24093 123 EIAEAKIGKKVEKAVITVPAYF-----NDAQRQAT---KDAGAIAGLNVLRIINEPTAAAIAYglgAGKSEKERHVLIFD 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 216 IGGGTTDCSLLlmgpqwhHRRDRENSLLGHSG-CRVGGNDLDIALAfkslmpllgmggqtekgialpilpwwnaiaindv 294
Cdd:cd24093 195 LGGGTFDVSLL-------HIAGGVYTVKSTSGnTHLGGQDFDTNLL---------------------------------- 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 295 paqSDFYSTANGRLLNDLVRDAQdaekvallykvwrqrlSYRVVRTA-EESKIALSDRPEHAVTLPFISD--DLATAITQ 371
Cdd:cd24093 234 ---EHFKAEFKKKTGLDISDDAR----------------ALRRLRTAaERAKRTLSSVTQTTVEVDSLFDgeDFESSITR 294
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 550733447 372 EGLEMALAQPLQRILEQVQLALENGK-EKPDV--IYLTGGSARSPLIKKALAEQLPG 425
Cdd:cd24093 295 ARFEDLNAALFKSTLEPVEQVLKDAKiSKSQIdeVVLVGGSTRIPKVQKLLSDFFDG 351
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
2-226 |
4.28e-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: 54.68 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 2 FIGFDYGTANCSVAIM-QNGQPQLLKMENGStllpsmlcaptreavsewlfrhHQVPAtaaetqallrrAVSFNREEDId 80
Cdd:cd10232 2 VIGISFGNSNSSIAIInKDGRAEVIANEDGD----------------------RQIPS-----------ILAYHGDEEY- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 81 vtpssvqFGLSSLGQYIEDPEEV--YFVkspkSFLGASGLKPQqvamfeDLVCAMMLHIRNQAQSQVPDAITQAVIGRPI 158
Cdd:cd10232 48 -------HGSQAKAQLVRNPKNTvaNFR----DLLGTTTLTVS------EVTTRYLRRLKESAEDYLGKKVTGAVLSVPT 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 550733447 159 NFQglggdEANQQAqgiLERAAHRAGFRDVVFQYEPVAAGLDFEATL------TEEKRVLVVDIGGGTTDCSLL 226
Cdd:cd10232 111 DFT-----EKQKAA---LVAAAAAAGLEVLQLIPEPAAAALAYDLRAetsgdtIKDKTVVVADLGGTRSDVTVV 176
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
3-421 |
6.23e-08 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 54.80 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSmlcaptreaVSEWLFRHHQVPATAAETQAllrravsfnreEDIDVT 82
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPS---------VVRYLEDGIEVGYEARANAA-----------QDPKNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 83 PSSVQ-FglssLGQYIEDPEEVY------FVKSPK---SFLGASGLK-PQQVAmfedlvcAMML-HIRNQAQSQVPDAIT 150
Cdd:PRK05183 82 ISSVKrF----MGRSLADIQQRYphlpyqFVASENgmpLIRTAQGLKsPVEVS-------AEILkALRQRAEETLGGELD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 151 QAVIGRPINFqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAA----GLDFEAtlteEKRVLVVDIGGGTTDCSLL 226
Cdd:PRK05183 151 GAVITVPAYF-----DDAQRQAT---KDAARLAGLNVLRLLNEPTAAaiayGLDSGQ----EGVIAVYDLGGGTFDISIL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 227 LM----------GpqwhhrrdrensllGHSGcrVGGNDLDIALAfkslmpllgmggqtekgialpilpwwnaiaiNDVPA 296
Cdd:PRK05183 219 RLskgvfevlatG--------------GDSA--LGGDDFDHLLA-------------------------------DWILE 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 297 QSDfystangrllndlVRDAQDAEKVALLykvwrqrlsyrvVRTAEESKIALSDRPEHAVTLPfisdDLATAITQEGLEm 376
Cdd:PRK05183 252 QAG-------------LSPRLDPEDQRLL------------LDAARAAKEALSDADSVEVSVA----LWQGEITREQFN- 301
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 550733447 377 ALAQPL-QRILEQVQLALENGKEKPD----VIyLTGGSARSPLIKKALAE 421
Cdd:PRK05183 302 ALIAPLvKRTLLACRRALRDAGVEADevkeVV-MVGGSTRVPLVREAVGE 350
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
3-421 |
8.68e-08 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 54.34 E-value: 8.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLcAPTREA---VSEwlfrhhqvpatAAETQALL------------ 67
Cdd:PRK00290 5 IGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVV-AFTKDGerlVGQ-----------PAKRQAVTnpentifsikrl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 68 --RRavSFNREEDIDVTPSSVqfglsslgqyIEDPEEVYFVKSP-KSFlgasglKPQQVAmfedlvcAMML-HIRNQAQS 143
Cdd:PRK00290 73 mgRR--DEEVQKDIKLVPYKI----------VKADNGDAWVEIDgKKY------TPQEIS-------AMILqKLKKDAED 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 144 QVPDAITQAVIGRPINFqglggDEANQQAQgileRAAHR-AGFrDVV-FQYEPVAA----GLDFEatltEEKRVLVVDIG 217
Cdd:PRK00290 128 YLGEKVTEAVITVPAYF-----NDAQRQAT----KDAGKiAGL-EVLrIINEPTAAalayGLDKK----GDEKILVYDLG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 218 GGTTDCSLLLMGpqwhhrrDRENSLLGHSG-CRVGGNDLD------IALAFKSlmpllgmggqtEKGIalpilpwwnaia 290
Cdd:PRK00290 194 GGTFDVSILEIG-------DGVFEVLSTNGdTHLGGDDFDqriidyLADEFKK-----------ENGI------------ 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 291 indvpaqsdfystangrllnDLVRDaqdaeKVALlykvwrQRLSyrvvRTAEESKIALSDRPEHAVTLPFISDD------ 364
Cdd:PRK00290 244 --------------------DLRKD-----KMAL------QRLK----EAAEKAKIELSSAQQTEINLPFITADasgpkh 288
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550733447 365 LATAITQEGLEmALAQPL-QRILEQVQLALENGKEKP----DVIyLTGGSARSPLIKKALAE 421
Cdd:PRK00290 289 LEIKLTRAKFE-ELTEDLvERTIEPCKQALKDAGLSVsdidEVI-LVGGSTRMPAVQELVKE 348
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
169-265 |
2.71e-07 |
|
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: 52.28 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 169 NQQAQGILERAAHRAGFRD------VVFQYEPVAAGL--------DFEATLTEEKRVLVVDIGGGTTDCSLLlmgpQWHH 234
Cdd:cd10229 152 SDAAKQFMREAAVKAGLISeenseqLIIALEPEAAALycqkllaeGEEKELKPGDKYLVVDCGGGTVDITVH----EVLE 227
|
90 100 110
....*....|....*....|....*....|.
gi 550733447 235 RRDRENSLLGhSGCRVGGNDLDiaLAFKSLM 265
Cdd:cd10229 228 DGKLEELLKA-SGGPWGSTSVD--EEFEELL 255
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
137-427 |
2.96e-07 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 51.91 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 137 IRNQAQSQVPDAITQAVIGRPINFQGLggdeanqqaqgilERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDI 216
Cdd:cd24004 55 LLKELEEKLGSKLKDVVIAIAKVVESL-------------LNVLEKAGLEPVGLTLEPFAAANLLIPYDMRDLNIALVDI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 217 GGGTTDCSLLlmgpqwhhrrdRENSLLGHSGCRVGGNDL--DIALAFKslmpllgmggqtekgialpiLPWWNaiaindv 294
Cdd:cd24004 122 GAGTTDIALI-----------RNGGIEAYRMVPLGGDDFtkAIAEGFL--------------------ISFEE------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 295 paqsdfystangrllndlvrdaqdaekvallykvwrqrlsyrvvrtAEESKIALSDRpehavTLPFISDDLATAITQEGL 374
Cdd:cd24004 164 ----------------------------------------------AEKIKRTYGIF-----LLIEAKDQLGFTINKKEV 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 550733447 375 EMALAQPLQRILEQVQLALE--NGKEK-PDVIYLTGGSARSPLIKKALAEQLpGIP 427
Cdd:cd24004 193 YDIIKPVLEELASGIANAIEeyNGKFKlPDAVYLVGGGSKLPGLNEALAEKL-GLP 247
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
3-260 |
1.28e-06 |
|
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: 50.32 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSML-CAPTREAVSewlfrhhqvpatAAETQALLRRAVSfnreedIDV 81
Cdd:cd10238 3 FGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVaFTDNEKIVG------------LAAKQGLIRNASN------TVV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 82 TPSSVqfglssLGQYIEDPEEVYFVK-SPKSFLGASGL---------KPQQVAMfEDLVCAMMLHIRNQAQSQVPDAITQ 151
Cdd:cd10238 65 RVKQL------LGRSFDDPAVQELKKeSKCKIIEKDGKpgyeieleeKKKLVSP-KEVAKLIFKKMKEIAQSHGGSDVID 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 152 AVIGRPINFqglggDEANQQAqgiLERAAHRAGFRDVVFQYEPVAAGLDFE---ATLTEEKRVLVVDIGGGTTDCSLLL- 227
Cdd:cd10238 138 VVLTVPLDF-----DEDQRNA---LKEAAEKAGFNVLRVISEPSAAALAYGigqDDPTENSNVLVYRLGGTSLDVTVLSv 209
|
250 260 270
....*....|....*....|....*....|....*.
gi 550733447 228 ---MGPQWHHRRDREnsllghsgcrVGGNDLDIALA 260
Cdd:cd10238 210 nngMYRVLATRTDDN----------LGGDDFTEALA 235
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
3-432 |
2.81e-06 |
|
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: 49.16 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLcaptreAVSEwlfRHHQVPATAAETQALL---RRAVSFNREedi 79
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVV------SVDE---DGSILVGRAAKERLVThpdRTAASFKRF--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 80 dvTPSSVQFglsSLGQYIEDPEEvyfvkspksfLGASGLKpqqvAMFEDlvcammlhirnqAQSQVPDAITQAVIGRPIN 159
Cdd:cd10235 69 --MGTDKQY---RLGNHTFRAEE----------LSALVLK----SLKED------------AEAYLGEPVTEAVISVPAY 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 160 FqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAAGLDFE-ATLTEEKRVLVVDIGGGTTDCSLLLMgpqwhhrrdR 238
Cdd:cd10235 118 F-----NDEQRKAT---KDAGELAGLKVERLINEPTAAALAYGlHKREDETRFLVFDLGGGTFDVSVLEL---------F 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 239 ENSLLGHSGC---RVGGNDLDIALAfkslmpllgmggqtekgialpilpwwnaiainDVPAQSdfystangrllNDLVRD 315
Cdd:cd10235 181 EGVIEVHASAgdnFLGGEDFTHALA--------------------------------DYFLKK-----------HRLDFT 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 316 AQDAEKVALLYKvwrqrlsyrvvrTAEESKIALSDrPEHAVTLPFISDDLATA-ITQEGLEMALAQPLQRILEQVQLALE 394
Cdd:cd10235 218 SLSPSELAALRK------------RAEQAKRQLSS-QDSAEIRLTYRGEELEIeLTREEFEELCAPLLERLRQPIERALR 284
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 550733447 395 NGKEKP---DVIYLTGGSARSPLIKKALAEQLPGIPIAGGD 432
Cdd:cd10235 285 DAGLKPsdiDAVILVGGATRMPLVRQLIARLFGRLPLSSLD 325
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
179-428 |
3.18e-06 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 48.93 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 179 AAHRAGFRDVVFQYEPVAA----GLDfeatLTEEKRVLVVDIGGGTTDCSLLlmgpqwhhrrdrenSLLG--HSGC-RVG 251
Cdd:PRK13927 118 SALGAGAREVYLIEEPMAAaigaGLP----VTEPTGSMVVDIGGGTTEVAVI--------------SLGGivYSKSvRVG 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 252 GNDLDialafkslmpllgmggqtekgialpilpwwNAIaINDVpaqsdfystangrllndlvrdaqdaekvallykvwrq 331
Cdd:PRK13927 180 GDKFD------------------------------EAI-INYV------------------------------------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 332 RLSYRVV---RTAEESKIAL-SDRPEHAV-TLPFISDDLATA------ITQEGLEMALAQPLQRILEQVQLALEngKEKP 400
Cdd:PRK13927 192 RRNYNLLigeRTAERIKIEIgSAYPGDEVlEMEVRGRDLVTGlpktitISSNEIREALQEPLSAIVEAVKVALE--QTPP 269
|
250 260 270
....*....|....*....|....*....|....*....
gi 550733447 401 DV--------IYLTGGSArspLIK---KALAEQLpGIPI 428
Cdd:PRK13927 270 ELaadivdrgIVLTGGGA---LLRgldKLLSEET-GLPV 304
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
176-433 |
3.89e-06 |
|
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: 48.56 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 176 LERAAHRAGFRDVVFQYEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSLLlmgpqwhhrrdrenSLLG---HSGCRVGG 252
Cdd:TIGR00904 117 VKESALSAGAREVYLIEEPMAAAIGAGLPVEEPTGSMVVDIGGGTTEVAVI--------------SLGGivvSRSIRVGG 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 253 NDLDIALA--FKSLMPLLgMGGQTEKGIALPIlpwWNAIAINDVPAQSDFystaNGR-LLNDLVRdaqdaekvallykvw 329
Cdd:TIGR00904 183 DEFDEAIInyIRRTYNLL-IGEQTAERIKIEI---GSAYPLNDEPRKMEV----RGRdLVTGLPR--------------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 330 RQRLSYRVVRTaeeskialsdrpehavtlpfisddlataitqeglemALAQPLQRILEQVQLALEngKEKPDV------- 402
Cdd:TIGR00904 240 TIEITSVEVRE------------------------------------ALQEPVNQIVEAVKRTLE--KTPPELaadiver 281
|
250 260 270
....*....|....*....|....*....|....*
gi 550733447 403 -IYLTGGSArspLIK---KALAEQLpGIPIAGGDD 433
Cdd:TIGR00904 282 gIVLTGGGA---LLRnldKLLSKET-GLPVIVADD 312
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
132-433 |
4.87e-06 |
|
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: 48.32 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 132 AMMLHIRNQAQSQVPDAITQAVIGRPInfqglGGDEANQQAqgiLERAAHRAGFRDVVFQYEPVAA----GLD-FEATLT 206
Cdd:pfam06723 76 AMLKYFIKKVHGRRSFSKPRVVICVPS-----GITEVERRA---VKEAAKNAGAREVFLIEEPMAAaigaGLPvEEPTGN 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 207 eekrvLVVDIGGGTTDCSLLLMGpqwhhrrdrenSLLGHSGCRVGGNDLDialafkslmpllgmggqtekgialpilpww 286
Cdd:pfam06723 148 -----MVVDIGGGTTEVAVISLG-----------GIVTSKSVRVAGDEFD------------------------------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 287 NAIaINDVpaqsdfystangrllndlvrdaqdaekvallykvwrqRLSYRVV---RTAEESKIAL-SDRPEHAV-TLPFI 361
Cdd:pfam06723 182 EAI-IKYI-------------------------------------RKKYNLLigeRTAERIKIEIgSAYPTEEEeKMEIR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 362 SDDLATA------ITQEGLEMALAQPLQRILEQVQLALEngKEKPDV--------IYLTGGSARSPLIKKALAEQLpGIP 427
Cdd:pfam06723 224 GRDLVTGlpktieISSEEVREALKEPVSAIVEAVKEVLE--KTPPELaadivdrgIVLTGGGALLRGLDKLLSDET-GLP 300
|
....*.
gi 550733447 428 IAGGDD 433
Cdd:pfam06723 301 VHIAED 306
|
|
| ftsA |
TIGR01174 |
cell division protein FtsA; This bacterial cell division protein interacts with FtsZ, the ... |
176-262 |
1.17e-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: 47.24 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 176 LERAAHRAGFR--DVVFQyePVAAGldfEATLTEEKR---VLVVDIGGGTTDCSLLLmgpqwhhrrdrENSLLgHSGC-R 249
Cdd:TIGR01174 163 LVKCVERCGLEvdNIVLS--GLASA---IAVLTEDEKelgVCLIDIGGGTTDIAVYT-----------GGSIR-YTKViP 225
|
90
....*....|....*
gi 550733447 250 VGGND--LDIALAFK 262
Cdd:TIGR01174 226 IGGNHitKDIAKALR 240
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
3-421 |
1.72e-05 |
|
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: 46.92 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLCAPTRE------AVSEWLfrhHQVPATAAETQALLRRAvsFNRE 76
Cdd:cd24095 4 VGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQrflgeaAAASIL---MNPKNTISQLKRLIGRK--FDDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 77 EdidvtpssVQFGLSSLG-QYIEDPE-----EVYFVKSPKSFlgasglKPQQVAmfedlvcAMML-HIRNQAQSQVPDAI 149
Cdd:cd24095 79 E--------VQRDLKLFPfKVTEGPDgeigiNVNYLGEQKVF------TPEQIL-------AMLLsNLKRIAEKNLKTPV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 150 TQAVIGRPINFqglggdeANQQAQGILErAAHRAGFRDVVFQYEPVAAGLDF-----EATLTEEKRVLVVDIGGGTTDCS 224
Cdd:cd24095 138 TDCVISVPVYF-------TDAQRRAMLD-AAQIAGLNCLRLMNETTATALAYgiyktDLPETDPTNVVFVDVGHSSTQVC 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 225 LLLMgpqwhhrrdRENSL--LGHSGCR-VGGNDLDIALafkslmpllgmggqtekgialpilpwwnaiaindvpaqsdfy 301
Cdd:cd24095 210 VVAF---------KKGQLkvLSHAFDRnLGGRDFDEVL------------------------------------------ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 302 stangrlLNDLVRDAQDAEKVALLYKvwrQRLSYRVVRTAEESKIALSDRPEHAVTLPFISD--DLATAITQEGLEmALA 379
Cdd:cd24095 239 -------FDHFAAEFKEKYKIDVKSN---KKASLRLRAACEKVKKILSANPEAPLNIECLMEdkDVKGMITREEFE-ELA 307
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 550733447 380 QP-LQRILEQVQLALENGKEKPDVIY---LTGGSARSPLIKKALAE 421
Cdd:cd24095 308 APlLERLLEPLEKALADSGLTVDQIHsveVVGSGSRIPAILKILTK 353
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
179-259 |
3.67e-05 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 45.66 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 179 AAHRAGFRDVVFQYEPVAA----GLDfeatLTEEKRVLVVDIGGGTTDCSLLLMGpqwhhrrdrenSLLGHSGCRVGGND 254
Cdd:PRK13928 117 AAEQAGAKKVYLIEEPLAAaigaGLD----ISQPSGNMVVDIGGGTTDIAVLSLG-----------GIVTSSSIKVAGDK 181
|
....*
gi 550733447 255 LDIAL 259
Cdd:PRK13928 182 FDEAI 186
|
|
| ASKHA_NBD_ParM_R1-like |
cd24022 |
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
193-236 |
1.98e-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: 1.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 550733447 193 EPVAAGLDF--------EATLTEEKRVLVVDIGGGTTDCSLLLMGPQWHHRR 236
Cdd:cd24022 150 EGVAAYFDYlldedgngTDEEEEEGPVAVIDIGGTTTDIAVVSGGLSIDHAR 201
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
70-421 |
3.28e-04 |
|
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: 42.75 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 70 AVSFNREEDIDV-------TPSSVQFG---------------------LSSL----GQYIEDPE----EVYF-------- 105
Cdd:cd24094 13 AVARNRGIDIIVnevsnrsTPSLVGFGpksrylgeaaktqetsnfkntVGSLkrliGRTFSDPEvaeeEKYFtaklvdan 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 106 --VKSPKSFLGAsglkpQQVAMFEDLVcAMMLH-IRNQAQSQVPDAITQAVIGRPINFqglggdeANQQAQGILErAAHR 182
Cdd:cd24094 93 geVGAEVNYLGE-----KHVFSATQLA-AMYLGkLKDTTQAELKAPVSDVVISVPGWF-------TDEQRRAILD-AAEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 183 AGFRDVVFQYEPVAAGLDFEATLT-----EEK--RVLVVDIGGGTTDCS--------LLLMGPQWhhrrDREnsllghsg 247
Cdd:cd24094 159 AGLNPLRLMNDTTAAALGYGITKTdlpepEEKprIVAFVDIGHSSYTVSivafkkgqLTVKGTAY----DRH-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 248 crVGGNDLDIALafkslmpllgmggqtekgialpilpwwnaiaindvpaqsdfystangrlLNDLVRDAQDAEKVALLYK 327
Cdd:cd24094 227 --FGGRDFDKAL-------------------------------------------------TDHFADEFKEKYKIDVRSN 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 328 vwrQRLSYRVVRTAEESKIALSDRPEHAVTLPFISDDL-ATA-ITQEGLEMALAQPLQRILEQVQLALENGKEKPDVIY- 404
Cdd:cd24094 256 ---PKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIdVSSmLKREEFEELIAPLLERVTAPLEKALAQAGLTKDEIDf 332
|
410
....*....|....*....
gi 550733447 405 --LTGGSARSPLIKKALAE 421
Cdd:cd24094 333 veLVGGTTRVPALKESISA 351
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
137-442 |
3.87e-04 |
|
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: 42.27 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 137 IRNQAQSQVPDAITQAVIgrpiNFQGLGGDEANQQAQGIL------------ERAAHRAGFRDVVFQYEPVAAG--LDFE 202
Cdd:cd24049 94 IRFEAEQYLPFPLEEVVL----DYQILGEVEEGGEKLEVLvvaapkeivesyLELLKEAGLKPVAIDVESFALAraLEYL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 203 ATLTEEKRVLVVDIGGGTTDCSLLlmgpqwhhrrdRENSLLGHSGCRVGGNDLDIALAfkslmpllgmggqtekgialpi 282
Cdd:cd24049 170 LPDEEEETVALLDIGASSTTLVIV-----------KNGKLLFTRSIPVGGNDITEAIA---------------------- 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 283 lpwwnaiaindvpaqsdfystangrllNDLVRDAQDAEKVallykvwrqrlsyrvvrtaeesKIAlsdrpehavtlpFIS 362
Cdd:cd24049 217 ---------------------------KALGLSFEEAEEL----------------------KRE------------YGL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 363 DDLATAITQEGLEMALAQPLQRILEQVQLALE-----NGKEKPDVIYLTGGSARSPLIKKALAEQLpGIPIAGGDDFGSV 437
Cdd:cd24049 236 LLEGEEGELKKVAEALRPVLERLVSEIRRSLDyyrsqNGGEPIDKIYLTGGGSLLPGLDEYLSERL-GIPVEILNPFSNI 314
|
....*
gi 550733447 438 TAGLA 442
Cdd:cd24049 315 ESKKS 319
|
|
| AnmK |
COG2377 |
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis]; |
387-435 |
1.53e-03 |
|
1,6-Anhydro-N-acetylmuramate kinase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441944 Cd Length: 363 Bit Score: 40.43 E-value: 1.53e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 550733447 387 EQVQLALENGKEKPDVIYLTGGSARSPLIKKALAEQLPGIPIAGGDDFG 435
Cdd:COG2377 275 ASIADAIRRLPPPPDRVLVCGGGAHNPTLMERLQALLPGVPVVTTDELG 323
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
3-226 |
2.17e-03 |
|
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: 40.27 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 3 IGFDYGTANCSVAIMQNGQPQLLKMENGSTLLPSMLC-APTREAVSEwlfrhhqvpatAAETQAllrravSFNREEDI-D 80
Cdd:cd10241 4 IGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAfTDGERLIGD-----------AAKNQA------TSNPENTVfD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 81 V--------TPSSVQFGLSSLGQYIEDPE-----EVYFVKSPKSFlgasglKPQQVAmfedlvcAMML-HIRNQAQSQVP 146
Cdd:cd10241 67 VkrligrkfDDKEVQKDIKLLPFKIVNKNgkpyiQVEVKGEKKTF------APEEIS-------AMVLtKMKETAEAYLG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550733447 147 DAITQAVIGRPINFqglggDEANQQAQgilERAAHRAGFRDVVFQYEPVAA----GLDFEatlTEEKRVLVVDIGGGTTD 222
Cdd:cd10241 134 KKVTHAVVTVPAYF-----NDAQRQAT---KDAGTIAGLNVLRIINEPTAAaiayGLDKK---GGEKNILVFDLGGGTFD 202
|
....
gi 550733447 223 CSLL 226
Cdd:cd10241 203 VSLL 206
|
|
| PilM |
COG4972 |
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures]; |
376-441 |
2.65e-03 |
|
Type IV pilus assembly protein, ATPase PilM [Cell motility, Extracellular structures];
Pssm-ID: 443997 [Multi-domain] Cd Length: 294 Bit Score: 39.45 E-value: 2.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550733447 376 MALAQPLQRILE--QVQlaleNGKEKPDVIYLTGGSARSPLIKKALAEQLpGIPIAGGDDFGSVTAGL 441
Cdd:COG4972 210 FGLAQEIRRSLQfyRSQ----SGGNEVDRILLAGGGAKLPGLAEYLEERL-GIPVEVLNPFAGMALSV 272
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
185-222 |
5.36e-03 |
|
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: 38.66 E-value: 5.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 550733447 185 FRDVVFQYEPVAAGLD--FEATLTEEKRVLVVDIGGGTTD 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; ... |
193-226 |
6.54e-03 |
|
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: 38.76 E-value: 6.54e-03
10 20 30
....*....|....*....|....*....|....*...
gi 550733447 193 EPVAA----GLDfeATLTEEKRVLVVDIGGGTTDCSLL 226
Cdd:cd10233 170 EPTAAaiayGLD--KKGKGERNVLIFDLGGGTFDVSLL 205
|
|
| |
