NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|167466173|ref|NP_005337|]
View 

heat shock 70 kDa protein 1A/1B [Homo sapiens]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
HSPA1-2_6-8-like_NBD cd10233
Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, and similar proteins; This ...
6-381 0e+00

Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, 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). The genes for these three HSPA1 proteins map in close proximity on the major histocompatibility complex (MHC) class III region on chromosome 6, 6p21.3. This subfamily also includes human HSPA8 (heat shock 70kDa protein 8, also known as LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; NIP71; HSPA10; the HSPA8 gene maps to 11q24.1), human HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3, the HSPA2 gene maps to 14q24.1), human HSPA6 (also known as heat shock 70kDa protein 6 (HSP70B') gi 94717614, the HSPA6 gene maps to 1q23.3), human HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B; the HSPA7 gene maps to 1q23.3) and Saccharmoyces cerevisiae Stress-Seventy subfamily B/Ssb1p. 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). Associations of polymorphisms within the MHC-III HSP70 gene locus with longevity, systemic lupus erythematosus, Meniere's disease, noise-induced hearing loss, high-altitude pulmonary edema, and coronary heart disease, have been found. HSPA2 is involved in cancer cell survival, is required for maturation of male gametophytes, and is linked to male infertility. The induction of HSPA6 is a biomarker of cellular stress. HSPA8 participates in the folding and trafficking of client proteins to different subcellular compartments, and in the signal transduction and apoptosis process; it has been shown to protect cardiomyocytes against oxidative stress partly through an interaction with alpha-enolase. S. cerevisiae Ssb1p, is part of the ribosome-associated complex (RAC), it acts as a chaperone for nascent polypeptides, and is important for translation fidelity; Ssb1p is also a [PSI+] prion-curing factor.


:

Pssm-ID: 212675  Cd Length: 376  Bit Score: 889.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:cd10233    1 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFSDPVVQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd10233   81 DMKHWPFKVVNGGGKPPIIVEYKGETKTFYPEEISSMVLTKMKEIAEAYLGKTVTNAVITVPAYFNDSQRQATKDAGTIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:cd10233  161 GLNVLRIINEPTAAAIAYGLDKKGGGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAK 325
Cdd:cd10233  241 KRKHKKDISGNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRGTLEPVEKVLRDAK 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 167466173 326 LDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILM 381
Cdd:cd10233  321 LDKSQIHDIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILS 376
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
1-611 0e+00

heat shock 70 kDa protein; Provisional


:

Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 1159.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGD 80
Cdd:PTZ00009   1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  81 PVVQSDMKHWPFQVINDG-DKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATK 159
Cdd:PTZ00009  81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 160 DAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHK-KDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:PTZ00009 241 FCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAP 398
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 399 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTF 478
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 479 DIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGL 558
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|...
gi 167466173 559 KGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:PTZ00009 561 KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMY 613
 
Name Accession Description Interval E-value
HSPA1-2_6-8-like_NBD cd10233
Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, and similar proteins; This ...
6-381 0e+00

Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, 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). The genes for these three HSPA1 proteins map in close proximity on the major histocompatibility complex (MHC) class III region on chromosome 6, 6p21.3. This subfamily also includes human HSPA8 (heat shock 70kDa protein 8, also known as LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; NIP71; HSPA10; the HSPA8 gene maps to 11q24.1), human HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3, the HSPA2 gene maps to 14q24.1), human HSPA6 (also known as heat shock 70kDa protein 6 (HSP70B') gi 94717614, the HSPA6 gene maps to 1q23.3), human HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B; the HSPA7 gene maps to 1q23.3) and Saccharmoyces cerevisiae Stress-Seventy subfamily B/Ssb1p. 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). Associations of polymorphisms within the MHC-III HSP70 gene locus with longevity, systemic lupus erythematosus, Meniere's disease, noise-induced hearing loss, high-altitude pulmonary edema, and coronary heart disease, have been found. HSPA2 is involved in cancer cell survival, is required for maturation of male gametophytes, and is linked to male infertility. The induction of HSPA6 is a biomarker of cellular stress. HSPA8 participates in the folding and trafficking of client proteins to different subcellular compartments, and in the signal transduction and apoptosis process; it has been shown to protect cardiomyocytes against oxidative stress partly through an interaction with alpha-enolase. S. cerevisiae Ssb1p, is part of the ribosome-associated complex (RAC), it acts as a chaperone for nascent polypeptides, and is important for translation fidelity; Ssb1p is also a [PSI+] prion-curing factor.


Pssm-ID: 212675  Cd Length: 376  Bit Score: 889.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:cd10233    1 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFSDPVVQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd10233   81 DMKHWPFKVVNGGGKPPIIVEYKGETKTFYPEEISSMVLTKMKEIAEAYLGKTVTNAVITVPAYFNDSQRQATKDAGTIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:cd10233  161 GLNVLRIINEPTAAAIAYGLDKKGGGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAK 325
Cdd:cd10233  241 KRKHKKDISGNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRGTLEPVEKVLRDAK 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 167466173 326 LDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILM 381
Cdd:cd10233  321 LDKSQIHDIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILS 376
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
1-611 0e+00

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 1159.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGD 80
Cdd:PTZ00009   1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  81 PVVQSDMKHWPFQVINDG-DKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATK 159
Cdd:PTZ00009  81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 160 DAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHK-KDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:PTZ00009 241 FCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAP 398
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 399 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTF 478
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 479 DIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGL 558
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|...
gi 167466173 559 KGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:PTZ00009 561 KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMY 613
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
6-611 0e+00

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 249507 [Multi-domain]  Cd Length: 598  Bit Score: 1002.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173    6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:pfam00012   1 VIGIDLGTTNSCVAVMEGGGPEVIANDEGNRTTPSVVAFTPKERLVGQAAKRQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   86 DMKHWPFQVINDGD-KPKVQVSYKGETkaFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:pfam00012  81 DIKHVPYKVVKLPNgDAGVEVRYLGET--FTPEQISAMVLQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGRI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  165 AGLNVLRIINEPTAAAIAYGLDRTGKgERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:pfam00012 159 AGLNVLRIINEPTAAALAYGLDKKDK-ERNVLVFDLGGGTFDVSILEIGDGVFEVLATNGDTHLGGEDFDNRLVDHFVEE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFE-GIDFYTSITRARFEELCSDLFRSTLEPVEKALR 322
Cdd:pfam00012 238 FKKKYGIDLSKDPRALQRLREAAEKAKIELSSnQTEINLPFITAMAdGKDVSGTLTRAKFEELCADLFERTLEPVEKALK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  323 DAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksENVQDLLLLDVAPLSLG 402
Cdd:pfam00012 318 DAKLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKTVNPDEAVAIGAAVQAGVLSGT--FDVKDVLLLDVTPLSLG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  403 LETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDA 482
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  483 NGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGlkGKI 562
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQKITITNSSG-LSDDEIERMVKDAEEYAAEDKKRKERIEAKNEAEEYVYSLEKSLKEEG--DKL 551
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 167466173  563 SEADKKKVldkcQEVISWLDANTLAE-KDEFEHKRKELEQVCNPIISGLY 611
Cdd:pfam00012 552 PEADKKKV----EEAIEWLKEELEGEdKEEIEAKTEELQKVVQPIGERMY 597
dnaK PRK00290
molecular chaperone DnaK; Provisional
1-611 0e+00

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 870.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAaaIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKfg 79
Cdd:PRK00290   1 MGKI--IGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  80 DPVVQSDMKHWPFQVIN-DGDKPKVQVsykgETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQAT 158
Cdd:PRK00290  77 DEEVQKDIKLVPYKIVKaDNGDAWVEI----DGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQAT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 159 KDAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLV 238
Cdd:PRK00290 153 KDAGKIAGLEVLRIINEPTAAALAYGLDK--KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRII 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 239 NHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRS 312
Cdd:PRK00290 231 DYLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQT--EINLPFITADasgpkhLEIKLTRAKFEELTEDLVER 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 313 TLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLL 392
Cdd:PRK00290 309 TIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVL 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 393 LLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVP 472
Cdd:PRK00290 384 LLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVP 463
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 473 QIEVTFDIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSA 552
Cdd:PRK00290 464 QIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKT 542
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167466173 553 VEDegLKGKISEADKKKVLDKCQEVISWLDANtlaEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:PRK00290 543 LKE--LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMY 596
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
6-611 0e+00

chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved [Protein fate, Protein folding and stabilization].


Pssm-ID: 233830 [Multi-domain]  Cd Length: 595  Bit Score: 802.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173    6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGdpVVQ 84
Cdd:TIGR02350   2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   85 SDMKHWPFQVINDGDKPKVQVsykgETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:TIGR02350  80 EEAKRVPYKVVGDGGDVRVKV----DGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  165 AGLNVLRIINEPTAAAIAYGLDRTGKGERnVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLST--EINLPFITADasgpkhLEMTLTRAKFEELTADLVERTKEPVR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAP 398
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTP 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  399 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTF 478
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  479 DIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegL 558
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE--A 544
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 167466173  559 KGKISEADKKKVLDKCQEVISWLDANTlaeKDEFEHKRKELEQVCNPIISGLY 611
Cdd:TIGR02350 545 GDKLPAEEKEKIEKAVAELKEALKGED---VEEIKAKTEELQQALQKLAEAMY 594
DnaK COG0443
Molecular chaperone [Posttranslational modification, protein turnover, chaperones]
1-611 0e+00

Molecular chaperone [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 223520 [Multi-domain]  Cd Length: 579  Bit Score: 732.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAA-AIGIDLGTTYSCVGVFQHG-KVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVALNPQNTVFDAKRLIGRK 77
Cdd:COG0443    1 MSTAKkAIGIDLGTTNSVVAVMRGGgLPKVIENAEGERLTPSVVAFSkNGEVLVGQAAKRQAVDNPENTIFSIKRKIGRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  78 fgdpvvqsdmkhwpfqviNDGDKPKVQVSykgeTKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQA 157
Cdd:COG0443   81 ------------------SNGLKISVEVD----GKKYTPEEISAMILTKLKEDAEAYLGEKVTDAVITVPAYFNDAQRQA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 158 TKDAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRL 237
Cdd:COG0443  139 TKDAARIAGLNVLRLINEPTAAALAYGLDK--GKEKTVLVYDLGGGTFDVSLLEIGDGVFEVLATGGDNHLGGDDFDNAL 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 238 VNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPV 317
Cdd:COG0443  217 IDYLVMEFKGKGGIDLRSDKAALQRLREAAEKAKIELSSATQTSINLPSIGGDIDLLKELTRAKFEELILDLLERTIEPV 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 318 EKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSenvqDLLLLDVA 397
Cdd:COG0443  297 EQALKDAGLEKSDIDLVILVGGSTRIPAVQELVKEFF-GKEPEKSINPDEAVALGAAIQAAVLSGEVP----DVLLLDVI 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 398 PLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVT 477
Cdd:COG0443  372 PLSLGIETLGGVRTPIIERNTTIPVKKSQEFSTAADGQTAVAIHVFQGEREMAADNKSLGRFELDGIPPAPRGVPQIEVT 451
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 478 FDIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEg 557
Cdd:COG0443  452 FDIDANGILNVTAKDLGTGKEQSITIKASSG-LSDEEIERMVEDAEANAALDKKFRELVEARNEAESLIYSLEKALKEI- 529
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167466173 558 lkGKISEADKKKVLDKCQEVISWLDantlAEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:COG0443  530 --VKVSEEEKEKIEEAITDLEEALE----GEKEEIKAKIEELQEVTQKLAEKKY 577
dnaK CHL00094
heat shock protein 70
1-602 0e+00

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 702.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAaaIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFG 79
Cdd:CHL00094   1 MGKV--VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  80 DpvVQSDMKHWPFQVINDG-DKPKVQVSYKGetKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQAT 158
Cdd:CHL00094  79 E--ISEEAKQVSYKVKTDSnGNIKIECPALN--KDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQAT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 159 KDAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLV 238
Cdd:CHL00094 155 KDAGKIAGLEVLRIINEPTAASLAYGLDK--KNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 239 NHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLE---IDSLFEG-IDFYTSITRARFEELCSDLFRSTL 314
Cdd:CHL00094 233 NWLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 315 EPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLL 394
Cdd:CHL00094 313 IPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLL 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 395 DVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQI 474
Cdd:CHL00094 388 DVTPLSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQI 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 475 EVTFDIDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVE 554
Cdd:CHL00094 468 EVTFDIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLK 546
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 167466173 555 DegLKGKISEADKKKVldkcQEVISWLDANTlaEKDEFEHKRKELEQV 602
Cdd:CHL00094 547 E--LKDKISEEKKEKI----ENLIKKLRQAL--QNDNYESIKSLLEEL 586
PLN03184 PLN03184
chloroplast Hsp70; Provisional
7-602 0e+00

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 630.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQS 85
Cdd:PLN03184  42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQVINDgDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:PLN03184 120 ESKQVSYRVVRD-ENGNVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIA 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:PLN03184 199 GLEVLRIINEPTAASLAYGFEK--KSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNF 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLE---IDSLFEG---IDfyTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:PLN03184 277 KKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPVEN 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFfNGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAPL 399
Cdd:PLN03184 355 ALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTPL 429
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 400 SLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFD 479
Cdd:PLN03184 430 SLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFD 509
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 480 IDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegLK 559
Cdd:PLN03184 510 IDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--LG 586
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....
gi 167466173 560 GKISEADKKKVLDKCQEVISWLDA-NTLAEKDEFEHKRKELEQV 602
Cdd:PLN03184 587 DKVPADVKEKVEAKLKELKDAIASgSTQKMKDAMAALNQEVMQI 630
 
Name Accession Description Interval E-value
HSPA1-2_6-8-like_NBD cd10233
Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, and similar proteins; This ...
6-381 0e+00

Nucleotide-binding domain of HSPA1-A, -B, -L, HSPA-2, -6, -7, -8, 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). The genes for these three HSPA1 proteins map in close proximity on the major histocompatibility complex (MHC) class III region on chromosome 6, 6p21.3. This subfamily also includes human HSPA8 (heat shock 70kDa protein 8, also known as LAP1; HSC54; HSC70; HSC71; HSP71; HSP73; NIP71; HSPA10; the HSPA8 gene maps to 11q24.1), human HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3, the HSPA2 gene maps to 14q24.1), human HSPA6 (also known as heat shock 70kDa protein 6 (HSP70B') gi 94717614, the HSPA6 gene maps to 1q23.3), human HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B; the HSPA7 gene maps to 1q23.3) and Saccharmoyces cerevisiae Stress-Seventy subfamily B/Ssb1p. 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). Associations of polymorphisms within the MHC-III HSP70 gene locus with longevity, systemic lupus erythematosus, Meniere's disease, noise-induced hearing loss, high-altitude pulmonary edema, and coronary heart disease, have been found. HSPA2 is involved in cancer cell survival, is required for maturation of male gametophytes, and is linked to male infertility. The induction of HSPA6 is a biomarker of cellular stress. HSPA8 participates in the folding and trafficking of client proteins to different subcellular compartments, and in the signal transduction and apoptosis process; it has been shown to protect cardiomyocytes against oxidative stress partly through an interaction with alpha-enolase. S. cerevisiae Ssb1p, is part of the ribosome-associated complex (RAC), it acts as a chaperone for nascent polypeptides, and is important for translation fidelity; Ssb1p is also a [PSI+] prion-curing factor.


Pssm-ID: 212675  Cd Length: 376  Bit Score: 889.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:cd10233    1 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFSDPVVQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd10233   81 DMKHWPFKVVNGGGKPPIIVEYKGETKTFYPEEISSMVLTKMKEIAEAYLGKTVTNAVITVPAYFNDSQRQATKDAGTIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:cd10233  161 GLNVLRIINEPTAAAIAYGLDKKGGGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAK 325
Cdd:cd10233  241 KRKHKKDISGNKRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRGTLEPVEKVLRDAK 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 167466173 326 LDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILM 381
Cdd:cd10233  321 LDKSQIHDIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILS 376
HSPA5-like_NBD cd10241
Nucleotide-binding domain of human HSPA5 and similar proteins; This subfamily includes human ...
7-378 0e+00

Nucleotide-binding domain of human HSPA5 and similar proteins; This subfamily includes human HSPA5 (also known as 70-kDa heat shock protein 5, glucose-regulated protein 78/GRP78, and immunoglobulin heavy chain-binding protein/BIP, MIF2; the gene encoding HSPA5 maps to 9q33.3.), Sacchaormyces cerevisiae Kar2p (also known as Grp78p), and related proteins. 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. HSPA5 and Kar2p are chaperones of the endoplasmic reticulum (ER). 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). Multiple ER DNAJ domain proteins have been identified and may exist in distinct complexes with HSPA5 in various locations in the ER, for example DNAJC3-p58IPK in the lumen. HSPA5-NEFs include SIL1 and an atypical HSP70 family protein HYOU1/ORP150. The ATPase activity of Kar2p is stimulated by the NEFs: Sil1p and Lhs1p.


Pssm-ID: 212681  Cd Length: 374  Bit Score: 715.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSD 86
Cdd:cd10241    4 IGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTIFDVKRLIGRKFDDKEVQKD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  87 MKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAG 166
Cdd:cd10241   84 IKLLPYKVVNKDGKPYIEVDVKGEKKTFSPEEISAMVLTKMKEIAEAYLGKKVKHAVVTVPAYFNDAQRQATKDAGTIAG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 167 LNVLRIINEPTAAAIAYGLDRTGkGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFK 246
Cdd:cd10241  164 LNVVRIINEPTAAAIAYGLDKKG-GEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMEHFIKLFK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 247 RKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKL 326
Cdd:cd10241  243 KKHGKDISKDKRALQKLRREVEKAKRALSSQHQTRIEIESLFDGEDFSETLTRAKFEELNMDLFKKTLKPVKKVLEDADL 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167466173 327 DKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAA 378
Cdd:cd10241  323 KKSDIDEIVLVGGSTRIPKVQQLLKEFFNGKEPSRGINPDEAVAYGAAVQAG 374
HSP70_NBD cd10170
Nucleotide-binding domain of the HSP70 family; HSP70 (70-kDa heat shock protein) family ...
7-378 0e+00

Nucleotide-binding domain 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.


Pssm-ID: 212667 [Multi-domain]  Cd Length: 369  Bit Score: 534.88  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQ-HGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd10170    1 IGIDLGTTNSAVAYVDnGGKPEIIPNGEGSRTTPSVVYFDGDgEVLVGEAAKRQALDNPENTVGDFKRLIGRKFDDPLVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  85 SDMKHwpfqVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:cd10170   81 SAKKV----IGVDRGAPIIPVPVELGGKKYSPEEVSALILKKLKEDAEAYLGEPVTEAVITVPAYFNDAQREATKEAAEI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:cd10170  157 AGLNVVRLINEPTAAALAYGLDKKDEKGRTILVFDLGGGTFDVSLVEVEGGVFEVLATGGDNHLGGDDFDNALADYLAEK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:cd10170  237 FKEKGGIDLRLDPRALRRLKEAAEKAKIALSSSEEATITLPGLGSGGDLEVELTREEFEELIRPLLERTIDLVERVLADA 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167466173 325 KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAA 378
Cdd:cd10170  317 GLKPEDIDAVLLVGGSSRIPLVRELLEELF-GKKPLRSIDPDEAVALGAAIYAA 369
HSPA9-Ssq1-like_NBD cd10234
Nucleotide-binding domain of human HSPA9 and similar proteins; This subfamily includes human ...
1-380 0e+00

Nucleotide-binding domain of human HSPA9 and similar proteins; This subfamily includes human mitochondrial HSPA9 (also known as 70-kDa heat shock protein 9, CSA; MOT; MOT2; GRP75; PBP74; GRP-75; HSPA9B; MTHSP75; the gene encoding HSPA9 maps to 5q31.1), Escherichia coli DnaK, Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p, Ssh1p, mtHSP70 homolog), and S. cerevisiae Stress-Seventy subfamily C/Ssc1p (also called mtHSP70, Endonuclease SceI 75 kDa subunit). 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); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.


Pssm-ID: 212676 [Multi-domain]  Cd Length: 376  Bit Score: 521.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAaaIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFG 79
Cdd:cd10234    1 MGKI--IGIDLGTTNSCVAVMEGGEPTVIPNAEGSRTTPSVVAFTKKgERLVGQPAKRQAVTNPENTIFSIKRFMGRKFD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  80 DPVVQSDMKHWPFQVINDGDKPKVQVSykgeTKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATK 159
Cdd:cd10234   79 EVEEERKVPYKVVVDEGGNYKVEIDSN----GKDYTPQEISAMILQKLKEDAEAYLGEKVTEAVITVPAYFNDSQRQATK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 160 DAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:cd10234  155 DAGKIAGLEVLRIINEPTAAALAYGLDK--KGNEKILVYDLGGGTFDVSILEIGDGVFEVLATNGDTHLGGDDFDQRIID 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRST 313
Cdd:cd10234  233 WLVEEFKKEEGIDLRKDKMALQRLKEAAEKAKIELSSVTET--EINLPFITADatgpkhLEMTLTRAKFEELTEDLVERT 310
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466173 314 LEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10234  311 IEPVKQALKDAKLSPSDIDEVILVGGSTRIPAVQELVKELF-GKEPNKGVNPDEVVAIGAAIQGGVL 376
HSPA9-like_NBD cd11733
Nucleotide-binding domain of human HSPA9, Escherichia coli DnaK, and similar proteins; This ...
3-380 2.64e-173

Nucleotide-binding domain of human HSPA9, Escherichia coli DnaK, and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as 70-kDa heat shock protein 9, CSA; MOT; MOT2; GRP75; PBP74; GRP-75; HSPA9B; MTHSP75; the gene encoding HSPA9 maps to 5q31.1), Escherichia coli DnaK, and Saccharomyces cerevisiae Stress-Seventy subfamily C/Ssc1p (also called mtHSP70, Endonuclease SceI 75 kDa subunit). 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); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively. HSPA9 is involved in multiple processses including mitochondrial import, antigen processing, control of cellular proliferation and differentiation, and regulation of glucose responses. During glucose deprivation-induced cellular stress, HSPA9 plays an important role in the suppression of apoptosis by inhibiting a conformational change in Bax that allow the release of cytochrome c. DnaK modulates the heat shock response in Escherichia coli. It protects E. coli from protein carbonylation, an irreversible oxidative modification that increases during organism aging and bacterial growth arrest. Under severe thermal stress, it functions as part of a bi-chaperone system: the DnaK system and the ring-forming AAA+ chaperone ClpB (Hsp104) system, to promote cell survival. DnaK has also been shown to cooperate with GroEL and the ribosome-associated Escherichia coli Trigger Factor in the proper folding of cytosolic proteins. S. cerevisiae Ssc1p is the major HSP70 chaperone of the mitochondrial matrix, promoting translocation of proteins from the cytosol, across the inner membrane, to the matrix, and their subsequent folding. Ssc1p interacts with Tim44, a peripheral inner membrane protein associated with the TIM23 protein translocase. It is also a subunit of the endoSceI site-specific endoDNase and is required for full endoSceI activity. Ssc1p plays roles in the import of Yfh1p, a nucleus-encoded mitochondrial protein involved in iron homeostasis (and a homolog of human frataxin, implicated in the neurodegenerative disease, Friedreich's ataxia). Ssc1 also participates in translational regulation of cytochrome c oxidase (COX) biogenesis by interacting with Mss51 and Mss51-containing complexes.


Pssm-ID: 212683  Cd Length: 377  Bit Score: 501.52  E-value: 2.64e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   3 KAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDP 81
Cdd:cd11733    1 KGAVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTkDGERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  82 VVQSDMKHWPFQVI--NDGDkpkVQVSYKGetKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATK 159
Cdd:cd11733   81 EVQKDIKNVPYKIVkaSNGD---AWVEAHG--KKYSPSQIGAFVLMKMKETAEAYLGKPVKNAVITVPAYFNDSQRQATK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 160 DAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:cd11733  156 DAGQIAGLNVLRVINEPTAAALAYGLDK--KDDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTFLGGEDFDNALLR 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRST 313
Cdd:cd11733  234 HLVKEFKKEQGIDLTKDNMALQRLREAAEKAKIELSSSLQT--DINLPYITADasgpkhLNMKLTRAKFESLVGDLIKRT 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466173 314 LEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11733  312 IEPCKKALKDAGVSKSDIGEVILVGGMTRMPKVQETVKEIF-GKEPSKGVNPDEAVAIGAAIQGGVL 377
Ssq1_like_NBD cd11734
Nucleotide-binding domain of Saccharomyces cerevisiae Ssq1 and similar proteins; Ssq1p (also ...
7-380 2.02e-159

Nucleotide-binding domain of Saccharomyces cerevisiae Ssq1 and similar proteins; Ssq1p (also called Stress-seventy subfamily Q protein 1, Ssc2p, Ssh1p, mtHSP70 homolog) 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). S. cerevisiae Ssq1p is a mitochondrial chaperone that is involved in iron-sulfur (Fe/S) center biogenesis. Ssq1p plays a role in the maturation of Yfh1p, a nucleus-encoded mitochondrial protein involved in iron homeostasis (and a homolog of human frataxin, implicated in the neurodegenerative disease, Friedreich's ataxia).


Pssm-ID: 212684 [Multi-domain]  Cd Length: 373  Bit Score: 465.83  E-value: 2.02e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSD 86
Cdd:cd11734    5 IGIDLGTTNSCVAVIDKTTPVIIENAEGKRTTPSIVSFTKTGILVGEAAKRQEALHPENTFFATKRLIGRQFKDVEVQRK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  87 MKHWPFQVInDGDKPKVQVSYKGetKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAG 166
Cdd:cd11734   85 MKVPYYKIV-EGRNGDAWIYTNG--KKYSPSQIASFVLKKLKKTAEAYLGKRVDEAVITVPAYFNDSQRQATKDAGTLAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 167 LNVLRIINEPTAAAIAYGLDrTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFK 246
Cdd:cd11734  162 LKVLRIINEPTAAALAYGID-KRKENKNIAVYDLGGGTFDISILNIEDGVFEVKATNGDTMLGGEDFDNAIVQYIIKEFK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 247 RKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKL 326
Cdd:cd11734  241 RKYKIDLTRNKKAIQRIKEAAEKAKIELSSSEESVIELPYLDGPKHLRITITRREFEQLRKSICKRTIYPCKQCLKDAGL 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167466173 327 DKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11734  321 RKKDIDEVILVGGMTRMPYIQNVVQEIF-GKKPSKSVNPDEAVALGAAIQGSIL 373
HSPA4_like_NDB cd10228
Nucleotide-binding domain of 105/110 kDa heat shock proteins including HSPA4 and similar ...
5-380 3.30e-155

Nucleotide-binding domain of 105/110 kDa heat shock proteins including HSPA4 and similar proteins; This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4, APG-2, HS24/P52, hsp70 RY, and HSPH2; the human HSPA4 gene maps to 5q31.1), HSPA4L (also known as 70-kDa heat shock protein 4-like, APG-1, HSPH3, and OSP94; the human HSPA4L gene maps to 4q28), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1, HSP105; HSP105A; HSP105B; NY-CO-25; the human HSPH1 gene maps to 13q12.3), Saccharomyces cerevisiae Sse1p and Sse2p, and a sea urchin sperm receptor. It belongs 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: 212670  Cd Length: 381  Bit Score: 455.45  E-value: 3.30e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd10228    1 SVVGIDFGNLNSVVAVARKGGIDVVANEYSNRETPSLVSFGEKQRLIGEAAKNQAISNFKNTVRNFKRLIGRKFDDPEVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  85 SDMKHWPFQVI-NDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGV 163
Cdd:cd10228   81 KELKFLPFKVVeLPDGKVGIKVNYLGEEKVFSPEQVLAMLLTKLKEIAEKALKGKVTDCVISVPSYFTDAQRRALLDAAQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGLDRTGKGE----RNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:cd10228  161 IAGLNCLRLMNETTATALAYGIYKTDLPEeekpRNVAFVDIGHSSTQVSIVAFNKGKLKVLSTAFDRNLGGRDFDEALFE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:cd10228  241 HFAKEFKEKYKIDVLSNPKARLRLLAACEKLKKVLSANTEAPLNIECLMEDKDVSGKIKREEFEELCAPLLERVEEPLEK 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd10228  321 ALAEAGLTKEDIHSVEIVGGSTRIPAVKELIAKVF-GKELSTTLNADEAVARGCALQCAML 380
HscC_like_NBD cd10235
Nucleotide-binding domain of Escherichia coli HscC and similar proteins; This subfamily ...
7-378 2.91e-135

Nucleotide-binding domain of Escherichia coli HscC and similar proteins; This subfamily includes Escherichia coli HscC (also called heat shock cognate protein C, Hsc62, or YbeW) and the the putative DnaK-like protein Escherichia coli ECs0689. 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). 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: 212677 [Multi-domain]  Cd Length: 339  Bit Score: 402.65  E-value: 2.91e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTER-LIGDAAKNQVALNPQNTVFDAKRLIGrkfgdpvvqS 85
Cdd:cd10235    1 IGIDLGTTNSLVAVWQDGKARLIPNALGEYLTPSVVSVDEDGEiLVGKAARERLITHPDLTAASFKRFMG---------T 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKhwpfqvindgdkpkvqvsYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd10235   72 DKK------------------YRLGKREFRAEELSSLVLRSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKRAGELA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDrTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLvnhfVEEF 245
Cdd:cd10235  134 GLKVERLINEPTAAALAYGLH-DKDEETKFLVFDLGGGTFDVSVLELFDGVMEVRASAGDNYLGGEDFTRAL----AEAF 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDI-SQNKRAVRRLRTACERAKRTLSSSTQASLEIDslFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:cd10235  209 LKKHGLDFeKLDPSELARLLRAAERAKRALSDQEEAEMSVR--IEGEELEYTLTREEFEEICQPLLERLRQPIERALRDA 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167466173 325 KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAA 378
Cdd:cd10235  287 RLKPSDIDEIILVGGATRMPVVRKLVSRLF-GRFPLVHLNPDEVVALGAAIQAG 339
HSPA14-like_NBD cd10238
Nucleotide-binding domain of human HSPA14 and similar proteins; Human HSPA14 (also known as ...
5-378 2.13e-129

Nucleotide-binding domain of human HSPA14 and similar proteins; Human HSPA14 (also known as 70-kDa heat shock protein 14, HSP70L1, HSP70-4; the gene encoding HSPA14 maps to 10p13), is ribosome-associated and 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). HSPA14 interacts with the J-protein MPP11 to form the mammalian ribosome-associated complex (mRAC). HSPA14 participates in a pathway along with Nijmegen breakage syndrome 1 (NBS1, also known as p85 or nibrin), heat shock transcription factor 4b (HSF4b), and HSPA4 (belonging to a different subfamily), that induces tumor migration, invasion, and transformation. HSPA14 is a potent T helper cell (Th1) polarizing adjuvant that contributes to antitumor immune responses.


Pssm-ID: 212680  Cd Length: 375  Bit Score: 388.67  E-value: 2.13e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd10238    1 AAIGVHFGNTSACLAVYKDGRADVVANDAGDRVTPAVVAFTDTEVIVGLAAKQGRIRNAANTIVKNKQILGRSYSDPFKQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  85 SDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:cd10238   81 KEKTESSCKIIEKDGEPKYEIFTEEKTKHVSPKEVAKLIFKKMKEIAQSALGSDSKDVVITVPVYFSEKQKLALREAAEE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGK-GERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVE 243
Cdd:cd10238  161 AGFNVLRIIHEPSAAALAYGIGQDSPtGKSYVLVYRLGGTSTDVTILRVNSGMYRVLATSTDDNLGGESFTETLSQYLAN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 244 EFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRD 323
Cdd:cd10238  241 EFKRKWKQDVRGNARAMMKLNNAAEVAKQILSTLPSANCFVESLYEGIDFQCSVSRARFESLCSSLFPKCLEPIEKVLEQ 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 167466173 324 AKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAA 378
Cdd:cd10238  321 ANLTKTDINKVVLCGGSSRIPKLQQLIKDLFPSVEVLNSISPDEVIAIGAAKQAG 375
HscA_like_NBD cd10236
Nucleotide-binding domain of HscA and similar proteins; Escherichia coli HscA (heat shock ...
6-377 3.14e-125

Nucleotide-binding domain of HscA and similar proteins; Escherichia coli HscA (heat shock cognate protein A, also called Hsc66), 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). 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: 212678 [Multi-domain]  Cd Length: 355  Bit Score: 377.32  E-value: 3.14e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQS 85
Cdd:cd10236    2 AIGIDLGTTNSLVASVLSGKVKILPDENGRVLLPSVVHYGDGGISVGHDALKLAISDPKNTISSVKRLMGKSIED--IKK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQVINDGDKPKVQVSYKGETkafyPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd10236   80 SFPYLPILEGKNGGIILFHTQQGTVT----PVEVSAEILKALKERAEKSLGGEIKGAVITVPAYFDDAQRQATKDAARLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEef 245
Cdd:cd10236  156 GLNVLRLLNEPTAAALAYGLDK--KKEGIYAVYDLGGGTFDVSILKLHKGVFEVLATGGDSALGGDDFDQLLAELLLK-- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 krKHKKDISQNKRAVRRLRTACERAKRTLSSSTQasLEIDslfeGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAK 325
Cdd:cd10236  232 --KYGLKSLISDEDQAELLLIARKAKEALSGAEE--VEVR----GQDFKCTITREEFEKLIDPLVKKTLNICKQALRDAG 303
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 167466173 326 LDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNkSINPDEAVAYGAAVQA 377
Cdd:cd10236  304 LSVKDIKGVILVGGSTRIPLVQEAVSKFFGQKPLC-DINPDEVVAIGAALQA 354
HSPA13-like_NBD cd10237
Nucleotide-binding domain of human HSPA13 and similar proteins; Human HSPA13 (also called ...
7-382 3.30e-122

Nucleotide-binding domain of human HSPA13 and similar proteins; Human HSPA13 (also called 70-kDa heat shock protein 13, STCH, "stress 70 protein chaperone, microsome-associated, 60kD", "stress 70 protein chaperone, microsome-associated, 60kDa"; the gene encoding HSPA13 maps to 21q11.1) 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). STCH contains an NBD but lacks an SBD. STCH 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: 212679 [Multi-domain]  Cd Length: 417  Bit Score: 371.80  E-value: 3.30e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQ--HGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd10237   23 IGIDLGTTYSSVGVYQagTGETDIIPDENGRKSIPSVVAFTPGTVLVGYKAVEQAEHNPQNTIYDAKRFIGKIFTKEELE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  85 SDMKHWPFQVIND-GDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGV 163
Cdd:cd10237  103 FESDRYRFKVKINsRNGAFFFSVLTNETKTVTPEEIGSRLILKLRKMAEKYLGTPVGKAVISVPAEFDEKQRNATVKAAN 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGLDRTgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVE 243
Cdd:cd10237  183 LAGLEVLRVINEPTAAALAYGLHKK-QDVFNVLVVDLGGGTLDVSLLNKQGGMFLTRAMAGNNRLGGQDFNQRLLQYLYQ 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 244 EFKRKHKKDISqNKRAVRRLRTACERAK--RTLSSSTQASLEIDSLFEG---IDFYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:cd10237  262 KIYEKYGKVPD-NKEDIQRLRQAVEAAKinLTLHPSTTISLNLTLLSEGesiVKFEYELTRDEFETLNEDLFQKILLPIE 340
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466173 319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMG 382
Cdd:cd10237  341 AVLAEGHLDKEEVDEIVLVGGSTRIPRIRQVIGRFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 403
HYOU1-like_NBD cd10230
Nucleotide-binding domain of human HYOU1 and similar proteins; This subgroup includes human ...
7-378 3.40e-114

Nucleotide-binding domain of human HYOU1 and similar proteins; This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, GRP170; HSP12A; ORP150; GRP-170; ORP-150; the human HYOU1 gene maps to11q23.1-q23.3) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (alos known as BiP, Grp78 or HspA5) and may also function 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. This subgroup belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as 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: 212672  Cd Length: 388  Bit Score: 349.94  E-value: 3.40e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGK-VEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:cd10230    1 LGIDLGSEWIKVALVKPGVpFEIVLNEESKRKTPSAVAFKGGERLFGSDASSLAARFPQQVYLHLKDLLGKPADDPSVSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQVINDGDKPK-VQVSYKGETkAFYPEEISSMVLTKMKEIAEAYLG-YPVTNAVITVPAYFNDSQRQATKDAGV 163
Cdd:cd10230   81 YQSRHPLPYLVVDESRGtVAFKISDGE-EYSVEELVAMILNYAKKLAEEHAKeAPVKDVVITVPPYFTQAQRQALLDAAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGLDRTGKGER--NVLIFDLGGGTFDVSILTI----------DDGIFEVKATAGDTHLGGE 231
Cdd:cd10230  160 LAGLNVLALVNDGTAAALNYALDRRFENNKpqYVLFYDMGAGSTTATVVEFspveekekskTVPQIEVLGVGWDRTLGGR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 232 DFDNRLVNHFVEEFKRKHK--KDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDL 309
Cdd:cd10230  240 EFDLRLADHLAKEFEEKHKakVDVRTNPRAMAKLLKEANRAKEVLSANSEAPVSIESLYDDIDFKTKITRAEFEELCADL 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 167466173 310 FRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAA 378
Cdd:cd10230  320 FERAVAPIKKALESAGLTLKDIDSVELIGGATRVPKVQEELSEAVGKKKLGKHLNADEAAAMGAAYYAA 388
ScSsz1p_like_NBD cd10232
Nucleotide-binding domain of Saccharmomyces cerevisiae Ssz1pp and similar proteins; ...
5-378 1.80e-103

Nucleotide-binding domain of Saccharmomyces cerevisiae Ssz1pp and similar proteins; Saccharomyces cerevisiae Ssz1p (also known as /Pdr13p/YHR064C) 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). Some family members are not chaperones but rather, function as NEFs for their Hsp70 partners, while other family members function as both chaperones and NEFs. Ssz1 does not function as a chaperone; it facilitates the interaction between the HSP70 Ssb protein and its partner J-domain protein Zuo1 (also known as zuotin) on the ribosome. Ssz1 is found in a stable heterodimer (called RAC, ribosome associated complex) with Zuo1. Zuo1 can only stimulate the ATPase activity of Ssb, when it is in complex with Ssz1. Ssz1 binds ATP but neither nucleotide-binding, hydrolysis, or its SBD, is needed for its in vivo function.


Pssm-ID: 212674 [Multi-domain]  Cd Length: 386  Bit Score: 322.03  E-value: 1.80e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd10232    1 TVIGINFGNTYSSIACINQGKADVIANEDGERQIPSAISYHGEQEYHGNQAKAQLIRNAKNTITNFRDLLGKPFSEIDVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  85 SDMKHWPFQViNDGDKPKVqVSYKGE----TKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKD 160
Cdd:cd10232   81 AAAAAAPVPV-AVIDVGGT-VQEKEEpvpkETILTVHEVTVRFLRRLKEAAEDFLGKKVAGAVLSVPTWFSDEQTEALVK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 161 AGVIAGLNVLRIINEPTAAAIAYGL-DRTGK--GERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRL 237
Cdd:cd10232  159 AAEAAGLPVLQLIPEPAAALLAYDAgEPTEDeaLDRNVVVADFGGTRTDVSVIAVRGGLYTILATAHDPGLGGDTLDDAL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 238 VNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPV 317
Cdd:cd10232  239 VKHFAKEFTKKTKTDPRTNARALAKLRAESEITKKTLSASTSATCSVESLAEGIDFHSSINRLRFELLASAVFRQFAAFV 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 167466173 318 EKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGR-------DLNKSINPDEAVAYGAAVQAA 378
Cdd:cd10232  319 TSAVAKAGLDALDIDEVLLVGGTAFTPKLASNLSYLFPETttitapiTVSKALDPSELVARGCAIQAS 386
HSPH1_NBD cd11739
Nucleotide-binding domain of HSPH1; Human HSPH1 (also known as heat shock 105kDa/110kDa ...
5-380 1.68e-98

Nucleotide-binding domain of HSPH1; Human HSPH1 (also known as heat shock 105kDa/110kDa protein 1, HSP105; HSP105A; HSP105B; NY-CO-25; the human HSPH1 gene maps to 13q12.3) suppresses the aggregation of denatured proteins caused by heat shock in vitro, and may substitute for HSP70 family proteins to suppress the aggregation of denatured proteins in cells under severe stress. It reduces the protein aggregation and cytotoxicity associated with Polyglutamine (PolyQ) diseases, including Huntington's disease, which are a group of inherited neurodegenerative disorders sharing the characteristic feature of having insoluble protein aggregates in neurons. The expression of HSPH1 is elevated in various malignant tumors, including malignant melanoma, and there is a direct correlation between HSPH1 expression and B-cell non-Hodgkin lymphomas (B-NHLs) aggressiveness and proliferation. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212689  Cd Length: 383  Bit Score: 309.19  E-value: 1.68e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd11739    1 SVVGFDVGFQSCYIAVARAGGIETVANEFSDRCTPSVISFGSKNRTIGVAAKNQQITHANNTVSNFKRFHGRAFNDPFVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  85 SDMKHWPFQVI--NDGdKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAG 162
Cdd:cd11739   81 KEKENLSYDLVplKNG-GVGVKVMYMGEEHLFSVEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 163 VIAGLNVLRIINEPTAAAIAYGL---DRTGKGE--RNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRL 237
Cdd:cd11739  160 QIVGLNCLRLMNDMTAVALNYGIykqDLPSLDEkpRIVVFVDMGHSAFQVSACAFNKGKLKVLGTAFDPFLGGKNFDEKL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 238 VNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEP 316
Cdd:cd11739  240 VEHFCAEFKTKYKLDAKSKIRALLRLYQECEKLKKLMSSnSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVP 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466173 317 VEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11739  320 LYSLLEQTHLKVEDVSAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQCAIL 382
HSPA4_NBD cd11737
Nucleotide-binding domain of HSPA4; Human HSPA4 (also known as 70-kDa heat shock protein 4, ...
5-380 2.98e-97

Nucleotide-binding domain of HSPA4; Human HSPA4 (also known as 70-kDa heat shock protein 4, APG-2, HS24/P52, hsp70 RY, and HSPH2; the human HSPA4 gene maps to 5q31.1) responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212687  Cd Length: 383  Bit Score: 305.77  E-value: 2.98e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd11737    1 SVVGIDLGFQSCYVAVARAGGIETIANEYSDRCTPACISFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  85 SDMKHWPFQVIN-DGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGV 163
Cdd:cd11737   81 AEKPSLAYDLVQlPTGSTGIKVMYMEEERNFTTEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGLDRTG-----KGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLV 238
Cdd:cd11737  161 IAGLNCLRLMNETTAVALAYGIYKQDlpaleEKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDTTLGGRKFDEVLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 239 NHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPV 317
Cdd:cd11737  241 NYFCEEFGKKYKLDIKSKIRALLRLSQECEKLKKLMSAnASDLPLNIECFMNDIDVSGTMNRGKFLEMCDDLLARVEPPL 320
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167466173 318 EKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11737  321 RSVLEQAKLKKEDIYAVEIVGGATRIPAVKEKISKFF-GKEVSTTLNADEAVARGCALQCAIL 382
HSP105-110_like_NBD cd11732
Nucleotide-binding domain of 105/110 kDa heat shock proteins including HSPA4, HYOU1, and ...
7-378 8.85e-94

Nucleotide-binding domain of 105/110 kDa heat shock proteins including HSPA4, HYOU1, and similar proteins; This subfamily include the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4, APG-2, HS24/P52, hsp70 RY, and HSPH2; the human HSPA4 gene maps to 5q31.1), HSPA4L (also known as 70-kDa heat shock protein 4-like, APG-1, HSPH3, and OSP94; the human HSPA4L gene maps to 4q28), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1, HSP105; HSP105A; HSP105B; NY-CO-25; the human HSPH1 gene maps to 13q12.3), HYOU1 (also known as human hypoxia up-regulated 1, GRP170; HSP12A; ORP150; GRP-170; ORP-150; the human HYOU1 gene maps to11q23.1-q23.3), Saccharomyces cerevisiae Sse1p, Sse2p, and Lhs1p, and a sea urchin sperm receptor. It belongs 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: 212682 [Multi-domain]  Cd Length: 377  Bit Score: 296.55  E-value: 8.85e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSD 86
Cdd:cd11732    1 FGLDLGNNNSVLAVARNRGIDIVVNEVSNRSTPSVVGFGPKNRYLGETGKNKQTSNIKNTVANLKRIIGLDYHHPDFEQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  87 MKH-WPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:cd11732   81 SKHfTSKLVELDDKKTGAEVRFAGEKHVFSATQLAAMFIDKVKDTVKQDTKANITDVCIAVPPWYTEEQRYNIADAARIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRTGKGE-----RNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNH 240
Cdd:cd11732  161 GLNPVRIVNDVTAAGVSYGIFKTDLPEgeekpRIVAFVDIGHSSYTCSIVAFKKGQLKVLGTACDKHFGGRDFDLAITEH 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 241 FVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKA 320
Cdd:cd11732  241 FADEFKTKYKIDIRENPKAYNRILTAAEKLKKVLSANTNAPFSVESVMNDVDVSSQLSREELEELVKPLLERVTEPVTKA 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 167466173 321 LRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAA 378
Cdd:cd11732  321 LAQAKLSAEEVDFVEIIGGTTRIPTLKQSISEAF-GKPLSTTLNQDEAIAKGAAFICA 377
HSPA4L_NBD cd11738
Nucleotide-binding domain of HSPA4L; Human HSPA4L (also known as 70-kDa heat shock protein ...
5-380 3.22e-79

Nucleotide-binding domain of HSPA4L; Human HSPA4L (also known as 70-kDa heat shock protein 4-like, APG-1, HSPH3, and OSP94; the human HSPA4L gene maps to 4q28) is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 212688  Cd Length: 383  Bit Score: 258.42  E-value: 3.22e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   5 AAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:cd11738    1 SVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTPACISLGSRTRAIGNAAKSQIVTNVRNTIHGFKKLHGRSFDDPIVQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  85 SDMKHWPF--QVINDGDKpKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAG 162
Cdd:cd11738   81 TERIRLPYelQKMPNGSV-GVKVRYLEEERPFAIEQVTGMLLAKLKETSENALKKPVADCVISIPSFFTDAERRSVMAAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 163 VIAGLNVLRIINEPTAAAIAYGLDRTG-----KGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRL 237
Cdd:cd11738  160 QVAGLNCLRLMNETTAVALAYGIYKQDlpaldEKPRNVVFIDMGHSAYQVSVCAFNKGKLKVLATTFDPYLGGRNFDEAL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 238 VNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEP 316
Cdd:cd11738  240 VDYFCDEFKTKYKINVKENSRALLRLYQECEKLKKLMSAnASDLPLNIECFMNDLDVSSKMNRAQFEQLCASLLARVEPP 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466173 317 VEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAIL 380
Cdd:cd11738  320 LKAVMEQANLQREDIYSIEIVGGATRIPAVKEQITSFF-LKDISTTLNADEAVARGCALQCAIL 382
YegD_like cd10231
Escherichia coli YegD, a putative chaperone protein, and related proteins; This bacterial ...
7-354 1.03e-32

Escherichia coli YegD, a putative chaperone protein, and related proteins; This bacterial subfamily includes the uncharacterized Escherichia coli YegD. 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. 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: 212673 [Multi-domain]  Cd Length: 415  Bit Score: 129.58  E-value: 1.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTER------LIGDAAKNQVALNPQNTvfdakRLIgrkfgd 80
Cdd:cd10231    1 LGIDFGTSNSAVAVARDGQPRLVPLEGGSTTLPSALFFPHEESalerevLFGRAAIAAYLEGPGEG-----RLM------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  81 pvvQSdmkhwpfqvindgdkPKvqvSYKG-----ET----KAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFN 151
Cdd:cd10231   70 ---RS---------------LK---SFLGsslfrETrifgRRLTFEDLVARFLAELKQRAEAALGAEIDRVVIGRPVHFV 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 152 DSQ----RQATKD---AGVIAGLNVLRIINEPTAAAIAYGldRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAG 224
Cdd:cd10231  129 GDDeaadAQAEARlraAARAAGFKDVEFQYEPIAAALDYE--QRLTREELVLVVDIGGGTSDFSLVRLGPSRRGRADRRA 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 225 DT------HLGGEDFDNRLVNHFV----------EEFK-------------------------------RKHKKDISQNk 257
Cdd:cd10231  207 DIlahsgvRIGGTDFDRRLSLHAVmpllgkgstyRSGGkglpvpnsyfadlatwhkinflytpktlrelRELARDAVEP- 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 258 RAVRRLRT------------ACERAKRTLSSSTQASLEIDslFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAK 325
Cdd:cd10231  286 ELLERLITvieeelghrlarAVEAAKIALSSQDETRIDLD--FVEVGLEAPVTRAEFEGAIAPDLERIEAAVDEALAQAG 363
                        410       420
                 ....*....|....*....|....*....
gi 167466173 326 LDKAQIHDLVLVGGSTRIPKVQKLLQDFF 354
Cdd:cd10231  364 VSPDAIDRVFLTGGSSLVPAVRQAFAARF 392
HSPA12_like_NBD cd10229
Nucleotide-binding domain of HSPA12A, HSPA12B and similar proteins; Human HSPA12A (also known ...
7-374 1.93e-17

Nucleotide-binding domain of HSPA12A, HSPA12B and similar proteins; Human HSPA12A (also known as 70-kDa heat shock protein-12A) and HSPA12B (also known as 70-kDa heat shock protein-12B, chromosome 20 open reading frame 60/C20orf60, dJ1009E24.2) 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 or HSPA12B. The gene encoding HSPA12A maps to 10q26.12, a cytogenetic region that might represent a common susceptibility locus for both schizophrenia and bipolar affective disorder; reduced expression of HSPA12A has been shown in the prefrontal cortex of subjects with schizophrenia. HSPA12A is also a candidate gene for forelimb-girdle muscular anomaly, an autosomal recessive disorder of Japanese black cattle. HSPA12A is predominantly expressed in neuronal cells. It may also play a role in the atherosclerotic process. The gene encoding HSPA12B maps to 20p13. HSPA12B is 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. HSPA12B expression is up-regulated in lipopolysaccharide (LPS)-induced inflammatory response in the spinal cord, and mostly located in active microglia; this induced expression may be regulated by activation of MAPK-p38, ERK1/2 and SAPK/JNK signaling pathways. Overexpression of HSPA12B also protects against LPS-induced cardiac dysfunction and involves the preserved activation of the PI3K/Akt signaling pathway.


Pssm-ID: 212671 [Multi-domain]  Cd Length: 404  Bit Score: 83.48  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVG-VFQHGKVEII--------ANDQGNRTTPSYVAFTDTERLI--GdaaknqvalnpqntvFDAKRLIG 75
Cdd:cd10229    3 VGIDFGTTFSGVAyAFLDSSPPDIrvitrwpgGEGRGYCKVPTEILYDPEGKLVawG---------------YEAEREYA 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  76 RKFGDPVVQsDMKHWP---------FQVINDGDKPKvqvsykGETKAfyPEEISSMVLTKMKE-----IAEAYLGYPVTN 141
Cdd:cd10229   68 ELEAEDEGW-LFFEWFkllldpdalKLQGDDKLKPL------PPGKT--AVDVIADYLRYLYEhaleeLKKTYGNGEFTA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 142 A----VITVPAYFNDSQRQATKDAGVIAGLNV-------LRIINEPTAAAIA--YGLDRTG---KGERnVLIFDLGGGTF 205
Cdd:cd10229  139 LdiewVLTVPAIWSDAAKQAMREAAIKAGLVSsregpdrLLIVLEPEAAALYclKLLLISLnlkPGDG-FLVCDAGGGTV 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 206 DVSILTIDDGI-FEVK-ATAGDTHLGGEDFDNRlvnHFVEEFKRKHKKDI----SQNKRAVRRLRTACERAKRTLSSSTQ 279
Cdd:cd10229  218 DLTVYEVTSVEpLRLKeLAAGSGGLCGSTFVDR---AFEELLKERLGELFyelpSKSPALWLILMRFFETIKRSFGGTDN 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 280 aSLEIDSLFEGIDFYTSIT-RARFEELCS------DLFRSTLEPVEKALRDaKLDKAQIHD----LVLVGGSTRIPKVQK 348
Cdd:cd10229  295 -DTNIVLPGSLALSKKDPErGIRNGELKIsgedmkSLFDPVIEEIIDLIEE-QLEQAEKGDkvkyIFLVGGFGESPYLRS 372
                        410       420
                 ....*....|....*....|....*...
gi 167466173 349 LLQDFFNGRDLNKSI--NPDEAVAYGAA 374
Cdd:cd10229  373 RLKERFSSRGIRVLRppDPQLAVVRGAV 400
MreB_like cd10225
MreB and similar proteins; MreB is a bacterial protein which assembles into filaments ...
7-374 2.14e-16

MreB and similar proteins; MreB is a bacterial protein which assembles into filaments resembling those of eukaryotic F-actin. It is involved in determining the shape of rod-like bacterial cells, by assembling into large fibrous spirals beneath the cell membrane. MreB has also been implicated in chromosome segregation; specifically MreB is thought to bind to and segregate the replication origin of bacterial chromosomes.


Pssm-ID: 212668 [Multi-domain]  Cd Length: 320  Bit Score: 79.39  E-value: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERL--IGDaaknqvalnpqntvfDAKRLIGRKFGDPVV 83
Cdd:cd10225    1 IGIDLGT--ANTLVYVKGK-GIVLNE------PSVVAIdTKTGKIlaVGE---------------EAKEMLGRTPGNIEV 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  84 QSDMKHwpfQVINDgdkpkvqvsykgetkaFypeeissmvltkmkEIAEAYLGYPVTNA-----------VITVPAYFND 152
Cdd:cd10225   57 IRPLKD---GVIAD----------------F--------------EATEAMLRYFIKKVkgrslffrprvVICVPSGITE 103
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 153 SQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLD-RTGKGernVLIFDLGGGTFDVSILTiDDGIfeVKATAgdTHLGGE 231
Cdd:cd10225  104 VERRAVIDAALHAGAREVYLIEEPLAAAIGAGLDiFEPKG---NMVVDIGGGTTEIAVIS-LGGI--VVSKS--IRVGGD 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 232 DFDNRLVNHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARfeELCSDLFR 311
Cdd:cd10225  176 DFDEAIIRY----VRRKYNLLIGE--------RTA-EEIKIEIGSAYPLDEEETMEVKGRDLVTGLPRTV--EVTSEEVR 240
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466173 312 STL-EPVEKALRDAK--LDK------AQIHD--LVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAA 374
Cdd:cd10225  241 EALkEPLDEIVEAIKsvLEKtppelaADILDrgIVLTGGGALLRGLDELISEET-GLPVRVAEDPLTCVAKGAG 313
NBD_sugar-kinase_HSP70_actin cd00012
Nucleotide-Binding Domain of the sugar kinase/HSP70/actin superfamily; This superfamily ...
92-223 8.11e-09

Nucleotide-Binding Domain of the sugar kinase/HSP70/actin superfamily; This superfamily includes the actin family, the HSP70 family of molecular chaperones and nucleotide exchange factors, the ROK (repressor, ORF, kinase) family, the hexokinase family, the FGGY family (which includes glycerol kinase and similar carbohydrate kinases such as rhamnulokinase and xylulokinase), the exopolyphosphatase/guanosine pentaphosphate phosphohydrolase/nucleoside triphosphate diphosphohydrolase family, propionate kinase/acetate kinase family, glycerol dehydratase reactivase, 2-hydroxyglutaryl-CoA dehydratase component A, N-acetylglucosamine kinase, butyrate kinase 2, Escherichia coli YeaZ and similar glycoproteases, the cell shape-determining protein MreB, the plasmid DNA segregation factor ParM, cell cycle proteins FtsA, Pili assembly protein PilM, ethanolamine utilization protein EutJ, and similar proteins. The nucleotide-binding site residues are conserved; the nucleotide sits in a deep cleft formed between the two lobes of the nucleotide-binding domain (NBD). Substrate binding to superfamily members is associated with closure of this catalytic site cleft. The functional activities of several members of the superfamily, including hexokinases, actin, and HSP70s, are modulated by allosteric effectors, which may act on the cleft closure.


Pssm-ID: 212657  Cd Length: 185  Bit Score: 54.52  E-value: 8.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  92 FQVINDGDKPKVQVSYK---GETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQAT---------- 158
Cdd:cd00012   12 AGVADLDGEILPEEIVPtpvGRPGAVTDLDELEEALRELLKEALRQLKSEIDAVGITEPGGVPKENREVIilpnlllipl 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 167466173 159 KDAGVIAGLNVLRIINEPTAAAIAYGldRTGKGERNVLIFDLGGGTFDVSIltIDDGIFEVKATA 223
Cdd:cd00012   92 ALALEDLGGVPVAVVNDAVAAALAEG--LFGKEEDTVLVVDLGTGTTGIAI--VEDGKGGVGAAG 152
HSPA12B_like_NBD cd11736
Nucleotide-binding domain of HSPA12B and similar proteins; Human HSPA12B (also known as 70-kDa ...
124-382 3.52e-05

Nucleotide-binding domain of HSPA12B and similar proteins; Human HSPA12B (also known as 70-kDa heat shock protein-12B, chromosome 20 open reading frame 60/C20orf60, dJ1009E24.2; the gene encoding HSPA12B maps to 20p13) belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12B. HSPA12B is predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. HSPA12B may be important for host defense in microglia-mediated immune response. HSPA12B expression is up-regulated in lipopolysaccharide (LPS)-induced inflammatory response in the spinal cord, and mostly located in active microglia; this induced expression may be regulated by activation of MAPK-p38, ERK1/2 and SAPK/JNK signaling pathways. Overexpression of HSPA12B also protects against LPS-induced cardiac dysfunction and involves the preserved activation of the PI3K/Akt signaling pathway.


Pssm-ID: 212686  Cd Length: 468  Bit Score: 45.36  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 124 LTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGL------NVLRIINEPTAAAI---------------- 181
Cdd:cd11736  125 LQELKDQSPSLLEKNEVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIycrklrlhqltdlsqr 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 182 -----AYGLDR-------------------------TGKGE--------RNVLIFDLGGGTFDVSILTIDD--GIFE--V 219
Cdd:cd11736  205 avtnfDIDGSRsidssfrqareqlrrsrhsrtflveSGTGElwsemqagDRYIVADCGGGTVDLTVHQIEQpqGTLKelY 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 220 KATAGDTHLGGED--FDNRLVNHFVEEFKRKHKKdisQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFY--- 294
Cdd:cd11736  285 KASGGPYGAVGVDlaFETMLCQIFGEDFIDTFKA---KRPAAWVDLTIAFEARKRTAAPGRANTLNISLPFSFIDFYrkh 361
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 295 ------TSITRARFE--------------ELCSDLFRSTLEPVEKALRD--AKLDKAQIHDLVLVGGSTRIPKVQKLLQD 352
Cdd:cd11736  362 rgqnveTALRKSSVNfvkwssqgmlrmstEAMNELFQPTINNIIQHIENlmQKPEVKGVKFLFLVGGFAESPMLQRAVQN 441
                        330       340       350
                 ....*....|....*....|....*....|
gi 167466173 353 FFnGRDLNKSINPDEAVaygAAVQAAILMG 382
Cdd:cd11736  442 AL-GRNCRVIIPHDVGL---TILKGAVLFG 467
FGGY_1 cd07774
uncharacterized subgroup; belongs to the FGGY family of carbohydrate kinases; This subfamily ...
287-377 5.84e-04

uncharacterized subgroup; belongs to the FGGY family of carbohydrate kinases; This subfamily is composed of uncharacterized carbohydrate kinases. They are sequence homologous to bacterial glycerol kinase and have been classified as members of the FGGY family of carbohydrate kinases. The monomers of FGGY proteins contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 198352 [Multi-domain]  Cd Length: 430  Bit Score: 41.21  E-value: 5.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 287 LFEGIDFYTS---ITRARFEELCSDlFRSTLEPVEKAlrdakldKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNkSI 363
Cdd:cd07774  347 AFYGLTDTTSqedITRSVLEGLTFE-ARSTLECLEKL-------GFEGSRIVVIGGGSRNKLWLQLKASVL-GKPIE-VL 416
                         90
                 ....*....|....
gi 167466173 364 NPDEAVAYGAAVQA 377
Cdd:cd07774  417 DEAELVALGAALLA 430
ParM_like cd10227
Plasmid segregation protein ParM and similar proteins; ParM is a plasmid-encoded bacterial ...
171-254 1.86e-03

Plasmid segregation protein ParM and similar proteins; 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.


Pssm-ID: 212669 [Multi-domain]  Cd Length: 312  Bit Score: 39.32  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 171 RIINEPTAAAIAYGLDRTGKGER-NVLIFDLGGGTFDvsILTIDDGifEVKATAGDTHLGGedfDNRLVNHFVEEFKRKH 249
Cdd:cd10227  144 KVFPEGVGALFDLLLDEGGLLKDkKVLVIDIGGGTTD--VVVFDNG--KPVESSSGSLELG---VSDLYEAIAKELNKEY 216

                 ....*
gi 167466173 250 KKDIS 254
Cdd:cd10227  217 GIDLS 221
FGGY_D-XK_1 cd07809
D-xylulose kinases, subgroup 1; members of the FGGY family of carbohydrate kinases; This ...
319-378 2.46e-03

D-xylulose kinases, subgroup 1; members of the FGGY family of carbohydrate kinases; This subgroup is composed of D-xylulose kinases (XK, also known as xylulokinase; EC 2.7.1.17) from bacteria and eukaryota. They share high sequence similarity with Escherichia coli xylulokinase (EcXK), which catalyzes the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P) and ADP. Some uncharacterized sequences are also included in this subfamily. EcXK exists as a dimer. Each monomer consists of two large domains separated by an open cleft that forms an active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subgroup belong to the FGGY family of carbohydrate kinases.


Pssm-ID: 198375 [Multi-domain]  Cd Length: 487  Bit Score: 39.22  E-value: 2.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167466173 319 KALRDAKLDKAQIHdlvLVGGSTRIPKVQKLLQDFFNGrdlnKSINP--DEAVAYGAAVQAA 378
Cdd:cd07809  386 DLLRALGLKSTEIR---LIGGGAKSPAWRQIIADIMNA----EVVVPdtEEAAALGAAIQAA 440
PTZ00009 PTZ00009
heat shock 70 kDa protein; Provisional
1-611 0e+00

heat shock 70 kDa protein; Provisional


Pssm-ID: 240227 [Multi-domain]  Cd Length: 653  Bit Score: 1159.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGD 80
Cdd:PTZ00009   1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  81 PVVQSDMKHWPFQVINDG-DKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATK 159
Cdd:PTZ00009  81 SVVQSDMKHWPFKVTTGGdDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 160 DAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:PTZ00009 161 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHK-KDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:PTZ00009 241 FCVQDFKRKNRgKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAP 398
Cdd:PTZ00009 321 KVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSSQVQDLLLLDVTP 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 399 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTF 478
Cdd:PTZ00009 401 LSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTF 480
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 479 DIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGL 558
Cdd:PTZ00009 481 DIDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEKV 560
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|...
gi 167466173 559 KGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:PTZ00009 561 KGKLSDSDKATIEKAIDEALEWLEKNQLAEKEEFEHKQKEVESVCNPIMTKMY 613
HSP70 pfam00012
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ...
6-611 0e+00

Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.


Pssm-ID: 249507 [Multi-domain]  Cd Length: 598  Bit Score: 1002.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173    6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:pfam00012   1 VIGIDLGTTNSCVAVMEGGGPEVIANDEGNRTTPSVVAFTPKERLVGQAAKRQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   86 DMKHWPFQVINDGD-KPKVQVSYKGETkaFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:pfam00012  81 DIKHVPYKVVKLPNgDAGVEVRYLGET--FTPEQISAMVLQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGRI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  165 AGLNVLRIINEPTAAAIAYGLDRTGKgERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:pfam00012 159 AGLNVLRIINEPTAAALAYGLDKKDK-ERNVLVFDLGGGTFDVSILEIGDGVFEVLATNGDTHLGGEDFDNRLVDHFVEE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSS-STQASLEIDSLFE-GIDFYTSITRARFEELCSDLFRSTLEPVEKALR 322
Cdd:pfam00012 238 FKKKYGIDLSKDPRALQRLREAAEKAKIELSSnQTEINLPFITAMAdGKDVSGTLTRAKFEELCADLFERTLEPVEKALK 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  323 DAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksENVQDLLLLDVAPLSLG 402
Cdd:pfam00012 318 DAKLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKTVNPDEAVAIGAAVQAGVLSGT--FDVKDVLLLDVTPLSLG 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  403 LETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDA 482
Cdd:pfam00012 395 IETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDA 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  483 NGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGlkGKI 562
Cdd:pfam00012 475 NGILTVSAKDKGTGKEQKITITNSSG-LSDDEIERMVKDAEEYAAEDKKRKERIEAKNEAEEYVYSLEKSLKEEG--DKL 551
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|
gi 167466173  563 SEADKKKVldkcQEVISWLDANTLAE-KDEFEHKRKELEQVCNPIISGLY 611
Cdd:pfam00012 552 PEADKKKV----EEAIEWLKEELEGEdKEEIEAKTEELQKVVQPIGERMY 597
dnaK PRK00290
molecular chaperone DnaK; Provisional
1-611 0e+00

molecular chaperone DnaK; Provisional


Pssm-ID: 234715 [Multi-domain]  Cd Length: 627  Bit Score: 870.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAaaIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKfg 79
Cdd:PRK00290   1 MGKI--IGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRR-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  80 DPVVQSDMKHWPFQVIN-DGDKPKVQVsykgETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQAT 158
Cdd:PRK00290  77 DEEVQKDIKLVPYKIVKaDNGDAWVEI----DGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQAT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 159 KDAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLV 238
Cdd:PRK00290 153 KDAGKIAGLEVLRIINEPTAAALAYGLDK--KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRII 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 239 NHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRS 312
Cdd:PRK00290 231 DYLADEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQT--EINLPFITADasgpkhLEIKLTRAKFEELTEDLVER 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 313 TLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLL 392
Cdd:PRK00290 309 TIEPCKQALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD----VKDVL 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 393 LLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVP 472
Cdd:PRK00290 384 LLDVTPLSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVP 463
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 473 QIEVTFDIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSA 552
Cdd:PRK00290 464 QIEVTFDIDANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKT 542
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 167466173 553 VEDegLKGKISEADKKKVLDKCQEVISWLDANtlaEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:PRK00290 543 LKE--LGDKVPADEKEKIEAAIKELKEALKGE---DKEAIKAKTEELTQASQKLGEAMY 596
prok_dnaK TIGR02350
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ...
6-611 0e+00

chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE chaperone system. All members of the seed alignment were taken from completely sequenced bacterial or archaeal genomes and (except for Mycoplasma sequence) found clustered with other genes of this systems. This model excludes DnaK homologs that are not DnaK itself, such as the heat shock cognate protein HscA (TIGR01991). However, it is not designed to distinguish among DnaK paralogs in eukaryotes. Note that a number of dnaK genes have shadow ORFs in the same reverse (relative to dnaK) reading frame, a few of which have been assigned glutamate dehydrogenase activity. The significance of this observation is unclear; lengths of such shadow ORFs are highly variable as if the presumptive protein product is not conserved [Protein fate, Protein folding and stabilization].


Pssm-ID: 233830 [Multi-domain]  Cd Length: 595  Bit Score: 802.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173    6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGdpVVQ 84
Cdd:TIGR02350   2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFD--EVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   85 SDMKHWPFQVINDGDKPKVQVsykgETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:TIGR02350  80 EEAKRVPYKVVGDGGDVRVKV----DGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  165 AGLNVLRIINEPTAAAIAYGLDRTGKGERnVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEK-ILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADE 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:TIGR02350 235 FKKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLST--EINLPFITADasgpkhLEMTLTRAKFEELTADLVERTKEPVR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAP 398
Cdd:TIGR02350 313 QALKDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD----VKDVLLLDVTP 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  399 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTF 478
Cdd:TIGR02350 388 LSLGIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTF 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  479 DIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegL 558
Cdd:TIGR02350 468 DIDANGILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKE--A 544
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 167466173  559 KGKISEADKKKVLDKCQEVISWLDANTlaeKDEFEHKRKELEQVCNPIISGLY 611
Cdd:TIGR02350 545 GDKLPAEEKEKIEKAVAELKEALKGED---VEEIKAKTEELQQALQKLAEAMY 594
DnaK COG0443
Molecular chaperone [Posttranslational modification, protein turnover, chaperones]
1-611 0e+00

Molecular chaperone [Posttranslational modification, protein turnover, chaperones]


Pssm-ID: 223520 [Multi-domain]  Cd Length: 579  Bit Score: 732.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAA-AIGIDLGTTYSCVGVFQHG-KVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVALNPQNTVFDAKRLIGRK 77
Cdd:COG0443    1 MSTAKkAIGIDLGTTNSVVAVMRGGgLPKVIENAEGERLTPSVVAFSkNGEVLVGQAAKRQAVDNPENTIFSIKRKIGRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  78 fgdpvvqsdmkhwpfqviNDGDKPKVQVSykgeTKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQA 157
Cdd:COG0443   81 ------------------SNGLKISVEVD----GKKYTPEEISAMILTKLKEDAEAYLGEKVTDAVITVPAYFNDAQRQA 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 158 TKDAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRL 237
Cdd:COG0443  139 TKDAARIAGLNVLRLINEPTAAALAYGLDK--GKEKTVLVYDLGGGTFDVSLLEIGDGVFEVLATGGDNHLGGDDFDNAL 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 238 VNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPV 317
Cdd:COG0443  217 IDYLVMEFKGKGGIDLRSDKAALQRLREAAEKAKIELSSATQTSINLPSIGGDIDLLKELTRAKFEELILDLLERTIEPV 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 318 EKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSenvqDLLLLDVA 397
Cdd:COG0443  297 EQALKDAGLEKSDIDLVILVGGSTRIPAVQELVKEFF-GKEPEKSINPDEAVALGAAIQAAVLSGEVP----DVLLLDVI 371
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 398 PLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVT 477
Cdd:COG0443  372 PLSLGIETLGGVRTPIIERNTTIPVKKSQEFSTAADGQTAVAIHVFQGEREMAADNKSLGRFELDGIPPAPRGVPQIEVT 451
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 478 FDIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEg 557
Cdd:COG0443  452 FDIDANGILNVTAKDLGTGKEQSITIKASSG-LSDEEIERMVEDAEANAALDKKFRELVEARNEAESLIYSLEKALKEI- 529
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....
gi 167466173 558 lkGKISEADKKKVLDKCQEVISWLDantlAEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:COG0443  530 --VKVSEEEKEKIEEAITDLEEALE----GEKEEIKAKIEELQEVTQKLAEKKY 577
dnaK CHL00094
heat shock protein 70
1-602 0e+00

heat shock protein 70


Pssm-ID: 214360 [Multi-domain]  Cd Length: 621  Bit Score: 702.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAaaIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFG 79
Cdd:CHL00094   1 MGKV--VGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKgDLLVGQIAKRQAVINPENTFYSVKRFIGRKFS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  80 DpvVQSDMKHWPFQVINDG-DKPKVQVSYKGetKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQAT 158
Cdd:CHL00094  79 E--ISEEAKQVSYKVKTDSnGNIKIECPALN--KDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQAT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 159 KDAGVIAGLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLV 238
Cdd:CHL00094 155 KDAGKIAGLEVLRIINEPTAASLAYGLDK--KNNETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 239 NHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLE---IDSLFEG-IDFYTSITRARFEELCSDLFRSTL 314
Cdd:CHL00094 233 NWLIKEFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 315 EPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLL 394
Cdd:CHL00094 313 IPVENALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE----VKDILLL 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 395 DVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQI 474
Cdd:CHL00094 388 DVTPLSLGVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQI 467
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 475 EVTFDIDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVE 554
Cdd:CHL00094 468 EVTFDIDANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLK 546
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 167466173 555 DegLKGKISEADKKKVldkcQEVISWLDANTlaEKDEFEHKRKELEQV 602
Cdd:CHL00094 547 E--LKDKISEEKKEKI----ENLIKKLRQAL--QNDNYESIKSLLEEL 586
PRK13411 PRK13411
molecular chaperone DnaK; Provisional
1-611 0e+00

molecular chaperone DnaK; Provisional


Pssm-ID: 184039 [Multi-domain]  Cd Length: 653  Bit Score: 695.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAaaIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFG 79
Cdd:PRK13411   1 MGKV--IGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSgDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  80 DpvVQSDMKHWPFQVINdGDKPKVQVSYKGetKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATK 159
Cdd:PRK13411  79 D--TEEERSRVPYTCVK-GRDDTVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 160 DAGVIAGLNVLRIINEPTAAAIAYGLDRTGKgERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN 239
Cdd:PRK13411 154 DAGTIAGLEVLRIINEPTAAALAYGLDKQDQ-EQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 240 HFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASleIDSLFEGID------FYTSITRARFEELCSDLFRST 313
Cdd:PRK13411 233 WLVENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTS--INLPFITADetgpkhLEMELTRAKFEELTKDLVEAT 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 314 LEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLL 393
Cdd:PRK13411 311 IEPMQQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE----VKDLLL 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 394 LDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQ 473
Cdd:PRK13411 387 LDVTPLSLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQ 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 474 IEVTFDIDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAV 553
Cdd:PRK13411 467 IEVSFEIDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTL 545
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 167466173 554 EDEGlkGKISEADKKKVLDKCQEVISWLDaNTLAEKDEFEHKRKELEQVCNPIISGLY 611
Cdd:PRK13411 546 KENG--ELISEELKQRAEQKVEQLEAALT-DPNISLEELKQQLEEFQQALLAIGAEVY 600
PTZ00400 PTZ00400
DnaK-type molecular chaperone; Provisional
7-611 0e+00

DnaK-type molecular chaperone; Provisional


Pssm-ID: 240403 [Multi-domain]  Cd Length: 663  Bit Score: 678.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:PTZ00400  44 VGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDATKK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQVINDgdkPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:PTZ00400 124 EQKILPYKIVRA---SNGDAWIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIA 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRT-GKgerNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:PTZ00400 201 GLDVLRIINEPTAAALAFGMDKNdGK---TIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAE 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQAslEIDSLFEGID------FYTSITRARFEELCSDLFRSTLEPVE 318
Cdd:PTZ00400 278 FKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQT--EINLPFITADqsgpkhLQIKLSRAKLEELTHDLLKKTIEPCE 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 319 KALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAP 398
Cdd:PTZ00400 356 KCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE----IKDLLLLDVTP 430
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 399 LSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTF 478
Cdd:PTZ00400 431 LSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTF 510
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 479 DIDANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegL 558
Cdd:PTZ00400 511 DVDANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSD--L 587
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|...
gi 167466173 559 KGKISEADKKKVLDKCQEVISWLDANTLaekDEFEHKRKELEQVCNPIISGLY 611
Cdd:PTZ00400 588 KDKISDADKDELKQKITKLRSTLSSEDV---DSIKDKTKQLQEASWKISQQAY 637
PRK13410 PRK13410
molecular chaperone DnaK; Provisional
7-590 0e+00

molecular chaperone DnaK; Provisional


Pssm-ID: 184038 [Multi-domain]  Cd Length: 668  Bit Score: 678.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQS 85
Cdd:PRK13410   5 VGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDE--LDP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQVINDgDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:PRK13410  83 ESKRVPYTIRRN-EQGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRIA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:PRK13410 162 GLEVERILNEPTAAALAYGLDR--SSSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLS--SSTQASLE-IDSLFEG---IDfyTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:PRK13410 240 LEKEGIDLRRDRQALQRLTEAAEKAKIELSgvSVTDISLPfITATEDGpkhIE--TRLDRKQFESLCGDLLDRLLRPVKR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAPL 399
Cdd:PRK13410 318 ALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLI-PREPNQNVNPDEVVAVGAAIQAGILAGE----LKDLLLLDVTPL 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 400 SLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFD 479
Cdd:PRK13410 393 SLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFD 472
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 480 IDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFN----MKSAVED 555
Cdd:PRK13410 473 IDANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQaerrLRDAALE 551
                        570       580       590
                 ....*....|....*....|....*....|....*
gi 167466173 556 EGLKGkiSEADKKKVLDKCQEVISWLDANTLAEKD 590
Cdd:PRK13410 552 FGPYF--AERQRRAVESAMRDVQDSLEQDDDRELD 584
PLN03184 PLN03184
chloroplast Hsp70; Provisional
7-602 0e+00

chloroplast Hsp70; Provisional


Pssm-ID: 215618 [Multi-domain]  Cd Length: 673  Bit Score: 630.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDT-ERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQS 85
Cdd:PLN03184  42 VGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VDE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQVINDgDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:PLN03184 120 ESKQVSYRVVRD-ENGNVKLDCPAIGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIA 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:PLN03184 199 GLEVLRIINEPTAASLAYGFEK--KSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNF 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLE---IDSLFEG---IDfyTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:PLN03184 277 KKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhID--TTLTRAKFEELCSDLLDRCKTPVEN 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFfNGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAPL 399
Cdd:PLN03184 355 ALRDAKLSFKDIDEVILVGGSTRIPAVQELVKKL-TGKDPNVTVNPDEVVALGAAVQAGVLAGE----VSDIVLLDVTPL 429
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 400 SLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFD 479
Cdd:PLN03184 430 SLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFD 509
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 480 IDANGILNVTATDKSTGKANKITITNdKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegLK 559
Cdd:PLN03184 510 IDANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKE--LG 586
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....
gi 167466173 560 GKISEADKKKVLDKCQEVISWLDA-NTLAEKDEFEHKRKELEQV 602
Cdd:PLN03184 587 DKVPADVKEKVEAKLKELKDAIASgSTQKMKDAMAALNQEVMQI 630
PTZ00186 PTZ00186
heat shock 70 kDa precursor protein; Provisional
7-601 0e+00

heat shock 70 kDa precursor protein; Provisional


Pssm-ID: 140213 [Multi-domain]  Cd Length: 657  Bit Score: 605.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSD 86
Cdd:PTZ00186  30 IGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHIQKD 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  87 MKHWPFQVI--NDGDKpKVQvsyKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:PTZ00186 110 IKNVPYKIVraGNGDA-WVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTI 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGkgERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:PTZ00186 186 AGLNVIRVVNEPTAAALAYGMDKTK--DSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEE 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGID----FYTSITRARFEELCSDLFRSTLEPVEKA 320
Cdd:PTZ00186 264 FRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADgaqhIQMHISRSKFEGITQRLIERSIAPCKQC 343
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 321 LRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDksenVQDLLLLDVAPLS 400
Cdd:PTZ00186 344 MKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD----VKGLVLLDVTPLS 418
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 401 LGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDI 480
Cdd:PTZ00186 419 LGIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDI 498
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 481 DANGILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAfnmKSAVEDEGLKG 560
Cdd:PTZ00186 499 DANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQL---TTAERQLGEWK 574
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|.
gi 167466173 561 KISEADKKKVLDKCQEVISWLDaNTLAEKDEFEHKRKELEQ 601
Cdd:PTZ00186 575 YVSDAEKENVKTLVAELRKAME-NPNVAKDDLAAATDKLQK 614
hscA PRK05183
chaperone protein HscA; Provisional
6-544 0e+00

chaperone protein HscA; Provisional


Pssm-ID: 235360 [Multi-domain]  Cd Length: 616  Bit Score: 554.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDpvVQS 85
Cdd:PRK05183  21 AVGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHWPFQvINDGDKPKVQVSYKGETKAfyPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:PRK05183  99 RYPHLPYQ-FVASENGMPLIRTAQGLKS--PVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDRtgKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEF 245
Cdd:PRK05183 176 GLNVLRLLNEPTAAAIAYGLDS--GQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILEQA 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 246 KRKHKKDISQnkraVRRLRTACERAKRTLSSSTQASLEIdSLFEGIdfytsITRARFEELCSDLFRSTLEPVEKALRDAK 325
Cdd:PRK05183 254 GLSPRLDPED----QRLLLDAARAAKEALSDADSVEVSV-ALWQGE-----ITREQFNALIAPLVKRTLLACRRALRDAG 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 326 LDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSENvqDLLLLDVAPLSLGLET 405
Cdd:PRK05183 324 VEADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDS--DMLLLDVIPLSLGLET 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 406 AGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGI 485
Cdd:PRK05183 401 MGGLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGL 480
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167466173 486 LNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQR----ERVSAKNALES 544
Cdd:PRK05183 481 LSVTAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQARalaeQKVEAERVLEA 542
HscA TIGR01991
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ...
6-579 0e+00

Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK [Protein fate, Protein folding and stabilization].


Pssm-ID: 233673 [Multi-domain]  Cd Length: 599  Bit Score: 533.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173    6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAF-TDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQ 84
Cdd:TIGR01991   1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPKNTISSVKRLMGRSIEDIKTF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   85 SDMkhwPFqVINDGDKPKVQVSYKGETKAfyPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:TIGR01991  81 SIL---PY-RFVDGPGEMVRLRTVQGTVT--PVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  165 AGLNVLRIINEPTAAAIAYGLDRTGKGerNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:TIGR01991 155 AGLNVLRLLNEPTAAAVAYGLDKASEG--IYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWILKQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  245 FKRKHKKDISQNKRAVRRLRTACERAkrtlssSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:TIGR01991 233 LGISADLNPEDQRLLLQAARAAKEAL------TDAESVEVDFTLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDA 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  325 KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAAVQAAILMGDKSENvqDLLLLDVAPLSLGLE 404
Cdd:TIGR01991 307 GLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGN--DLLLLDVTPLSLGIE 383
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  405 TAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANG 484
Cdd:TIGR01991 384 TMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADG 463
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  485 ILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAED-----------EVQRERVSAKNALEsyafnmksav 553
Cdd:TIGR01991 464 LLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDmyaralaeqkvEAERILEALQAALA---------- 532
                         570       580
                  ....*....|....*....|....*....
gi 167466173  554 EDEGLkgkISEADKKKV---LDKCQEVIS 579
Cdd:TIGR01991 533 ADGDL---LSEDERAAIdaaMEALQKALQ 558
hscA PRK01433
chaperone protein HscA; Provisional
6-610 8.23e-111

chaperone protein HscA; Provisional


Pssm-ID: 234955 [Multi-domain]  Cd Length: 595  Bit Score: 348.38  E-value: 8.23e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   6 AIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDaaknqvalnpQNTVFDAKRLIGRKFGDPVVQS 85
Cdd:PRK01433  21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGKTLKEILNTP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMkhwpFQVINDG-DKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVI 164
Cdd:PRK01433  91 AL----FSLVKDYlDVNSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYGLDRTGKGerNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEE 244
Cdd:PRK01433 167 AGFEVLRLIAEPTAAAYAYGLNKNQKG--CYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 245 FKRKHKKDISQnkravrrlrtACERAKRTLSSstQASLEIDSLfegidfytSITRARFEELCSDLFRSTLEPVEKALRDA 324
Cdd:PRK01433 245 FDLPNSIDTLQ----------LAKKAKETLTY--KDSFNNDNI--------SINKQTLEQLILPLVERTINIAQECLEQA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 325 KldKAQIHDLVLVGGSTRIPKVQKLLQDFFNgRDLNKSINPDEAVAYGAAVQAAILMGDKsenvQDLLLLDVAPLSLGLE 404
Cdd:PRK01433 305 G--NPNIDGVILVGGATRIPLIKDELYKAFK-VDILSDIDPDKAVVWGAALQAENLIAPH----TNSLLIDVVPLSLGME 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 405 TAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANG 484
Cdd:PRK01433 378 LYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADG 457
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 485 ILNVTATDKSTGKANKITITNDKGrLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDegLKGKISE 564
Cdd:PRK01433 458 ILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAE--LTTLLSE 534
                        570       580       590       600       610
                 ....*....|....*....|....*....|....*....|....*....|.
gi 167466173 565 ADK---KKVLDKCQEVISWLDANTLAEK-DEFEHK-RKELEQVCNPIISGL 610
Cdd:PRK01433 535 SEIsiiNSLLDNIKEAVHARDIILINNSiKEFKSKiKKSMDTKLNIIINDL 585
PRK13930 PRK13930
rod shape-determining protein MreB; Provisional
7-374 1.06e-13

rod shape-determining protein MreB; Provisional


Pssm-ID: 237564 [Multi-domain]  Cd Length: 335  Bit Score: 71.32  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYscVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERL--IGDaaknqvalnpqntvfDAKRLIGRKFGDPVV 83
Cdd:PRK13930  11 IGIDLGTAN--TLVYVKGK-GIVLNE------PSVVAIdTKTGKVlaVGE---------------EAKEMLGRTPGNIEA 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  84 QSDMKHwpfQVINDGDKPKVQVSYkgetkaFYpeeisSMVLTKMkeiaeaYLGYPvtNAVITVPAYFNDSQRQATKDAGV 163
Cdd:PRK13930  67 IRPLKD---GVIADFEATEAMLRY------FI-----KKARGRR------FFRKP--RIVICVPSGITEVERRAVREAAE 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 164 IAGLNVLRIINEPTAAAIAYGLDRTgKGERNvLIFDLGGGTFDVSILTIdDGIfevkATAGDTHLGGEDFDNRLVNHfve 243
Cdd:PRK13930 125 HAGAREVYLIEEPMAAAIGAGLPVT-EPVGN-MVVDIGGGTTEVAVISL-GGI----VYSESIRVAGDEMDEAIVQY--- 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 244 eFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQA----SLEIdslfEGIDFYTSITRARfeELCSDLFRSTL-EPVE 318
Cdd:PRK13930 195 -VRRKYNLLIGE--------RTA-EEIKIEIGSAYPLdeeeSMEV----RGRDLVTGLPKTI--EISSEEVREALaEPLQ 258
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 167466173 319 K---ALRDAkLDK------AQIHD--LVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGAA 374
Cdd:PRK13930 259 QiveAVKSV-LEKtppelaADIIDrgIVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTCVARGTG 323
mreB TIGR00904
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ...
7-352 3.90e-12

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: 66.66  E-value: 3.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173    7 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAFtdtERLIGDAAKNQVALNPqntvfDAKRLIGRKFGDPVVQSD 86
Cdd:TIGR00904   5 IGIDLGTANTLVYVKGRG---IVLNE------PSVVAI---RTDRDAKTKSILAVGH-----EAKEMLGKTPGNIVAIRP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   87 MKHwpfQVINDGDKPKVQVSYkgetkaFYPEEISSMVLTKMKeiaeaylgypvtnAVITVPAYFNDSQRQATKDAGVIAG 166
Cdd:TIGR00904  68 MKD---GVIADFEVTEKMIKY------FIKQVHSRKSFFKPR-------------IVICVPSGITPVERRAVKESALSAG 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  167 LNVLRIINEPTAAAIAYGL---DRTGKgernvLIFDLGGGTFDVSILTIdDGIFEVKAtagdTHLGGEDFDNRLVNHfve 243
Cdd:TIGR00904 126 AREVYLIEEPMAAAIGAGLpveEPTGS-----MVVDIGGGTTEVAVISL-GGIVVSRS----IRVGGDEFDEAIINY--- 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  244 eFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQASLEIDSL-FEGIDFYTSITRArfEELCSDLFRSTL-EPVE--- 318
Cdd:TIGR00904 193 -IRRTYNLLIGE--------QTA-ERIKIEIGSAYPLNDEPRKMeVRGRDLVTGLPRT--IEITSVEVREALqEPVNqiv 260
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 167466173  319 KALRDAkLDK------AQIHD--LVLVGGSTRIPKVQKLLQD 352
Cdd:TIGR00904 261 EAVKRT-LEKtppelaADIVErgIVLTGGGALLRNLDKLLSK 301
EutJ COG4820
Ethanolamine utilization protein, possible chaperonin [Amino acid transport and metabolism]
123-251 4.10e-09

Ethanolamine utilization protein, possible chaperonin [Amino acid transport and metabolism]


Pssm-ID: 227157 [Multi-domain]  Cd Length: 277  Bit Score: 56.79  E-value: 4.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 123 VLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGkgernvlIFDLGG 202
Cdd:COG4820   77 IVRRLKDTLEKQLGIRFTHAATAIPPGTEQGDPRISINVIESAGLEVLHVLDEPTAAADVLQLDDGG-------VVDIGG 149
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 167466173 203 GTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVN-HFVEEFKRKHKK 251
Cdd:COG4820  150 GTTGISIVKKGKVIYSADEPTGGTHMTLVLAGNYGISlEEAEQYKRGHKK 199
MreB_Mbl pfam06723
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ...
7-373 4.20e-09

MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.


Pssm-ID: 253878 [Multi-domain]  Cd Length: 327  Bit Score: 57.18  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173    7 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvalnpqntvfDAKRLIGRKFGDPVV 83
Cdd:pfam06723   4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGN---------------EAKKMLGRTPGNIVA 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   84 QSDMKhwpfqvinDGdkpkvqvsykgetkafypeeissmVLTKMkEIAEAYLGY-----------PVTNAVITVPAYFND 152
Cdd:pfam06723  60 VRPLK--------DG------------------------VIADF-EVTEAMLKYfikkvhgrrsfSKPRVVICVPSGITE 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  153 SQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDrTGKGERNvLIFDLGGGTFDVSILTIdDGIfevkATAGDTHLGGED 232
Cdd:pfam06723 107 VERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLP-VEEPTGN-MVVDIGGGTTEVAVISL-GGI----VTSKSVRVAGDE 179
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  233 FDNRLVNHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSSSTQA----SLEIdslfEGIDFYT------SITRARF 302
Cdd:pfam06723 180 MDEAIIKY----IRKKYNLLIGE--------RTA-ERIKIEIGSAYPTeeeeKMEI----RGRDLVTglpktiEISSEEV 242
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 167466173  303 EELCSDLFRSTLEPVEKALRDAKLD-KAQIHD--LVLVGGSTRIPKVQKLLQDFFnGRDLNKSINPDEAVAYGA 373
Cdd:pfam06723 243 REALKEPVSAIVEAVKEVLEKTPPElAADIVDrgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
EutJ TIGR02529
ethanolamine utilization protein EutJ family protein;
120-252 4.68e-09

ethanolamine utilization protein EutJ family protein;


Pssm-ID: 213718 [Multi-domain]  Cd Length: 239  Bit Score: 55.91  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  120 SSMVLTKMKEIAEAYLGYPVTNAVITVPAyfNDSQRQATKDAGVI--AGLNVLRIINEPTAAAIAYGLDrtgkgerNVLI 197
Cdd:TIGR02529  42 AVEIVRRLKDTLEQKLGIELTHAATAIPP--GTIEGDPKVIVNVIesAGIEVLHVLDEPTAAAAVLQIK-------NGAV 112
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 167466173  198 FDLGGGTFDVSILTIDDGIFEVKATAGDTHLG-------GEDFDNrlvnhfVEEFKRKHKKD 252
Cdd:TIGR02529 113 VDVGGGTTGISILKKGKVIYSADEPTGGTHMSlvlagayGISFEE------AEEYKRGHKDE 168
PRK13928 PRK13928
rod shape-determining protein Mbl; Provisional
7-250 7.50e-08

rod shape-determining protein Mbl; Provisional


Pssm-ID: 237563 [Multi-domain]  Cd Length: 336  Bit Score: 53.37  E-value: 7.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTtySCVGVFQHGKvEIIANDqgnrttPSYVAF-TDTERLI--GDaaknqvalnpqntvfDAKRLIGRKFGDPVV 83
Cdd:PRK13928   6 IGIDLGT--ANVLVYVKGK-GIVLNE------PSVVAIdKNTNKVLavGE---------------EARRMVGRTPGNIVA 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  84 QSDMKHwpfQVINDGDkpkvqvsykgetkafypeeissmvltkmkeIAEAYLGYPVTNA-----------VITVPAYFND 152
Cdd:PRK13928  62 IRPLRD---GVIADYD------------------------------VTEKMLKYFINKAcgkrffskpriMICIPTGITS 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 153 SQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTgKGERNVLIfDLGGGTFDVSILTIDDGIfevkaTAGDTHLGGED 232
Cdd:PRK13928 109 VEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDIS-QPSGNMVV-DIGGGTTDIAVLSLGGIV-----TSSSIKVAGDK 181
                        250
                 ....*....|....*...
gi 167466173 233 FDNRLVNHfveeFKRKHK 250
Cdd:PRK13928 182 FDEAIIRY----IRKKYK 195
XylB TIGR01312
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ...
287-385 6.66e-07

D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see PMID:9324246), was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization [Energy metabolism, Sugars].


Pssm-ID: 233354 [Multi-domain]  Cd Length: 481  Bit Score: 50.78  E-value: 6.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  287 LFEGIDFYTsiTRArfeelcsDLFRSTLEPVEKALRDA-----KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRdlnk 361
Cdd:TIGR01312 351 SFIGLTHNT--TRA-------DLTRAVLEGVTFALRDSldilrEAGGIPIQSIRLIGGGAKSPAWRQMLADIFGTP---- 417
                          90       100
                  ....*....|....*....|....*..
gi 167466173  362 sI---NPDEAVAYGAAVQAAILMGDKS 385
Cdd:TIGR01312 418 -VdvpEGEEGPALGAAILAAWALGEKD 443
ftsA COG0849
Cell division ATPase FtsA [Cell division and chromosome partitioning]
165-375 9.45e-07

Cell division ATPase FtsA [Cell division and chromosome partitioning]


Pssm-ID: 223918 [Multi-domain]  Cd Length: 418  Bit Score: 50.31  E-value: 9.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 165 AGLNVLRIINEPTAAAIAYgLDRTGKgERNVLIFDLGGGTFDVSILTIDDGIF-EVKATAGDthlggedfdnrlvnHFVe 243
Cdd:COG0849  177 AGLKVDNIVLEPLASALAV-LTEDEK-ELGVALIDIGGGTTDIAIYKNGALRYtGVIPVGGD--------------HVT- 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 244 efkrkhkKDISQNKRAvrRLRTAcERAKRTLSSSTQASLEIDSLFE----GIDFYTSITRARFEELCSDLFRSTLEPVEK 319
Cdd:COG0849  240 -------KDIAKGLKT--PFEEA-ERIKIKYGSALISLADDEETIEvpsvGSDIPRQVTRSELSEIIEARVEEILELVKA 309
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 167466173 320 ALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFF-----NGRDLNKSINPDEAV--AYGAAV 375
Cdd:COG0849  310 ELRKSGLPNHLPGGVVLTGGGAQLPGIVELAERIFgrpvrLGVPLNIVGLTDIARnpAFSTAV 372
MreB COG1077
Actin-like ATPase involved in cell morphogenesis [Cell division and chromosome partitioning]
7-246 2.89e-06

Actin-like ATPase involved in cell morphogenesis [Cell division and chromosome partitioning]


Pssm-ID: 224003 [Multi-domain]  Cd Length: 342  Bit Score: 48.38  E-value: 2.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAftdterlIGDAAKNQVALnpqnTV-FDAKRLIGRKFGDPVVQS 85
Cdd:COG1077    9 IGIDLGTANTLVYVKGKG---IVLNE------PSVVA-------IESEGKTKVVL----AVgEEAKQMLGRTPGNIVAIR 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  86 DMKHwpfQVINDGDkpkvqvsykgetkafYPEEissMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIA 165
Cdd:COG1077   69 PMKD---GVIADFE---------------VTEL---MLKYFIKKVHKNGSSFPKPRIVICVPSGITDVERRAIKEAAESA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 166 GLNVLRIINEPTAAAIAYGLDrTGKGERNVLIfDLGGGTFDVSILTiDDGIfeVKATAgdTHLGGEDFDNRLVNHFVEEF 245
Cdd:COG1077  128 GAREVYLIEEPMAAAIGAGLP-IMEPTGSMVV-DIGGGTTEVAVIS-LGGI--VSSSS--VRVGGDKMDEAIIVYVRKKY 200

                 .
gi 167466173 246 K 246
Cdd:COG1077  201 N 201
PRK13929 PRK13929
rod-share determining protein MreBH; Provisional
1-240 4.75e-06

rod-share determining protein MreBH; Provisional


Pssm-ID: 184403 [Multi-domain]  Cd Length: 335  Bit Score: 47.59  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   1 MAKAAAIGIDLGTTYSCVGVFQHGkveIIANDqgnrttPSYVAFtDTErligdaAKNQVALNPqntvfDAKRLIGRKFGD 80
Cdd:PRK13929   1 MFQSTEIGIDLGTANILVYSKNKG---IILNE------PSVVAV-DTE------TKAVLAIGT-----EAKNMIGKTPGK 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  81 PVVQSDMKHwpfQVINDGDkpkvqvsykgetkafypeeISSMVLTKMKEIAEAYLGYPV--TNAVITVPAYFNDSQRQAT 158
Cdd:PRK13929  60 IVAVRPMKD---GVIADYD-------------------MTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAI 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 159 KDAGVIAGLNVLRIINEPTAAAIAYGLDrTGKGERNVLIfDLGGGTFDVSILTiddgiFEVKATAGDTHLGGEDFDNRLV 238
Cdd:PRK13929 118 SDAVKNCGAKNVHLIEEPVAAAIGADLP-VDEPVANVVV-DIGGGTTEVAIIS-----FGGVVSCHSIRIGGDQLDEDIV 190

                 ..
gi 167466173 239 NH 240
Cdd:PRK13929 191 SF 192
PRK15080 PRK15080
ethanolamine utilization protein EutJ; Provisional
123-228 5.17e-06

ethanolamine utilization protein EutJ; Provisional


Pssm-ID: 237904 [Multi-domain]  Cd Length: 267  Bit Score: 47.13  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 123 VLTKMKEIAEAYLGYPVTNAVITVPAyfndsqrqAT--KDAGVI------AGLNVLRIINEPTAAAIAYGLDrtgkgerN 194
Cdd:PRK15080  72 IVRRLKATLEEKLGRELTHAATAIPP--------GTseGDPRAIinvvesAGLEVTHVLDEPTAAAAVLGID-------N 136
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 167466173 195 VLIFDLGGGTFDVSILtiDDGifEVKATA----GDTHL 228
Cdd:PRK15080 137 GAVVDIGGGTTGISIL--KDG--KVVYSAdeptGGTHM 170
PRK11678 PRK11678
putative chaperone; Provisional
7-351 6.43e-06

putative chaperone; Provisional


Pssm-ID: 236954 [Multi-domain]  Cd Length: 450  Bit Score: 47.55  E-value: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173   7 IGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTE-------RLIGDAA---KNQVAL--------------N 62
Cdd:PRK11678   3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREavsewlyRHLDVPAyddERQALLrrairynreedidvT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173  63 PQnTVFDAKRLIGRKFGDP----VVQSdmkhwpfqvindgdkPKvqvSYKGETK------AFYpEEISSMVLTKMKEIAE 132
Cdd:PRK11678  83 AQ-SVFFGLAALAQYLEDPeevyFVKS---------------PK---SFLGASGlkpqqvALF-EDLVCAMMLHIKQQAE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 133 AYLGYPVTNAVITVPAYFN-----DSQRQAT---KDAGVIAGLNVLRIINEPTAAaiayGLD--RTGKGERNVLIFDLGG 202
Cdd:PRK11678 143 AQLQAAITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA----GLDfeATLTEEKRVLVVDIGG 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 203 GTFDVSILTIddgifevkataGDTH-----------------LGGEDFDNRL-VNHFV---------------------- 242
Cdd:PRK11678 219 GTTDCSMLLM-----------GPSWrgradrsasllghsgqrIGGNDLDIALaFKQLMpllgmgsetekgialpslpfwn 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 243 -----------EEFKRKHKKDISQNKR------AVRRL-------------RTAcERAKRTLSSSTQASLEIDSLFEGID 292
Cdd:PRK11678 288 avaindvpaqsDFYSLANGRLLNDLIRdarepeKVARLlkvwrqrlsyrlvRSA-EEAKIALSDQAETRASLDFISDGLA 366
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 167466173 293 fyTSITRARFEELCSdlfrSTLEPVEKALRDAkLDKAQIH-DLV-LVGGSTRIPKVQKLLQ 351
Cdd:PRK11678 367 --TEISQQGLEEAIS----QPLARILELVQLA-LDQAQVKpDVIyLTGGSARSPLIRAALA 420
PRK13927 PRK13927
rod shape-determining protein MreB; Provisional
143-276 5.66e-05

rod shape-determining protein MreB; Provisional


Pssm-ID: 237562 [Multi-domain]  Cd Length: 334  Bit Score: 44.31  E-value: 5.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 143 VITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLD---RTGkgernVLIFDLGGGTFDVSILTIdDGIfev 219
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPvtePTG-----SMVVDIGGGTTEVAVISL-GGI--- 170
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 167466173 220 kATAGDTHLGGEDFDNRLVNHfveeFKRKHKKDISQnkravrrlRTAcERAKRTLSS 276
Cdd:PRK13927 171 -VYSKSVRVGGDKFDEAIINY----VRRNYNLLIGE--------RTA-ERIKIEIGS 213
XylB COG1070
Sugar (pentulose and hexulose) kinases [Carbohydrate transport and metabolism]
307-392 1.26e-03

Sugar (pentulose and hexulose) kinases [Carbohydrate transport and metabolism]


Pssm-ID: 223996 [Multi-domain]  Cd Length: 502  Bit Score: 40.44  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 307 SDLFRSTLEPVEKALRDA-----KLDKAQIHDLVLVGGSTRIPKVQKLLQDFFnGRDLNKSiNPDEAVAYGAAVQAAILM 381
Cdd:COG1070  373 AHLARAVLEGVAFALADGlealeELGGKPPSRVRVVGGGARSPLWLQILADAL-GLPVVVP-EVEEAGALGGAALAAAAL 450
                         90
                 ....*....|.
gi 167466173 382 GDKSENVQDLL 392
Cdd:COG1070  451 GGIYDSAEGAL 461
PRK03918 PRK03918
chromosome segregation protein; Provisional
497-602 2.36e-03

chromosome segregation protein; Provisional


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 167466173 497 KANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAK-NALESYAFNMKSAVED-EGLKGK-------ISEADK 567
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARiGELKKEIKELKKAIEElKKAKGKcpvcgreLTEEHR 450
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 167466173 568 KKVLDKCQEVISWLdANTLAEKDEFEHK-RKELEQV 602
Cdd:PRK03918 451 KELLEEYTAELKRI-EKELKEIEEKERKlRKELREL 485
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH