|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-626 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1026.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 1 MARnpVIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGTDWK 80
Cdd:PRK00290 1 MGK--IIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRLMGRRDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 81 R----------------------KIDDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRI 138
Cdd:PRK00290 79 EvqkdiklvpykivkadngdawvEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 139 AGLEVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAI 218
Cdd:PRK00290 159 AGLEVLRIINEPTAAALAYGLDKKGDEKILVYDLGGGTFDVSILEI----GDGVFEVLSTNGDTHLGGDDFDQRIIDYLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 219 SEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMGPTR 298
Cdd:PRK00290 235 DEFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 299 QALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDetVTDVLLLDVTPLTL 378
Cdd:PRK00290 315 QALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGD--VKDVLLLDVTPLSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 379 GIETLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDID 458
Cdd:PRK00290 393 GIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDID 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 459 ANGIVSVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEADDKLDE 538
Cdd:PRK00290 473 ANGIVHVSAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 539 EDTKPVEEKLDELEELIikdgtpipmEDIDDAAIQTKVKELEESMHAISAKLYEAASAQmeadEAAEGMAEDGNEVVDAD 618
Cdd:PRK00290 553 DEKEKIEAAIKELKEAL---------KGEDKEAIKAKTEELTQASQKLGEAMYQQAQAA----QGAAGAAAKDDDVVDAE 619
|
....*...
gi 663513430 619 FEVVDDDN 626
Cdd:PRK00290 620 FEEVKDDK 627
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
6-592 |
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: 274091 [Multi-domain] Cd Length: 595 Bit Score: 887.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGTDWKR---- 81
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNGERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDEvtee 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 82 -----------------KIDDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVL 144
Cdd:TIGR02350 82 akrvpykvvgdggdvrvKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 145 RIINEPTAAALAFGVDKSD-DETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAISEFKK 223
Cdd:TIGR02350 162 RIINEPTAAALAYGLDKSKkDEKILVFDLGGGTFDVSILEI----GDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 224 SSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMGPTRQALKD 303
Cdd:TIGR02350 238 EEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQALKD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 304 SKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDetVTDVLLLDVTPLTLGIETL 383
Cdd:TIGR02350 318 AGLSASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGD--VKDVLLLDVTPLSLGIETL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 384 GGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDIDANGIV 463
Cdd:TIGR02350 396 GGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGIL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 464 SVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEADDKLDEEDTKP 543
Cdd:TIGR02350 476 HVSAKDKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEK 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 663513430 544 VEEKLDELEELiikdgtpipMEDIDDAAIQTKVKELEESMHAISAKLYE 592
Cdd:TIGR02350 556 IEKAVAELKEA---------LKGEDVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
6-623 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 783.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGTDWKR---- 81
Cdd:PRK13411 4 VIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGKSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDteee 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 82 ------------------KIDDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEV 143
Cdd:PRK13411 84 rsrvpytcvkgrddtvnvQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAGLEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 144 LRIINEPTAAALAFGVDKSD-DETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAISEFK 222
Cdd:PRK13411 164 LRIINEPTAAALAYGLDKQDqEQLILVFDLGGGTFDVSILQL----GDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 223 KSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMGPTRQALK 302
Cdd:PRK13411 240 QQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 303 DSKVGKDGIDKVLLIGGSTRVPAVQEAIRKEL-GKDPYKGINPDEAVALGAALQAGIIVGDetVTDVLLLDVTPLTLGIE 381
Cdd:PRK13411 320 DAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFgGKQPDRSVNPDEAVALGAAIQAGVLGGE--VKDLLLLDVTPLSLGIE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 382 TLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDIDANG 461
Cdd:PRK13411 398 TLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 462 IVSVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEADDKLDEEDT 541
Cdd:PRK13411 478 ILKVSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 542 KPVEEKLDELEELIIKDgtpipmeDIDDAAIQTKVKELEESMHAISAKLYEAASAQ---------------------MEA 600
Cdd:PRK13411 558 QRAEQKVEQLEAALTDP-------NISLEELKQQLEEFQQALLAIGAEVYQQGGSQttdtveptsdtlitatmnssnETT 630
|
650 660
....*....|....*....|...
gi 663513430 601 DEAAEGMAEDGNEVVDADFEVVD 623
Cdd:PRK13411 631 LIDEFNFDFDDEETVASDYEAID 653
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
6-619 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 782.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMG--------- 76
Cdd:CHL00094 4 VVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTKKGDLLVGQIAKRQAVINPENTFYSVKRFIGrkfseisee 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 77 ---------TDWKRKID------DAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGL 141
Cdd:CHL00094 84 akqvsykvkTDSNGNIKiecpalNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKIAGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 142 EVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAISEF 221
Cdd:CHL00094 164 EVLRIINEPTAASLAYGLDKKNNETILVFDLGGGTFDVSILEV----GDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 222 KKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMGPTRQAL 301
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 302 KDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDetVTDVLLLDVTPLTLGIE 381
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGE--VKDILLLDVTPLSLGVE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 382 TLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDIDANG 461
Cdd:CHL00094 398 TLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANG 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 462 IVSVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEADDKLDEEDT 541
Cdd:CHL00094 478 ILSVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKK 557
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 663513430 542 KPVEEKLDELEELIIKDgtpipmediDDAAIQTKVKELEESMHAISAKLYEAASaqmeadeaAEGMAEDGNEVVDADF 619
Cdd:CHL00094 558 EKIENLIKKLRQALQND---------NYESIKSLLEELQKALMEIGKEVYSSTS--------TTDPASNDDDVIDTDF 618
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
6-592 |
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: 394970 [Multi-domain] Cd Length: 598 Bit Score: 781.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGTDWKRKIDD 85
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFT-PKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 86 AE--------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIA 139
Cdd:pfam00012 80 RDikhlpykvvklpngdagvevrylgetFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 140 GLEVLRIINEPTAAALAFGVDKSDDE-TILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAI 218
Cdd:pfam00012 160 GLNVLRIVNEPTAAALAYGLDKTDKErNIAVYDLGGGTFDVSILEI----GRGVFEVKATNGDTHLGGEDFDLRLVDHLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 219 SEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQqAQINLPFIT-MVDGQpaHLDLSLSKAKFEDLIGALIEKTMGPT 297
Cdd:pfam00012 236 EEFKKKYGIDLSKDKRALQRLREAAEKAKIELSSNQ-TNINLPFITaMADGK--DVSGTLTRAKFEELVADLFERTLEPV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 298 RQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDETVTDVLLLDVTPLT 377
Cdd:pfam00012 313 EKALKDAGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGTFDVKDFLLLDVTPLS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 378 LGIETLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDI 457
Cdd:pfam00012 393 LGIETLGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDI 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 458 DANGIVSVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEADDKLD 537
Cdd:pfam00012 473 DANGILTVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVP 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 663513430 538 EEDTKPVEEKLDELeeliikdgtPIPMEDIDDAAIQTKVKELEESMHAISAKLYE 592
Cdd:pfam00012 553 EAEKSKVESAIEWL---------KDELEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-532 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 729.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 1 MARnpVIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGTDW- 79
Cdd:PRK13410 1 MGR--IVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTKDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 80 ------KR-----KIDDA------------EYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAG 136
Cdd:PRK13410 79 eldpesKRvpytiRRNEQgnvrikcprlerEFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 137 RIAGLEVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAW 216
Cdd:PRK13410 159 RIAGLEVERILNEPTAAALAYGLDRSSSQTVLVFDLGGGTFDVSLLEV----GNGVFEVKATSGDTQLGGNDFDKRIVDW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 217 AISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMGP 296
Cdd:PRK13410 235 LAEQFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 297 TRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDetVTDVLLLDVTPL 376
Cdd:PRK13410 315 VKRALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGE--LKDLLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 377 TLGIETLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFD 456
Cdd:PRK13410 393 SLGLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFD 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 663513430 457 IDANGIVSVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEA 532
Cdd:PRK13410 473 IDANGILQVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDA 548
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
6-481 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 712.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGTDWK---RK 82
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDGEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFdeaTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 83 IDDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGVDK- 161
Cdd:COG0443 81 VGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLDKg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 162 SDDETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAISEFKKSSGIDLSKDLQAMSRLKE 241
Cdd:COG0443 161 KEEETILVYDLGGGTFDVSILRL----GDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEEGIDLRLDPAALQRLRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 242 AAEKAKIELSNTQQAQINLPFitmvdGQPAHLDLSLSKAKFEDLIGALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGST 321
Cdd:COG0443 237 AAEKAKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDIDAVLLVGGST 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 322 RVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDetVTDvllLDVTPLTLGIETLGGVTTVMIERNTTIPSRR 401
Cdd:COG0443 312 RMPAVRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGD--VKD---LDVTPLSLGIETLGGVFTKLIPRNTTIPTAK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 402 SEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDIDANGIVSVSAKDMGTGKEQSIRIE 481
Cdd:COG0443 387 SQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITIK 466
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
6-619 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 690.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGTDWKRKIDD 85
Cdd:PLN03184 41 VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSEVDEE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 86 A------------------------EYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGL 141
Cdd:PLN03184 121 SkqvsyrvvrdengnvkldcpaigkQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 142 EVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAISEF 221
Cdd:PLN03184 201 EVLRIINEPTAASLAYGFEKKSNETILVFDLGGGTFDVSVLEV----GDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 222 KKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMGPTRQAL 301
Cdd:PLN03184 277 KKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPVENAL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 302 KDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDetVTDVLLLDVTPLTLGIE 381
Cdd:PLN03184 357 RDAKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGE--VSDIVLLDVTPLSLGLE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 382 TLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDIDANG 461
Cdd:PLN03184 435 TLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANG 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 462 IVSVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEADDKLDEEDT 541
Cdd:PLN03184 515 ILSVSATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVK 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 542 KPVEEKLDELEELIIKDGTpipmEDIDDA--AIQTKVKELEESMHAISAKLYEAASAQMEADEAAE-GMAEDGNEVVDAD 618
Cdd:PLN03184 595 EKVEAKLKELKDAIASGST----QKMKDAmaALNQEVMQIGQSLYNQPGAGGAGPAPGGEAGSSSSsSSGGDGDDVIDAD 670
|
.
gi 663513430 619 F 619
Cdd:PLN03184 671 F 671
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
2-613 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 685.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 2 ARNPVIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkR 81
Cdd:PTZ00400 39 ATGDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDGQRLVGIVAKRQAVTNPENTVFATKRLIG----R 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 82 KIDDAE----------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATK 133
Cdd:PTZ00400 115 RYDEDAtkkeqkilpykivrasngdawieaqgkkYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 134 DAGRIAGLEVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqIDGQpqIEVKATAGNNKLGGDDFDDEV 213
Cdd:PTZ00400 195 DAGKIAGLDVLRIINEPTAAALAFGMDKNDGKTIAVYDLGGGTFDISILEI--LGGV--FEVKATNGNTSLGGEDFDQRI 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 214 IAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKT 293
Cdd:PTZ00400 271 LNYLIAEFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKT 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 294 MGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDetVTDVLLLDV 373
Cdd:PTZ00400 351 IEPCEKCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGE--IKDLLLLDV 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 374 TPLTLGIETLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEV 453
Cdd:PTZ00400 429 TPLSLGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 454 AFDIDANGIVSVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEAD 533
Cdd:PTZ00400 509 TFDVDANGIMNISAVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLK 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 534 DKLDEEDTKPVeekldelEELIIKDGTPIPMEDIDdaAIQTKVKELEESMHAISAKLYEAASAQMEADEAAEGMAEDGNE 613
Cdd:PTZ00400 589 DKISDADKDEL-------KQKITKLRSTLSSEDVD--SIKDKTKQLQEASWKISQQAYKQGNSDNQQSEQSTNSEESEEK 659
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
6-359 |
0e+00 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar proteins; This subfamily includes Escherichia coli chaperone protein DnaK (also known as heat shock 70 kDa protein/HSP70), human mitochondrial heat shock 70 kDa protein HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74), Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466832 [Multi-domain] Cd Length: 373 Bit Score: 612.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGTDWKRK--- 82
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDGERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVeve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 83 -------------------IDDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEV 143
Cdd:cd10234 81 rkqvpypvvsagngdawveIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 144 LRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAISEFKK 223
Cdd:cd10234 161 LRIINEPTAAALAYGLDKKKDEKILVYDLGGGTFDVSILEI----GDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 224 SSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMGPTRQALKD 303
Cdd:cd10234 237 EEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKD 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 663513430 304 SKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGII 359
Cdd:cd10234 317 AKLSPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVL 372
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
6-531 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 597.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEgERLVGVSAKRQAVTNSSRTILSVKREMGTD------- 78
Cdd:PTZ00186 29 VIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGS-EKLVGLAAKRQAITNPQSTFYAVKRLIGRRfedehiq 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 79 ------------------WKRKIDDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAG 140
Cdd:PTZ00186 108 kdiknvpykivragngdaWVQDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 141 LEVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAISE 220
Cdd:PTZ00186 188 LNVIRVVNEPTAAALAYGMDKTKDSLIAVYDLGGGTFDISVLEI----AGGVFEVKATNGDTHLGGEDFDLALSDYILEE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 221 FKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMGPTRQA 300
Cdd:PTZ00186 264 FRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPCKQC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 301 LKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDetVTDVLLLDVTPLTLGI 380
Cdd:PTZ00186 344 MKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGD--VKGLVLLDVTPLSLGI 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 381 ETLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDIDAN 460
Cdd:PTZ00186 422 ETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDAN 501
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663513430 461 GIVSVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKE 531
Cdd:PTZ00186 502 GICHVTAKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGE 572
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
1-599 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 554.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 1 MARNPVIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwk 80
Cdd:PTZ00009 1 MTKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVARNPENTVFDAKRLIG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 81 RKIDDA--------------------------------EYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQ 128
Cdd:PTZ00009 76 RKFDDSvvqsdmkhwpfkvttggddkpmievtyqgekkTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 129 RKATKDAGRIAGLEVLRIINEPTAAALAFGVDKSDDE--TILVFDLGGGTFDVSVLEIYqiDGQpqIEVKATAGNNKLGG 206
Cdd:PTZ00009 156 RQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGDGekNVLIFDLGGGTFDVSLLTIE--DGI--FEVKATAGDTHLGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 207 DDFDDEVIAWAISEFK-KSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINL-PFITMVDGQPahldlSLSKAKFED 284
Cdd:PTZ00009 232 EDFDNRLVEFCVQDFKrKNRGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIdSLFEGIDYNV-----TISRARFEE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 285 LIGALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKEL-GKDPYKGINPDEAVALGAALQAGIIVGDE 363
Cdd:PTZ00009 307 LCGDYFRNTLQPVEKVLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFnGKEPCKSINPDEAVAYGAAVQAAILTGEQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 364 T--VTDVLLLDVTPLTLGIETLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGI 441
Cdd:PTZ00009 387 SsqVQDLLLLDVTPLSLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGI 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 442 PPAPRGMPQIEVAFDIDANGIVSVSAKDMGTGKEQSIRIESATS-LSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADS 520
Cdd:PTZ00009 467 PPAPRGVPQIEVTFDIDANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLEN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 521 IIYQTRRTLKEAD--DKLDEEDTKPVEEKLDELEELIIKDGTPIPMEdiddaaIQTKVKELEESMHAISAKLYEAASAQM 598
Cdd:PTZ00009 547 YCYSMKNTLQDEKvkGKLSDSDKATIEKAIDEALEWLEKNQLAEKEE------FEHKQKEVESVCNPIMTKMYQAAGGGM 620
|
.
gi 663513430 599 E 599
Cdd:PTZ00009 621 P 621
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
4-359 |
0e+00 |
|
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and similar proteins; This subgroup includes human mitochondrial HSPA9 (also known as mitochondrial stress-70 protein; mortalin; 75 kDa glucose-regulated protein/GRP-75; HSPA9B; MOT; peptide-binding protein 74/PBP74). It acts as a chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. It interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. HSPA9 regulates erythropoiesis via stabilization of ISC assembly. It may play a role in the control of cell proliferation and cellular aging. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466839 [Multi-domain] Cd Length: 377 Bit Score: 517.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 4 NPVIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKI 83
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADGERLVGMPAKRQAVTNPENTLYATKRLIG----RRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 84 DDAE----------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDA 135
Cdd:cd11733 77 DDPEvqkdikmvpykivkasngdawveahgkkYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 136 GRIAGLEVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIA 215
Cdd:cd11733 157 GQIAGLNVLRIINEPTAAALAYGLDKKDDKIIAVYDLGGGTFDISILEI----QKGVFEVKATNGDTFLGGEDFDNALLN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 216 WAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMG 295
Cdd:cd11733 233 YLVAEFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVE 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663513430 296 PTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGII 359
Cdd:cd11733 313 PCKKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
7-539 |
6.09e-179 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 520.89 E-value: 6.09e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGeRLVGVSAKRQAVTNSSRTILSVKREMG---TDWKRKI 83
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDG-IEVGYEARANAAQDPKNTISSVKRFMGrslADIQQRY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 84 DDAEY-------------------TPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVL 144
Cdd:PRK05183 101 PHLPYqfvasengmplirtaqglkSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLNVL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 145 RIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAWAIsefkKS 224
Cdd:PRK05183 181 RLLNEPTAAAIAYGLDSGQEGVIAVYDLGGGTFDISILRL----SKGVFEVLATGGDSALGGDDFDHLLADWIL----EQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 225 SGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINlpfITMVDGqpahldlSLSKAKFEDLIGALIEKTMGPTRQALKDS 304
Cdd:PRK05183 253 AGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVS---VALWQG-------EITREQFNALIAPLVKRTLLACRRALRDA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 305 KVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDETVTDVLLLDVTPLTLGIETLG 384
Cdd:PRK05183 323 GVEADEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKPDSDMLLLDVIPLSLGLETMG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 385 GVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDIDANGIVS 464
Cdd:PRK05183 403 GLVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLS 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513430 465 VSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEADDKLDEE 539
Cdd:PRK05183 483 VTAMEKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAA 557
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
6-581 |
1.85e-176 |
|
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: 273915 [Multi-domain] Cd Length: 599 Bit Score: 513.74 E-value: 1.85e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKIDD 85
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDGGVEVGKEALAAAAEDPKNTISSVKRLMG----RSIED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 86 AEY-------------------------TPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAG 140
Cdd:TIGR01991 77 IKTfsilpyrfvdgpgemvrlrtvqgtvTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 141 LEVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIYQidgqPQIEVKATAGNNKLGGDDFDDEVIAWAIse 220
Cdd:TIGR01991 157 LNVLRLLNEPTAAAVAYGLDKASEGIYAVYDLGGGTFDVSILKLTK----GVFEVLATGGDSALGGDDFDHALAKWIL-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 221 fkKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLpfitMVDGQpaHLDLSLSKAKFEDLIGALIEKTMGPTRQA 300
Cdd:TIGR01991 231 --KQLGISADLNPEDQRLLLQAARAAKEALTDAESVEVDF----TLDGK--DFKGKLTRDEFEALIQPLVQKTLSICRRA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 301 LKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDETVTDVLLLDVTPLTLGI 380
Cdd:TIGR01991 303 LRDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRIGNDLLLLDVTPLSLGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 381 ETLGGVTTVMIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDIDAN 460
Cdd:TIGR01991 383 ETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDAD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 461 GIVSVSAKDMGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEADDKLDEED 540
Cdd:TIGR01991 463 GLLTVSAQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDE 542
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 663513430 541 TKPVEEKLDELEELIIKDgtpipmediDDAAIQTKVKELEE 581
Cdd:TIGR01991 543 RAAIDAAMEALQKALQGD---------DADAIKAAIEALEE 574
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
5-361 |
2.25e-158 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein Ssc1p and Ssc3p and similar proteins; This subgroup includes Saccharomyces cerevisiae Stress-Seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and sc3p (also called extracellular mutant protein 10/Ecm10). Ssc1p is an essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. It constitutes the ATP-driven core of the motor and binds the precursor preprotein. It is required for the import of the processed frataxin homolog YFH1 into the mitochondrion. Ssc1p also acts as a non-catalytic component of endonuclease SceI (endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks. Ssc1p confers broader sequence specificity, greater stability, and higher activity on the catalytic subunit. Ssc3p plays a role in facilitating the assembly of some protein complexes inside the mitochondria. It may initiate the events that lead to refolding of imported precursors in the matrix space.
Pssm-ID: 466840 [Multi-domain] Cd Length: 378 Bit Score: 459.60 E-value: 2.25e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 5 PVIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKID 84
Cdd:cd11734 2 PVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDGERLVGVPAKRQAVVNPENTLFATKRLIG----RKFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 85 DAE----------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAG 136
Cdd:cd11734 78 DAEvqrdikevpykivkhsngdawveargqkYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 137 RIAGLEVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIYQidgqPQIEVKATAGNNKLGGDDFDDEVIAW 216
Cdd:cd11734 158 QIAGLNVLRVINEPTAAALAYGLDKSGDKVIAVYDLGGGTFDISILEIQK----GVFEVKSTNGDTHLGGEDFDIALVRH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 217 AISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMVDGQPAHLDLSLSKAKFEDLIGALIEKTMGP 296
Cdd:cd11734 234 IVSEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663513430 297 TRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVG 361
Cdd:cd11734 314 CKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
6-359 |
9.78e-153 |
|
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The HSPA1-like family includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10), HSPA13 (also known as 70-kDa heat shock protein 13; STCH; microsomal stress-70 protein ATPase core; stress-70 protein chaperone microsome-associated 60 kDa protein), as well as Saccharmoyces cerevisiae Hsp70 chaperone Ssb1-2 and heat shock protein Ssa1-4. HSPA1A/1B, HSPA1L, HSPA2 and HSPA6-8 are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). HSPA13 has peptide-independent ATPase activity. All family members belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466878 [Multi-domain] Cd Length: 376 Bit Score: 445.03 E-value: 9.78e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKIDD 85
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFT-DGERLVGEAAKNQAASNPENTIFDVKRLIG----RKFDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 86 AE--------------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATK 133
Cdd:cd24028 76 PSvqsdikhwpfkvvededgkpkievtykgeektFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 134 DAGRIAGLEVLRIINEPTAAALAFGVDK--SDDETILVFDLGGGTFDVSVLEiyqIDGQpQIEVKATAGNNKLGGDDFDD 211
Cdd:cd24028 156 DAATIAGLNVLRIINEPTAAALAYGLDKksSGERNVLVFDLGGGTFDVSLLS---IDNG-VFEVKATAGDTHLGGEDFDN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 212 EVIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFItmVDGQPahLDLSLSKAKFEDLIGALIE 291
Cdd:cd24028 232 RLVEYLVEEFKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSL--YDGID--FETTITRAKFEELCEDLFK 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663513430 292 KTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKEL-GKDPYKGINPDEAVALGAALQAGII 359
Cdd:cd24028 308 KCLEPVEKVLKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFFgGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
5-359 |
2.19e-147 |
|
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; This subfamily includes human BiP (also known as HSP70 family protein 5 /HSPA5; 70-kDa heat shock protein 5; glucose-regulated protein 78/GRP78; immunoglobulin heavy chain-binding protein), Sacchaormyces cerevisiae BiP (also known as Grp78p), Arabidopsis thaliana BiP1-3 (also known as luminal-binding protein 1-3) and related proteins. BiP plays a key role in protein folding and quality control in the endoplasmic reticulum lumen. It plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). BiP may function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. It appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. BiP may also play a role in apoptosis and cell proliferation. Plant BiP may be required for pollen development and pollen tube growth. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466837 [Multi-domain] Cd Length: 376 Bit Score: 431.25 E-value: 2.19e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 5 PVIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKID 84
Cdd:cd10241 2 TVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFT-DGERLIGDAAKNQATSNPENTVFDVKRLIG----RKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 85 DAE-------------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATK 133
Cdd:cd10241 77 DKEvqkdikllpfkivnkngkpyiqvevkgekktFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 134 DAGRIAGLEVLRIINEPTAAALAFGVDKSDDE-TILVFDLGGGTFDVSVLeiyQIDGQpQIEVKATAGNNKLGGDDFDDE 212
Cdd:cd10241 157 DAGTIAGLNVLRIINEPTAAAIAYGLDKKGGEkNILVFDLGGGTFDVSLL---TIDNG-VFEVLATNGDTHLGGEDFDQR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 213 VIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPfiTMVDGQpahlDLS--LSKAKFEDLIGALI 290
Cdd:cd10241 233 VMDHFIKLFKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIE--SLFDGE----DFSetLTRAKFEELNMDLF 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663513430 291 EKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIrKEL--GKDPYKGINPDEAVALGAALQAGII 359
Cdd:cd10241 307 RKTLKPVQKVLEDAGLKKSDIDEIVLVGGSTRIPKVQQLL-KDFfnGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
7-360 |
6.62e-146 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and similar proteins; Escherichia coli DnaK, also called heat shock 70 kDa protein/HSP70, plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Moreover, DnaK participates actively in the response to hyperosmotic shock. Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. The family also includes Saccharomyces cerevisiae stress-seventy subfamily C proteins, Ssc1p (also called import motor subunit, mitochondrial; endonuclease SceI 75 kDa subunit; mtHSP70; ENS1; endonuclease SceI 75 kDa subunit) and Ssc3p (also called extracellular mutant protein 10/Ecm10), and Saccharomyces cerevisiae Stress-seventy subfamily Q protein 1/Ssq1p (also called Ssc2p; Ssh1p; mtHSP70 homolog). They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs); for Escherichia coli DnaK, these are the DnaJ and GrpE, respectively.
Pssm-ID: 466879 [Multi-domain] Cd Length: 351 Bit Score: 426.61 E-value: 6.62e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGES-VVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGTD--WKRKI 83
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAeVIIENSEGKRTTPSVVYFDKDGEVLVGEEAKNQALLDPENTIYSVKRLMGRDtkDKEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 84 DDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGVDK-S 162
Cdd:cd24029 81 GGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNVLRLINEPTAAALAYGLDKeG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 163 DDETILVFDLGGGTFDVSVLEIYqiDGqpQIEVKATAGNNKLGGDDFDDEVIAWAISEFKKSSGI-DLSKDLQAMSRLKE 241
Cdd:cd24029 161 KDGTILVYDLGGGTFDVSILEIE--NG--KFEVLATGGDNFLGGDDFDEAIAELILEKIGIETGIlDDKEDERARARLRE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 242 AAEKAKIELSNTQQAQINLPFitmvDGQPAHLDLSLSKAKFEDLIGALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGST 321
Cdd:cd24029 237 AAEEAKIELSSSDSTDILILD----DGKGGELEIEITREEFEELIAPLIERTIDLLEKALKDAKLSPEDIDRVLLVGGSS 312
|
330 340 350
....*....|....*....|....*....|....*....
gi 663513430 322 RVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIV 360
Cdd:cd24029 313 RIPLVREMLEEYFGREPISSVDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
6-361 |
8.54e-135 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar proteins; Escherichia coli HscA, also called Hsc66, acts as a chaperone involved in the maturation of iron-sulfur cluster-containing proteins. It has a low intrinsic ATPase activity which is markedly stimulated by HscB. It is involved in the maturation of IscU. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HscA's partner J-domain protein is HscB; it does not appear to require a NEF and has been shown to be induced by cold-shock. The HscA-HscB chaperone/co-chaperone pair is involved in [Fe-S] cluster assembly.
Pssm-ID: 466834 [Multi-domain] Cd Length: 367 Bit Score: 398.90 E-value: 8.54e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMG-------TD 78
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITVGEKAKENAITDPENTISSVKRLMGrsladvkEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 79 WKR---------------KIDDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEV 143
Cdd:cd10236 84 LPLlpyrlvgdenelprfRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAGLNV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 144 LRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIYqiDGqpQIEVKATAGNNKLGGDDFDDEVIAWaiseFKK 223
Cdd:cd10236 164 LRLLNEPTAAALAYGLDQKKEGTIAVYDLGGGTFDISILRLS--DG--VFEVLATGGDTALGGDDFDHLLADW----ILK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 224 SSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPfitmVDGQPAhlDLSLSKAKFEDLIGALIEKTMGPTRQALKD 303
Cdd:cd10236 236 QIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVE----VEGKDW--EREITREEFEELIQPLVKRTLEPCRRALKD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 663513430 304 SKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVG 361
Cdd:cd10236 310 AGLEPADIDEVVLVGGSTRIPLVRQRVAEFFGREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
7-359 |
3.02e-129 |
|
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; This subfamily includes human HSPA1A (70-kDa heat shock protein 1A, also known as HSP72; HSPA1; HSP70I; HSPA1B; HSP70-1; HSP70-1A), HSPA1B (70-kDa heat shock protein 1B, also known as HSPA1A; HSP70-2; HSP70-1B), and HSPA1L (70-kDa heat shock protein 1-like, also known as HSP70T; hum70t; HSP70-1L; HSP70-HOM), HSPA2 (70-kDa heat shock protein 2, also known as HSP70-2; HSP70-3), HSPA6 (also known as heat shock 70kDa protein 6; HSP70B'), HSPA7 (heat shock 70kDa protein 7 , also known as HSP70B), and HSPA8 (heat shock 70kDa protein 8, also known as Lipopolysaccharide-associated protein 1/LAP1; HSC70; HSP73; HSPA10). They are molecular chaperones implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. They play pivotal roles in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The subfamily also includes Saccharomyces cerevisiae heat shock protein Ssa1-4, which may play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. This subfamily belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466831 [Multi-domain] Cd Length: 375 Bit Score: 384.67 E-value: 3.02e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKIDDA 86
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFT-DTERLIGDAAKNQVAMNPTNTVFDAKRLIG----RKFDDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 87 E-------------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDA 135
Cdd:cd10233 77 VvqsdmkhwpfkvvsggdkpkiqveykgetktFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 136 GRIAGLEVLRIINEPTAAALAFGVDKSD--DETILVFDLGGGTFDVSVLEIyqidgQPQI-EVKATAGNNKLGGDDFDDE 212
Cdd:cd10233 157 GTIAGLNVLRIINEPTAAAIAYGLDKKGkgERNVLIFDLGGGTFDVSLLTI-----EDGIfEVKATAGDTHLGGEDFDNR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 213 VIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPfiTMVDGqpahLDL--SLSKAKFEDLIGALI 290
Cdd:cd10233 232 LVNHFVQEFKRKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEID--SLFEG----IDFytSITRARFEELCADLF 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 291 EKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKEL-GKDPYKGINPDEAVALGAALQAGII 359
Cdd:cd10233 306 RSTLEPVEKVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFFnGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
7-361 |
6.83e-120 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar proteins; Escherichia coli HscC, also called Hsc62, or YbeW, may act as the chaperone. It has ATPase activity. It cannot be stimulated by DnaJ. Members in this subfamily belong to the heat shock protein 70 (Hsp70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, Hsp70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Two genes in the vicinity of the HscC gene code for potential cochaperones: J-domain containing proteins, DjlB/YbeS and DjlC/YbeV. HscC and its co-chaperone partners may play a role in the SOS DNA damage response. HscC does not appear to require a NEF.
Pssm-ID: 466833 [Multi-domain] Cd Length: 343 Bit Score: 359.64 E-value: 6.83e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKREMGTDWKRKIDDA 86
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDGSILVGRAAKERLVTHPDRTAASFKRFMGTDKQYRLGNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 87 EYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGVDKSDDET 166
Cdd:cd10235 81 TFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVERLINEPTAAALAYGLHKREDET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 167 -ILVFDLGGGTFDVSVLEIYqidgQPQIEVKATAGNNKLGGDDFDDEVIAWAISEFKKSSgidLSKDLQAMSRLKEAAEK 245
Cdd:cd10235 161 rFLVFDLGGGTFDVSVLELF----EGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDF---TSLSPSELAALRKRAEQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 246 AKIELSNTQQAQINLpfitMVDGQpaHLDLSLSKAKFEDLIGALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPA 325
Cdd:cd10235 234 AKRQLSSQDSAEIRL----TYRGE--ELEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAVILVGGATRMPL 307
|
330 340 350
....*....|....*....|....*....|....*.
gi 663513430 326 VQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVG 361
Cdd:cd10235 308 VRQLIARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
7-359 |
8.47e-111 |
|
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar proteins; Ssb is ribosome-bound, Hsp70-type chaperone that assists in the co-translational folding of newly synthesized proteins in the cytosol. It stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Saccharmoyces cerevisiae Ssb are encoded by two genes, SSB1 and SSB2. Ssb1p is also known as cold-inducible protein YG101. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466943 [Multi-domain] Cd Length: 375 Bit Score: 337.34 E-value: 8.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGESVvIANSEGARTTPSVVAFTTEgERLVGVSAKRQAVTNSSRTILSVKREMG---------- 76
Cdd:cd24093 2 IGIDLGTTYSCVATYESSVEI-IANEQGNRVTPSFVAFTPE-ERLIGDAAKNQAALNPRNTVFDAKRLIGrrfddesvqk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 77 --TDWKRKIDDAE---------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIA 139
Cdd:cd24093 80 dmKTWPFKVIDVNgnpvievqylgetktFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 140 GLEVLRIINEPTAAALAFGVD--KSDDE-TILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFDDEVIAW 216
Cdd:cd24093 160 GLNVLRIINEPTAAAIAYGLGagKSEKErHVLIFDLGGGTFDVSLLHI----AGGVYTVKSTSGNTHLGGQDFDTNLLEH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 217 AISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPfiTMVDGQpaHLDLSLSKAKFEDLIGALIEKTMGP 296
Cdd:cd24093 236 FKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVD--SLFDGE--DFESSITRARFEDLNAALFKSTLEP 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663513430 297 TRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKEL-GKDPYKGINPDEAVALGAALQAGII 359
Cdd:cd24093 312 VEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFdGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
6-540 |
2.12e-105 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 331.05 E-value: 2.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEG------------ERLVGVSAKRqaVTNSSRTILSVKR 73
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNftignnkglrsiKRLFGKTLKE--ILNTPALFSLVKD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 74 EM---GTDWKRKIDDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEP 150
Cdd:PRK01433 99 YLdvnSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFEVLRLIAEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 151 TAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidgQPQI-EVKATAGNNKLGGDDFDDEVIAWAISEFkkssgiDL 229
Cdd:PRK01433 179 TAAAYAYGLNKNQKGCYLVYDLGGGTFDVSILNI-----QEGIfQVIATNGDNMLGGNDIDVVITQYLCNKF------DL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 230 SKDLQAMsrlkEAAEKAKIELSNTQQAQINlpfitmvdgqpahlDLSLSKAKFEDLIGALIEKTMGPTRQALKDSkvGKD 309
Cdd:PRK01433 248 PNSIDTL----QLAKKAKETLTYKDSFNND--------------NISINKQTLEQLILPLVERTINIAQECLEQA--GNP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 310 GIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDETvtDVLLLDVTPLTLGIETLGGVTTV 389
Cdd:PRK01433 308 NIDGVILVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHT--NSLLIDVVPLSLGMELYGGIVEK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 390 MIERNTTIPSRRSEVFSTASDNQPAVEIHVLQGEREFARDNITLGRFFLEGIPPAPRGMPQIEVAFDIDANGIVSVSAKD 469
Cdd:PRK01433 386 IIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILSVSAYE 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663513430 470 MGTGKEQSIRIESATSLSEDDIQTKIAEAEQFAEEDSSKKAKVELRNQADSIIYQTRRTLKEADDKLDEED 540
Cdd:PRK01433 466 KISNTSHAIEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESE 536
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
6-361 |
6.31e-102 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; HSPA13, also called 70-kDa heat shock protein 13, STCH, microsomal stress-70 protein ATPase core, or stress-70 protein chaperone microsome-associated 60 kDa protein, has peptide-independent ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA13 contains an NBD but lacks an SBD. It may function to regulate cell proliferation and survival and modulate the TRAIL-mediated cell death pathway. The HSPA13 gene is a candidate stomach cancer susceptibility gene; a mutation in the NBD coding region of HSPA13 has been identified in stomach cancer cells. The NBD of HSPA13 interacts with the ubiquitin-like proteins Chap1 and Chap2, implicating HSPA13 in regulating cell cycle and cell death events. HSPA13 is induced by the Ca2+ ionophore A23187.
Pssm-ID: 466835 [Multi-domain] Cd Length: 409 Bit Score: 315.82 E-value: 6.31e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEG--GESVVIANSEGARTTPSVVAFTTEGERLVGVSAKRQAVTNSSRTILSVKR---------E 74
Cdd:cd10237 24 IVGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTPDGGVLVGYDALAQAEHNPSNTIYDAKRfigktftkeE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 75 MGTDWKR--------KIDDAEY-----------TPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDA 135
Cdd:cd10237 104 LEEEAKRypfkvvndNIGSAFFevplngstlvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRKA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 136 GRIAGLEVLRIINEPTAAALAFGV-DKSDDETILVFDLGGGTFDVSVLEIyqidgQPQI-EVKATAGNNKLGGDDFDDEV 213
Cdd:cd10237 184 ANLAGLEVLRVINEPTAAAMAYGLhKKSDVNNVLVVDLGGGTLDVSLLNV-----QGGMfLTRAMAGNNHLGGQDFNQRL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 214 IAWAISEFKKSSG--IDLSKDLQamsRLKEAAEKAKIELSNTQQAQINLPF-ITMVDGQPAHLDLSLSKAKFEDLIGALI 290
Cdd:cd10237 259 FQYLIDRIAKKFGktLTDKEDIQ---RLRQAVEEVKLNLTNHNSASLSLPLqISLPSAFKVKFKEEITRDLFETLNEDLF 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663513430 291 EKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVG 361
Cdd:cd10237 336 QRVLEPIRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
5-359 |
1.43e-89 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; HSPA14, also called HSP70-like protein 1 (Hsp70L1), or heat shock protein HSP60, is a component of the ribosome-associated complex (RAC), a complex involved in folding or maintaining nascent polypeptides in a folding-competent state. In the RAC complex, HSPA14 binds to the nascent polypeptide chain, while DNAJC2 stimulates its ATPase activity. It belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.
Pssm-ID: 466836 [Multi-domain] Cd Length: 377 Bit Score: 282.59 E-value: 1.43e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 5 PVIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKID 84
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFT-DNEKIVGLAAKQGLIRNASNTVVRVKQLLG----RSFD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 85 DAE-------------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATK 133
Cdd:cd10238 76 DPAvqelkkeskckiiekdgkpgyeieleekkklVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 134 DAGRIAGLEVLRIINEPTAAALAFGVDKSDDE---TILVFDLGGGTFDVSVLEIyqIDGqpQIEVKATAGNNKLGGDDFD 210
Cdd:cd10238 156 EAAEKAGFNVLRVISEPSAAALAYGIGQDDPTensNVLVYRLGGTSLDVTVLSV--NNG--MYRVLATRTDDNLGGDDFT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 211 DEVIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQInlpFI-TMVDGQpaHLDLSLSKAKFEDLIGAL 289
Cdd:cd10238 232 EALAEHLASEFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATC---SVeSLYDGM--DFQCNVSRARFESLCSSL 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 663513430 290 IEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKEL-GKDPYKGINPDEAVALGAALQAGII 359
Cdd:cd10238 307 FQQCLEPIQEVLNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLFpSAEVLSSIPPDEVIAIGAAKQAGLL 377
|
|
| ASKHA_NBD_HSP70_HSP105-110-like |
cd11732 |
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa ... |
7-356 |
5.44e-85 |
|
nucleotide-binding domain (NBD) of the 105/110 kDa heat shock protein family; The 105/110 kDa heat shock proteins family includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25), Saccharomyces cerevisiae Sse1p, Sse2p and a sea urchin sperm receptor. They all belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466838 [Multi-domain] Cd Length: 377 Bit Score: 270.58 E-value: 5.44e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGTDWKRKIDDA 86
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFT-EKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 87 E----------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRI 138
Cdd:cd11732 80 EikllpfklveledgkvgievsyngeevvFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 139 AGLEVLRIINEPTAAALAFGVDKS------DDETILVF-DLGGGTFDVSVLEIYqidgQPQIEVKATAGNNKLGGDDFDD 211
Cdd:cd11732 160 AGLNCLRLINETTAAALDYGIYKSdlleseEKPRIVAFvDMGHSSTQVSIAAFT----KGKLKVLSTAFDRNLGGRDFDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 212 EVIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFItMVDgqpahLDLS--LSKAKFEDLIGAL 289
Cdd:cd11732 236 ALVEHFAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECL-MED-----IDFSgqIKREEFEELIQPL 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663513430 290 IEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQA 356
Cdd:cd11732 310 LARLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQA 376
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
6-356 |
4.25e-81 |
|
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; This subgroup includes human HYOU1 (also known as human hypoxia up-regulated 1, 170 kDa glucose-regulated protein/GRP170; HSP12A; 150 kDa oxygen-regulated protein/ORP150; GRP-170; ORP-150) and Saccharomyces cerevisiae Lhs1p (also known as Cer1p, SsI1). Mammalian HYOU1 has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. It may play a role as a molecular chaperone and participate in protein folding. HYOU1 functions as a nucleotide exchange factor (NEF) for HSPA5 (also known as BiP, Grp78 or HspA5) and may also act as a HSPA5-independent chaperone. S. cerevisiae Lhs1p, does not have a detectable endogenous ATPase activity like canonical HSP70s, but functions as a NEF for Kar2p; it's interaction with Kar2p is stimulated by nucleotide-binding. In addition, Lhs1p has a nucleotide-independent holdase activity that prevents heat-induced aggregation of proteins in vitro. Members in this subgroup belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs).
Pssm-ID: 466828 [Multi-domain] Cd Length: 353 Bit Score: 259.73 E-value: 4.25e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIA-NSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkrkid 84
Cdd:cd10230 2 VLGIDLGSEFIKVALVKPGVPFEIVlNEESKRKTPSAVAFR-NGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 85 daeYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGVDKSDD 164
Cdd:cd10230 73 ---YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSLINDNTAAALNYGIDRRFE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 165 ----ETILVFDLGGGTFDVSVLEIYQIDG--------QPQIEVKATAGNNKLGGDDFDDEVIAWAISEFKKSSGI--DLS 230
Cdd:cd10230 150 nnepQNVLFYDMGASSTSATVVEFSSVKEkdkgknktVPQVEVLGVGWDRTLGGLEFDLRLADHLADEFNEKHKKdkDVR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 231 KDLQAMSRLKEAAEKAKIELS-NTQ-QAQINlpfiTMVDGQpaHLDLSLSKAKFEDLIGALIEKTMGPTRQALKDSKVGK 308
Cdd:cd10230 230 TNPRAMAKLLKEANRVKEVLSaNTEaPASIE----SLYDDI--DFRTKITREEFEELCADLFERVVAPIEEALEKAGLTL 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 663513430 309 DGIDKVLLIGGSTRVPAVQEAIRKELGKDPY-KGINPDEAVALGAALQA 356
Cdd:cd10230 304 DDIDSVELIGGGTRVPKVQEALKEALGRKELgKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
7-356 |
6.47e-76 |
|
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; This subgroup includes the human proteins, HSPA4 (also known as 70-kDa heat shock protein 4; APG-2; HS24/P52; hsp70 RY; HSPH2), HSPA4L (also known as 70-kDa heat shock protein 4-like; APG-1; HSPH3; OSP94), and HSPH1 (also known as heat shock 105kDa/110kDa protein 1; HSP105; HSP105A; HSP105B; NY-CO-25). They belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466826 [Multi-domain] Cd Length: 378 Bit Score: 247.19 E-value: 6.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKIDD- 85
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFG-EKNRSMGVAAKNQAITNLKNTVSGFKRLLG----RKFDDp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 86 ---AE----------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKD 134
Cdd:cd10228 76 fvqKElkhlpykvvklpngsvgikvqylgeehvFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 135 AGRIAGLEVLRIINEPTAAALAFGVDKSD----DET--ILVF-DLGGGTFDVSVLEIYqidgQPQIEVKATAGNNKLGGD 207
Cdd:cd10228 156 AAQIAGLNCLRLLNDTTAVALAYGIYKQDlpaeEEKprNVVFvDMGHSSLQVSVCAFN----KGKLKVLATAADPNLGGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 208 DFDDEVIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELS-NTQQAQINLPFItMVDgqpahLDLS--LSKAKFED 284
Cdd:cd10228 232 DFDELLVEHFAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSaNATELPLNIECF-MDD-----KDVSgkMKRAEFEE 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663513430 285 LIGALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQA 356
Cdd:cd10228 306 LCAPLFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
6-355 |
4.51e-75 |
|
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and similar proteins; The subgroup includes Arabidopsis thaliana Hsp70-14, also known as heat shock 70 kDa protein 14; heat shock protein 91), Hsp70-15 (also known as heat shock 70 kDa protein 15), and Hsp70-16 (also known as heat shock 70 kDa protein 16). In cooperation with other chaperones, they are key components that facilitate folding of de novo synthesized proteins, assist translocation of precursor proteins into organelles, and are responsible for degradation of damaged protein under stress conditions. Members in this subgroup belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466945 [Multi-domain] Cd Length: 389 Bit Score: 245.30 E-value: 4.51e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKIDD 85
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFG-EKQRFLGEAAAASILMNPKNTISQLKRLIG----RKFDD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 86 AE--------------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATK 133
Cdd:cd24095 78 PEvqrdlklfpfkvtegpdgeiginvnylgeqkvFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 134 DAGRIAGLEVLRIINEPTAAALAFGVDKSD-DET----ILVFDLGGGTFDVSVLEIYqidgQPQIEVKATAGNNKLGGDD 208
Cdd:cd24095 158 DAAQIAGLNCLRLMNETTATALAYGIYKTDlPETdptnVVFVDVGHSSTQVCVVAFK----KGQLKVLSHAFDRNLGGRD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 209 FDDEVIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFItMVDgqpahLDLS--LSKAKFEDLI 286
Cdd:cd24095 234 FDEVLFDHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECL-MED-----KDVKgmITREEFEELA 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 663513430 287 GALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQ 355
Cdd:cd24095 308 APLLERLLEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
7-359 |
1.77e-70 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and similar proteins; The subgroup includes two Saccharomyces cerevisiae heat shock protein homologs, Sse1 and Sse2. They may have calcium-dependent calmodulin-binding activities. Both Sse1 and Sse2 belong to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family, and includes proteins believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466944 [Multi-domain] Cd Length: 385 Bit Score: 233.04 E-value: 1.77e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGtdwkRKIDDA 86
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFG-PKSRYLGEAAKTQETSNFKNTVGSLKRLIG----RTFSDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 87 EYTPQE-------------------------------ISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDA 135
Cdd:cd24094 76 EVAEEEkyftaklvdangevgaevnylgekhvfsatqLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 136 GRIAGLEVLRIINEPTAAALAFGVDKSD------DETILVF-DLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDD 208
Cdd:cd24094 156 AEIAGLNPLRLMNDTTAAALGYGITKTDlpepeeKPRIVAFvDIGHSSYTVSIVAF----KKGQLTVKGTAYDRHFGGRD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 209 FDDEVIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFItMVDgqpahLDLS--LSKAKFEDLI 286
Cdd:cd24094 232 FDKALTDHFADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESL-MND-----IDVSsmLKREEFEELI 305
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663513430 287 GALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGII 359
Cdd:cd24094 306 APLLERVTAPLEKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFACAIL 378
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
5-359 |
2.77e-67 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex subunit Ssz1 and similar proteins; Ssz1, also called DnaK-related protein Ssz1, heat shock protein 70 homolog Ssz1, or pleiotropic drug resistance protein 13 (PDR13), is a component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones Ssb1/Ssb2 that bind to the nascent polypeptide chain. Ssz1 is required for Zuo1 to function efficiently as a J-protein for Ssb1/Ssb2. It is also involved in pleiotropic drug resistance by post-translational activation of transcription factor PDR1. Members in this subfamily belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis.
Pssm-ID: 466830 [Multi-domain] Cd Length: 349 Bit Score: 223.39 E-value: 2.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 5 PVIGIDLGTTNCCVATI-EGGESVVIANSEGARTTPSVVAFTtEGERLVGVSAKRQAVTNSSRTILSVKREMGTdwkrki 83
Cdd:cd10232 1 VVIGISFGNSNSSIAIInKDGRAEVIANEDGDRQIPSILAYH-GDEEYHGSQAKAQLVRNPKNTVANFRDLLGT------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 84 ddAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGV---- 159
Cdd:cd10232 74 --TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAYDLraet 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 160 --DKSDDETILVFDLGGGTFDVSVLE----IYQIdgqpqievKATAGNNKLGGDDFDDEVIAWAISEFKKSSGIDLSKDL 233
Cdd:cd10232 152 sgDTIKDKTVVVADLGGTRSDVTVVAvrggLYTI--------LATVHDYELGGVALDDVLVGHFAKEFKKKTKTDPRKNA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 234 QAMSRLKEAAEKAKIELSNTQQAQINLPfiTMVDGQPAHldLSLSKAKFEDLIGALIEKTMGPTRQALKDSKVGKDGIDK 313
Cdd:cd10232 224 RSLAKLRNAAEITKRALSQGTSAPCSVE--SLADGIDFH--SSINRTRYELLASKVFQQFADLVTDAIEKAGLDPLDIDE 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 663513430 314 VLLIGGSTRVPAVQEAIRKELGKDPYK----GINPDEAVALGAALQAGII 359
Cdd:cd10232 300 VLLAGGASRTPKLASNFEYLFPESTIIraptQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
6-358 |
2.24e-63 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; HSPA4, also called HSP70RY, , HS24/P52, hsp70 RY, and HSPH2, or heat shock 70-related protein APG-2, responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466843 [Multi-domain] Cd Length: 381 Bit Score: 214.03 E-value: 2.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEgERLVGVSAKRQAVTNSSRTILSVKREMGTDWKRKIDD 85
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPK-NRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 86 AE----------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGR 137
Cdd:cd11737 81 AEkpslayelvqlptgttgikvmymeeernFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 138 IAGLEVLRIINEPTAAALAFGVDKSD------DETILVF-DLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFD 210
Cdd:cd11737 161 IAGLNCLRLMNETTAVALAYGIYKQDlpapeeKPRNVVFvDMGHSAYQVSVCAF----NKGKLKVLATAFDPTLGGRKFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 211 DEVIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELS-NTQQAQINLP-FITMVDgqpahLDLSLSKAKFEDLIGA 288
Cdd:cd11737 237 EVLVNHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSaNASDLPLNIEcFMNDID-----VSGTMNRGQFEEMCAD 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 289 LIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGI 358
Cdd:cd11737 312 LLARVEPPLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
6-355 |
1.00e-60 |
|
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar proteins; HSPH1, also called heat shock protein 105 kDa, antigen NY-CO-25, heat shock 110 kDa protein, acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. It prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. It inhibits HSPA8/HSC70 ATPase and chaperone activities. HSPH1 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466845 [Multi-domain] Cd Length: 380 Bit Score: 207.02 E-value: 1.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEgERLVGVSAKRQAVTNSSRTILSVKREMGTDWKRKIDD 85
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSK-NRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 86 AE----------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGR 137
Cdd:cd11739 81 KEkenlsydlvplknggvgvkvmyldeehhFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 138 IAGLEVLRIINEPTAAALAFGVDKSD----DE--TILVF-DLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFD 210
Cdd:cd11739 161 IVGLNCLRLMNDMTAVALNYGIYKQDlpapDEkpRIVVFvDMGHSAFQVSACAF----NKGKLKVLGTAFDPYLGGRNFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 211 DEVIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKiELSNTQQAQINLPFITMVDgqpaHLDLS--LSKAKFEDLIGA 288
Cdd:cd11739 237 EKLVEHFCAEFKTKYKLDVKSKIRALLRLYQECEKLK-KLMSSNSTDLPLNIECFMN----DKDVSgkMNRSQFEELCAD 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663513430 289 LIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQ 355
Cdd:cd11739 312 LLQRIEVPLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
6-359 |
5.94e-59 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; HSPA4L, also called heat shock 70-related protein APG-1, heat-shock protein family A member 4-like protein, HSPA4-like protein, osmotic stress protein 94, or HSPH3, possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase. It is expressed ubiquitously and predominantly in the testis. It is required for normal spermatogenesis and plays a role in osmotolerance. HSPA4L belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.
Pssm-ID: 466844 [Multi-domain] Cd Length: 383 Bit Score: 202.45 E-value: 5.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEgERLVGVSAKRQAVTNSSRTILSVKREMGTDWKRKIDD 85
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSR-NRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 86 AE----------------------------YTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGR 137
Cdd:cd11738 81 AEkiklpyelqkmpngstgvkvryldeervFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 138 IAGLEVLRIINEPTAAALAFGVDKSD----DET---ILVFDLGGGTFDVSVLEIyqidGQPQIEVKATAGNNKLGGDDFD 210
Cdd:cd11738 161 IAGLNCLRLMNETTAVALAYGIYKQDlpalEEKprnVVFVDMGHSAYQVSICAF----NKGKLKVLATTFDPYLGGRNFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 211 DEVIAWAISEFKKSSGIDLSKDLQAMSRLKEAAEKAKIELS-NTQQAQINLPFItMVDgqpahLDLS--LSKAKFEDLIG 287
Cdd:cd11738 237 EVLVDYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSaNASDLPLNIECF-MND-----IDVSskMNRAQFEELCA 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663513430 288 ALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQAGII 359
Cdd:cd11738 311 SLLARVEPPLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAIL 382
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
7-354 |
3.88e-54 |
|
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family chaperones assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some HSP70 family members are not chaperones but instead, function as NEFs to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle, some may function as both chaperones and NEFs. The HSP70 family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466811 [Multi-domain] Cd Length: 329 Bit Score: 187.70 E-value: 3.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVAtieggesvviansegarttpsvVAFTTEGERLVGVSakrqavtnssrtilsvkremGTDWKRKIDDA 86
Cdd:cd10170 1 VGIDFGTTYSGVA----------------------YALLGPGEPPLVVL--------------------QLPWPGGDGGS 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 87 EYTPQ--EISAFILQKLKADAEDYLGQEVK-------QAVITCPAYFTDAQRKATKDAGRIAGL----EVLRIINEPTAA 153
Cdd:cd10170 39 SKVPSvlEVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALREAARAAGFgsdsDNVRLVSEPEAA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 154 ALAFGVDKSD------DETILVFDLGGGTFDVSVLEIYQIDGQPQIEVkATAGNNKLGGDDFDDEVIAWAISEFKKSSGI 227
Cdd:cd10170 119 ALYALEDKGDllplkpGDVVLVCDAGGGTVDLSLYEVTSGSPLLLEEV-APGGGALLGGTDIDEAFEKLLREKLGDKGKD 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 228 DLSKDLQAMSRLKEAAEKAKIELSNTQQAQINLPFITMvDGQPAHLDLSLSKAKFEDLIGALIEKTMGPTRQALKDSKVG 307
Cdd:cd10170 198 LGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLG-GGLPELGLEKGTLLLTEEEIRDLFDPVIDKILELIEEQLEA 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 663513430 308 KDG--IDKVLLIGGSTRVPAVQEAIRKELGKDP----YKGINPDEAVALGAAL 354
Cdd:cd10170 277 KSGtpPDAVVLVGGFSRSPYLRERLRERFGSAGiiivLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
7-354 |
5.08e-46 |
|
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar proteins; The family includes a group of uncharacterized proteins similar to Escherichia coli chaperone protein YegD that belongs to the heat shock protein 70 family of chaperones that assist in protein folding and assembly and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. YegD lacks the SBD. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). Some family members are not chaperones but instead, function as NEFs for their Hsp70 partners, other family members function as both chaperones and NEFs.
Pssm-ID: 466829 [Multi-domain] Cd Length: 409 Bit Score: 167.84 E-value: 5.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVVAFTTEGERL-----VGVSAKRQAVTN--SSRTILSVKREMGTDW 79
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREEEGaesiyFGNDAIDAYLNDpeEGRLIKSVKSFLGSSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 80 --KRKIDDAEYTPQEISAFILQKLKADAEDYLGQEVKQAVITCPAYFT------DAQRKAT-KDAGRIAGLEVLRIINEP 150
Cdd:cd10231 81 fdETTIFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSgvgaedDAQAESRlRDAARRAGFRNVEFQYEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 151 TAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIYQIDGQPQIEVKATAGnNKLGGDDFDDEVI---------------- 214
Cdd:cd10231 161 IAAALDYEQRLDREELVLVVDFGGGTSDFSVLRLGPNRTDRRADILATSG-VGIGGDDFDRELAlkkvmphlgrgstyvs 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 215 --------AW---------AISEFKKS-SGIDLSKDLQAMS------------------RLKEAAEKAKIELSNTQQAQI 258
Cdd:cd10231 240 gdkglpvpAWlyadlsnwhAISLLYTKkTLRLLLDLRRDAAdpekierllslvedqlghRLFRAVEQAKIALSSADEATL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 259 NLPFItmvdgqPAHLDLSLSKAKFEDLIGALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDP 338
Cdd:cd10231 320 SFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALASLFGQAR 393
|
410
....*....|....*.
gi 663513430 339 YKGINPDEAVALGAAL 354
Cdd:cd10231 394 LVEGDEFGSVAAGLAL 409
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
7-338 |
2.05e-22 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 100.32 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGESVVIANSEGARTTPSVV-AFTTE--GERLVG------VSAKRQAVTNSSRtilSVKREMGT 77
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLcAPTREavSEWLYRhldvpaYDDERQALLRRAI---RYNREEDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 78 D------------WKRKIDDAEYT----------------PQEISAF------ILQKLKADAEDYLGQEVKQAVITCPAY 123
Cdd:PRK11678 80 DvtaqsvffglaaLAQYLEDPEEVyfvkspksflgasglkPQQVALFedlvcaMMLHIKQQAEAQLQAAITQAVIGRPVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 124 FT-----DAQRKA----TKDAGRiAGLEVLRIINEPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIyqidgQPQIE 194
Cdd:PRK11678 160 FQglggeEANRQAegilERAAKR-AGFKDVEFQFEPVAAGLDFEATLTEEKRVLVVDIGGGTTDCSMLLM-----GPSWR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 195 VKATAGNNKL-------GGDDFDdevIAWAISEF--------KKSSGI-------------------------------- 227
Cdd:PRK11678 234 GRADRSASLLghsgqriGGNDLD---IALAFKQLmpllgmgsETEKGIalpslpfwnavaindvpaqsdfyslangrlln 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 228 DLSKDLQ---AMSRLKE------------AAEKAKIELSNTQQAQINLPFITmvdgqpAHLDLSLSKAKFEDLIGALIEK 292
Cdd:PRK11678 311 DLIRDARepeKVARLLKvwrqrlsyrlvrSAEEAKIALSDQAETRASLDFIS------DGLATEISQQGLEEAISQPLAR 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 663513430 293 TMGPTRQALKDSKVGKDGIdkvLLIGGSTRVPAVQEAIRKELGKDP 338
Cdd:PRK11678 385 ILELVQLALDQAQVKPDVI---YLTGGSARSPLIRAALAQQLPGIP 427
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
6-354 |
4.08e-18 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar proteins; The family includes heat shock 70 kDa proteins HSPA12A and HSPA12B. HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. Both HSPA12A and HSPA12B belong to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A and HSPA12B.
Pssm-ID: 466827 [Multi-domain] Cd Length: 372 Bit Score: 86.56 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 6 VIGIDLGTTNCCVA---TIEGGESVVIANSEGA------RTTPSVVAFTTEGErLV--GVSAKRQAVTNSSRTILSV--- 71
Cdd:cd10229 2 VVAIDFGTTYSGYAysfITDPGDIHTMYNWWGAptgvssPKTPTCLLLNPDGE-FHsfGYEAREKYSDLAEDEEHQWlyf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 72 -KREMGTDWKRKIDDA---------EYTPQEISAFILQKLKADAEDYLGQEVKQA--------VITCPAYFTDAQ----R 129
Cdd:cd10229 81 fKFKMMLLSEKELTRDtkvkavngkSMPALEVFAEALRYLKDHALKELRDRSGSSldeddirwVLTVPAIWSDAAkqfmR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 130 KATKDAGRIAG--LEVLRIINEPTAAAL---------AFGVDKSDDeTILVFDLGGGTFDVSVLEIyQIDGQPQIEVKAT 198
Cdd:cd10229 161 EAAVKAGLISEenSEQLIIALEPEAAALycqkllaegEEKELKPGD-KYLVVDCGGGTVDITVHEV-LEDGKLEELLKAS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 199 AGNnkLGGDDFDDEVIAW--------AISEFKKSSGIDLSKDLQAMSRLKEAAekakielsntqqaqinlpfitmvdgqp 270
Cdd:cd10229 239 GGP--WGSTSVDEEFEELleeifgddFMEAFKQKYPSDYLDLLQAFERKKRSF--------------------------- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 271 ahlDLSLSKAKFEDligaLIEKTMGPTRQALKD--SKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKDpyKGI----NP 344
Cdd:cd10229 290 ---KLRLSPELMKS----LFDPVVKKIIEHIKEllEKPELKGVDYIFLVGGFAESPYLQKAVKEAFSTK--VKIiippEP 360
|
410
....*....|
gi 663513430 345 DEAVALGAAL 354
Cdd:cd10229 361 GLAVVKGAVL 370
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
1-351 |
2.88e-15 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 77.25 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 1 MARNPVIGIDLGTTNCCVATIEGGesvVIANSegarttPSVVAFTTEGERLVGVSAK-RQAVTNSSRTILSVkremgtdw 79
Cdd:PRK13929 1 MFQSTEIGIDLGTANILVYSKNKG---IILNE------PSVVAVDTETKAVLAIGTEaKNMIGKTPGKIVAV-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 80 kRKIDDAEYTPQEISAFILQKLKADAEDYLGQEV-KQAVITC-PAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALaf 157
Cdd:PRK13929 64 -RPMKDGVIADYDMTTDLLKQIMKKAGKNIGMTFrKPNVVVCtPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAI-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 158 GVDKSDDETI--LVFDLGGGTFDVSVLEIYQIdgqpqievkATAGNNKLGGDDFDDEVIAWAISEFKKSSGidlskdlqa 235
Cdd:PRK13929 141 GADLPVDEPVanVVVDIGGGTTEVAIISFGGV---------VSCHSIRIGGDQLDEDIVSFVRKKYNLLIG--------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 236 msrlKEAAEKAKIELSntqQAQINLPFITM-------VDGQPAhlDLSLSKAKFEDLIGALIEKTMGPTRQALKDS--KV 306
Cdd:PRK13929 203 ----ERTAEQVKMEIG---YALIEHEPETMevrgrdlVTGLPK--TITLESKEIQGAMRESLLHILEAIRATLEDCppEL 273
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 663513430 307 GKDGIDK-VLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALG 351
Cdd:PRK13929 274 SGDIVDRgVILTGGGALLNGIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
7-353 |
3.53e-13 |
|
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and similar proteins; MreB proteins are bacterial actin homologs that may play a role in cell shape determination by positioning the cell wall synthetic machinery. MreB has also been implicated in chromosome segregation; specifically, MreB is thought to bind to and segregate the replication origin of bacterial chromosomes. The family includes three MreB isoforms, MreB (also called actin-like MreB protein or rod shape-determining protein MreB), Mbl (also called actin-like Mbl protein or rod shape-determining protein Mbl) and MreBH (also called actin-like MreBH protein or rod shape-determining protein MreBH), in cell morphogenesis of Bacillus subtilis. All isoforms can support rod-shaped cell growth normal conditions. They form membrane-associated dynamic filaments that are essential for cell shape determination. They act by regulating cell wall synthesis and cell elongation, and thus cell shape. The feedback loops between cell geometry and their localizations may maintain elongated cell shape by targeting cell wall growth to regions of negative cell wall curvature. Filaments rotate around the cell circumference in concert with the cell wall synthesis enzymes. The process is driven by the cell wall synthesis machinery and does not depend on their polymerization. They organize peptidoglycan synthesis in the lateral cell wall. MreB, Mbl and MreBH can form a complex. The MreB-like family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466824 [Multi-domain] Cd Length: 317 Bit Score: 70.96 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATieGGESVVIanSEgarttPSVVAFTTEGERLVGVsakrqavtnssrtilsvkremGTDWKRKIdda 86
Cdd:cd10225 2 IGIDLGTANTLVYV--KGKGIVL--NE-----PSVVAVDKNTGKVLAV---------------------GEEAKKML--- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 87 EYTPQEISAfiLQKLK----AD---AEDYLGQEVKQA-----------VITCPAYFTDAQRKATKDAGRIAGLEVLRIIN 148
Cdd:cd10225 49 GRTPGNIVA--IRPLRdgviADfeaTEAMLRYFIRKAhrrrgflrprvVIGVPSGITEVERRAVKEAAEHAGAREVYLIE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 149 EPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIYQIdgqpqievkATAGNNKLGGDDFDDeviawAISEF-KKSSGI 227
Cdd:cd10225 127 EPMAAAIGAGLPIEEPRGSMVVDIGGGTTEIAVISLGGI---------VTSRSVRVAGDEMDE-----AIINYvRRKYNL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 228 DLSkdlqamsrlKEAAEKAKIELSNTQQAQINLPF----ITMVDGQPAhlDLSLSKAKFEDLIGALIEKTMGPTRQALKD 303
Cdd:cd10225 193 LIG---------ERTAERIKIEIGSAYPLDEELSMevrgRDLVTGLPR--TIEITSEEVREALEEPVNAIVEAVRSTLER 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 663513430 304 SK--VGKDGIDK-VLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAA 353
Cdd:cd10225 262 TPpeLAADIVDRgIVLTGGGALLRGLDELLREETGLPVHVADDPLTCVAKGAG 314
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
1-353 |
1.22e-11 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 66.31 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 1 MARNpvIGIDLGTTNCCVATIEGGesVVIanSEgarttPSVVAFTTEGERLVGVSAK-RQAVTNSSRTILSVkREM--GT 77
Cdd:PRK13930 7 FSKD--IGIDLGTANTLVYVKGKG--IVL--NE-----PSVVAIDTKTGKVLAVGEEaKEMLGRTPGNIEAI-RPLkdGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 78 dwkrkIDDAEYTPQEISAFIlQKLKAdaedyLGQEVK-QAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALA 156
Cdd:PRK13930 75 -----IADFEATEAMLRYFI-KKARG-----RRFFRKpRIVICVPSGITEVERRAVREAAEHAGAREVYLIEEPMAAAIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 157 FGVDKSDDETILVFDLGGGTFDVSVLEIYQIdgqpqievkATAGNNKLGGDDFDDEVIAW-------AISEfkkssgidl 229
Cdd:PRK13930 144 AGLPVTEPVGNMVVDIGGGTTEVAVISLGGI---------VYSESIRVAGDEMDEAIVQYvrrkynlLIGE--------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 230 skdlqamsrlkEAAEKAKIELSNTQQAQinlPFITM-------VDGQPAHLDLS---LSKAkFEDLIGALIEKtmgpTRQ 299
Cdd:PRK13930 206 -----------RTAEEIKIEIGSAYPLD---EEESMevrgrdlVTGLPKTIEISseeVREA-LAEPLQQIVEA----VKS 266
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 663513430 300 ALKDSK--VGKDGIDK-VLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAA 353
Cdd:PRK13930 267 VLEKTPpeLAADIIDRgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARGTG 323
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
7-353 |
1.66e-11 |
|
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton];
Pssm-ID: 440695 [Multi-domain] Cd Length: 339 Bit Score: 65.87 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATieGGESVVIanSEgarttPSVVAFTTEGERLVGVsakrqavtnssrtilsvkremGTDWKRKIdda 86
Cdd:COG1077 10 IGIDLGTANTLVYV--KGKGIVL--NE-----PSVVAIDKKTGKVLAV---------------------GEEAKEML--- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 87 EYTPQEISAfiLQKLK----AD---AEDYLGQEVKQA-----------VITCPAYFTDAQRKATKDAGRIAGLEVLRIIN 148
Cdd:COG1077 57 GRTPGNIVA--IRPLKdgviADfevTEAMLKYFIKKVhgrrsffrprvVICVPSGITEVERRAVRDAAEQAGAREVYLIE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 149 EPTAAALAFGVDKSDDETILVFDLGGGTFDVSVLEIYQIdgqpqievkATAGNNKLGGDDFDDEVIAWaiseFKKSSGID 228
Cdd:COG1077 135 EPMAAAIGAGLPIEEPTGNMVVDIGGGTTEVAVISLGGI---------VVSRSIRVAGDELDEAIIQY----VRKKYNLL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 229 LSkdlqamsrlKEAAEKAKIELSNTQQAQINLPF----ITMVDGQPAHLDLS---LSKAkFEDLIGALIEKtmgpTRQAL 301
Cdd:COG1077 202 IG---------ERTAEEIKIEIGSAYPLEEELTMevrgRDLVTGLPKTITITseeIREA-LEEPLNAIVEA----IKSVL 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 663513430 302 KDSK--VGKDGIDK-VLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAA 353
Cdd:COG1077 268 EKTPpeLAADIVDRgIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVARGTG 322
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
7-352 |
3.55e-11 |
|
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: 64.74 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGG-----ESVVIANSEGARTTPSVVAFTTEGERLVGvsakrqavtNSSRTILSVkREM--GTdw 79
Cdd:TIGR00904 5 IGIDLGTANTLVYVKGRGivlnePSVVAIRTDRDAKTKSILAVGHEAKEMLG---------KTPGNIVAI-RPMkdGV-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 80 krkIDDAEYTPQEISAFILQKLKadAEDYLGQEVkqaVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGV 159
Cdd:TIGR00904 73 ---IADFEVTEKMIKYFIKQVHS--RKSFFKPRI---VICVPSGITPVERRAVKESALSAGAREVYLIEEPMAAAIGAGL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 160 DKSDDETILVFDLGGGTFDVSVLEIYQIdgqpqievkATAGNNKLGGDDFDDEVIAWAISEFKKSSGidlskdlqamsrl 239
Cdd:TIGR00904 145 PVEEPTGSMVVDIGGGTTEVAVISLGGI---------VVSRSIRVGGDEFDEAIINYIRRTYNLLIG------------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 240 KEAAEKAKIELS-----NTQQAQINLPFITMVDGQPAHLDLSlSKAKFEDL------IGALIEKTMGPTRQALkdskvGK 308
Cdd:TIGR00904 203 EQTAERIKIEIGsayplNDEPRKMEVRGRDLVTGLPRTIEIT-SVEVREALqepvnqIVEAVKRTLEKTPPEL-----AA 276
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 663513430 309 DGIDK-VLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGA 352
Cdd:TIGR00904 277 DIVERgIVLTGGGALLRNLDKLLSKETGLPVIVADDPLLCVAKGT 321
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
7-352 |
4.83e-11 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 64.50 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATieGGESVVIanSEgarttPSVVAFTTEGERL--VGVSAKrQAVTNSSRTILSVkREM--GTdwkrk 82
Cdd:pfam06723 4 IGIDLGTANTLVYV--KGKGIVL--NE-----PSVVAINTKTKKVlaVGNEAK-KMLGRTPGNIVAV-RPLkdGV----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 83 IDDAEYTPQEISAFILQKLKADAEDYLgqevkQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGVDKS 162
Cdd:pfam06723 68 IADFEVTEAMLKYFIKKVHGRRSFSKP-----RVVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 163 DDETILVFDLGGGTFDVSVLEIYQIdgqpqievkATAGNNKLGGDDFDDEVIAWAISEFKKSSGIdlskdlqamsrlkEA 242
Cdd:pfam06723 143 EPTGNMVVDIGGGTTEVAVISLGGI---------VTSKSVRVAGDEFDEAIIKYIRKKYNLLIGE-------------RT 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 243 AEKAKIELSNTQQAQINLPFIT----MVDGQPAHLDLSLSKAK--FEDLIGALIEKtmgpTRQALKDSK--VGKDGIDK- 313
Cdd:pfam06723 201 AERIKIEIGSAYPTEEEEKMEIrgrdLVTGLPKTIEISSEEVReaLKEPVSAIVEA----VKEVLEKTPpeLAADIVDRg 276
|
330 340 350
....*....|....*....|....*....|....*....
gi 663513430 314 VLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGA 352
Cdd:pfam06723 277 IVLTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGT 315
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
7-222 |
6.42e-11 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 64.15 E-value: 6.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATieGGESVVIANsegarttPSVVAFTTEGERLVGVSAK-RQAVTNSSRTILSVK--REmGTdwkrkI 83
Cdd:PRK13928 6 IGIDLGTANVLVYV--KGKGIVLNE-------PSVVAIDKNTNKVLAVGEEaRRMVGRTPGNIVAIRplRD-GV-----I 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 84 DDAEYTPQEISAFILqklKADAEDYLGQevKQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGVDKSD 163
Cdd:PRK13928 71 ADYDVTEKMLKYFIN---KACGKRFFSK--PRIMICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAGLDISQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 663513430 164 DETILVFDLGGGTFDVSVLEIYQIdgqpqievkATAGNNKLGGDDFDDEVIAWAISEFK 222
Cdd:PRK13928 146 PSGNMVVDIGGGTTDIAVLSLGGI---------VTSSSIKVAGDKFDEAIIRYIRKKYK 195
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
97-354 |
1.46e-10 |
|
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity.
Pssm-ID: 466897 [Multi-domain] Cd Length: 241 Bit Score: 61.90 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 97 ILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGVDKSddetiLVFDLGGGT 176
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG-----AVVDIGGGT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 177 FDVSVLEiyqiDGQpqieVKATAgnnklggddfdDEviawaisefkKSSGIDLSKDLqAMSRLKEAAEKAKIELSNTQQA 256
Cdd:cd24047 123 TGIAVLK----DGK----VVYTA-----------DE----------PTGGTHLSLVL-AGNYGISFEEAEIIKRDPARHK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 257 QInLPFITMVdgqpahldlslskakfedligalIEKTMGPTRQALKDSKVgkdgiDKVLLIGGSTRVPAVQEAIRKELGK 336
Cdd:cd24047 173 EL-LPVVRPV-----------------------IEKMASIVKRHIKGYKV-----KDLYLVGGTCCLPGIEEVFEKETGL 223
|
250
....*....|....*...
gi 663513430 337 DPYKGINPDEAVALGAAL 354
Cdd:cd24047 224 PVYKPSNPLLVTPLGIAL 241
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
97-354 |
1.45e-08 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 56.38 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 97 ILQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFGVDKSddetiLVFDLGGGT 176
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG-----AVVDIGGGT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 177 FDVSVLE----IYQIDgqpqievKATagnnklGGDDFdDEVIAWAIsefkkssGIDLskdlqamsrlkEAAEKAKIELSN 252
Cdd:PRK15080 147 TGISILKdgkvVYSAD-------EPT------GGTHM-SLVLAGAY-------GISF-----------EEAEQYKRDPKH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 253 TQQAqinLPFITMVdgqpahldlslskakfedligalIEKTMGPTRQALKDSKVgkdgiDKVLLIGGSTRVPAVQEAIRK 332
Cdd:PRK15080 195 HKEI---FPVVKPV-----------------------VEKMASIVARHIEGQDV-----EDIYLVGGTCCLPGFEEVFEK 243
|
250 260
....*....|....*....|..
gi 663513430 333 ELGKDPYKGINPDEAVALGAAL 354
Cdd:PRK15080 244 QTGLPVHKPQHPLFVTPLGIAL 265
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
90-366 |
5.12e-08 |
|
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes type IV pilus inner membrane component PilM, cell division protein FtsA, and ethanolamine utilization protein EutJ. PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. EutJ may protect ethanolamine ammonia-lyase (EAL, eutB-eutC) from inhibition. It may also function in assembling the bacterial microcompartment and/or in refolding EAL, suggesting it may have chaperone activity. Members in PilM-like family belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466854 [Multi-domain] Cd Length: 282 Bit Score: 54.61 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 90 PQEISAfILQKLKADAEDYLGQEVKQAVITCP----AYFTDAQRkatkdagriAGLEVLRIINEPTAAALAFGVDKSDDE 165
Cdd:cd24004 45 ISKVAE-SIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEPFAAANLLIPYDMRDL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 166 TILVFDLGGGTFDVSVLEiyqiDGqpqiEVKATaGNNKLGGDDFDDeviawAISEFKKSSgidlskdlqamsrlKEAAEK 245
Cdd:cd24004 115 NIALVDIGAGTTDIALIR----NG----GIEAY-RMVPLGGDDFTK-----AIAEGFLIS--------------FEEAEK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 246 AKIELSntqqaQINLPFITmvdgqpAHLDLSLSKAKFEDLIGALIEKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPA 325
Cdd:cd24004 167 IKRTYG-----IFLLIEAK------DQLGFTINKKEVYDIIKPVLEELASGIANAIEEYNGKFKLPDAVYLVGGGSKLPG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 663513430 326 VQEAIRKELGKDPYKGINPDEAVALGAALQAGIIVGDETVT 366
Cdd:cd24004 236 LNEALAEKLGLPVERIAPRNIGAISDITDETSKAKGPEFVT 276
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
92-335 |
5.49e-08 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A 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 HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 55.40 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 92 EISAFILQKLKADA----EDYLGQEVKQA----VITCPAYFTDAQRKATKDAGRIAGL------EVLRIINEPTAAAL-- 155
Cdd:cd11735 111 EIFAYALQFFKEQAlkelSDQAGSEFDNSdvrwVITVPAIWKQPAKQFMRQAAYKAGLaspenpEQLIIALEPEAASIyc 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 156 -AFGVDKSDdeTILVFDLGGGTFDVSVLEIYQIDGQPQIEVKATAGNNKLGGDDFDDEVIAWA------ISEFK---KSS 225
Cdd:cd11735 191 rKLRLHQMD--RYVVVDCGGGTVDLTVHQIRLPEGHLKELYKASGGPYGSLGVDYEFEKLLCKifgedfIDQFKikrPAA 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 226 GIDLskdLQAMSRLKEAAEKAKIELSNtqqaqINLPFiTMVD------GQPAHLDLSLSKAKF------------EDLIG 287
Cdd:cd11735 269 WVDL---MIAFESRKRAAAPDRTNPLN-----ITLPF-SFIDyykkfrGHSVEHALRKSNVDFvkwssqgmlrmsPDAMN 339
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 663513430 288 ALIEKTMGPTRQALKD--SKVGKDGIDKVLLIGGSTRVPAVQEAIRKELG 335
Cdd:cd11735 340 ALFKPTIDHIIQHLTDlfQKPEVSGVKFLFLVGGFAESPLLQQAVQNAFG 389
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
7-216 |
2.86e-07 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 52.78 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVatIEGGESVVIanSEgarttPSVVAFTTEGERL--VGVSAKRQAvtnsSRTILSVK--REMgtdwkrK 82
Cdd:PRK13927 8 LGIDLGTANTLV--YVKGKGIVL--NE-----PSVVAIRTDTKKVlaVGEEAKQML----GRTPGNIVaiRPM------K 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 83 ---IDDAEYTPQEISAFILQKLKadaedylGQEVKQAVITC-PAYFTDAQRKATKDAGRIAGLEVLRIINEPTAAALAFG 158
Cdd:PRK13927 69 dgvIADFDVTEKMLKYFIKKVHK-------NFRPSPRVVICvPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 663513430 159 VDKSDDETILVFDLGGGTFDVSVLEIYQIdgqpqievkATAGNNKLGGDDFDDEVIAW 216
Cdd:PRK13927 142 LPVTEPTGSMVVDIGGGTTEVAVISLGGI---------VYSKSVRVGGDKFDEAIINY 190
|
|
| ASKHA_NBD_MamK |
cd24009 |
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called ... |
7-352 |
1.27e-05 |
|
nucleotide-binding domain (NBD) of the actin-like protein MamK family; MamK, also called magnetosome cytoskeleton protein MamK, is a protein with ATPase activity which forms dynamic cytoplasmic filaments (probably with paralog MamK-like) that may organize magnetosomes into long chains running parallel to the long axis of the cell. Turnover of MamK filaments is probably promoted by MamK-like (e.g.. MamJ and/or LimJ), which provides a monomer pool. MamK forms twisted filaments in the presence of ATP or GTP. It serves to close gaps between magnetosomes in the chain. Interaction with MCP10 is involved in controlling the response to magnetic fields, possibly by controlling flagellar rotation. The MamK family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466859 [Multi-domain] Cd Length: 328 Bit Score: 47.59 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATieggesvvianSEGAR-TTPSVVAFT--------TEGERLVGvsakRQAVTNssRTILSVKR--EM 75
Cdd:cd24009 4 IGIDLGTSRSAVVT-----------SRGKRfSFRSVVGYPkdiiarklLGKEVLFG----DEALEN--RLALDLRRplED 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 76 GTDWKRKIDDAEYTpQEISAFILQKLKADAEDylgqEVKqAVITCPAYFTDAQRKATKDAGRIAGLEVLrIINEPTAAal 155
Cdd:cd24009 67 GVIKEGDDRDLEAA-RELLQHLIELALPGPDD----EIY-AVIGVPARASAENKQALLEIARELVDGVM-VVSEPFAV-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 156 AFGVDKSDDEtiLVFDLGGGTFDVSVLEIYQIDGQPQIEVKaTAGnnklggdDFDDEVIAWAISEfkKSSGIDLSKDLqa 235
Cdd:cd24009 138 AYGLDRLDNS--LIVDIGAGTTDLCRMKGTIPTEEDQITLP-KAG-------DYIDEELVDLIKE--RYPEVQLTLNM-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 236 msrLKEAAEKAKIELSNTQQAQINLPfitmVDGQPAHLDL-SLSKAKFEDLIGALIEKTMG------PTRQALKdskvgk 308
Cdd:cd24009 204 ---ARRWKEKYGFVGDASEPVKVELP----VDGKPVTYDItEELRIACESLVPDIVEGIKKliasfdPEFQEEL------ 270
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 663513430 309 dgIDKVLLIGGSTRVPAVQEAIRKELgkDPYKGIN------PDEAVALGA 352
Cdd:cd24009 271 --RNNIVLAGGGSRIRGLDTYIEKAL--KEYGGGKvtcvddPVFAGAEGA 316
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
7-354 |
2.67e-05 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 46.50 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIE-GGESVVIANSeGARTTPSVVAFTTEGERLVGVSA------------KRQAVTNSSRTILSVKR 73
Cdd:cd24049 1 LGIDIGSSSIKAVELKrSGGGLVLVAF-AIIPLPEGAIVDGEIADPEALAEalkkllkenkikGKKVVVALPGSDVIVRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 74 -EMGTDWKRKIDDA------EYTPQEISAFIL--QKLKADAEDYLGQEVkqAVITCPAYFTDAQRKATKDAGriagLEVL 144
Cdd:cd24049 80 iKLPKMPEKELEEAirfeaeQYLPFPLEEVVLdyQILGEVEEGGEKLEV--LVVAAPKEIVESYLELLKEAG----LKPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 145 RIINEPTAA--ALAFGVDKSDDETILVFDLGGGTFDVSVLEiyqiDGQPQIEVkatagNNKLGGDDFDDeviawAISEFK 222
Cdd:cd24049 154 AIDVESFALarALEYLLPDEEEETVALLDIGASSTTLVIVK----NGKLLFTR-----SIPVGGNDITE-----AIAKAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 223 kssGIDLskdlqamsrlkEAAEKAKIELSNTQQAQinlpfitmvDGQPAHLDLSLSKAkFEDLIGAlIEKTMgptrQALK 302
Cdd:cd24049 220 ---GLSF-----------EEAEELKREYGLLLEGE---------EGELKKVAEALRPV-LERLVSE-IRRSL----DYYR 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 303 dSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGK-----DPYKGINPDE-------------AVALGAAL 354
Cdd:cd24049 271 -SQNGGEPIDKIYLTGGGSLLPGLDEYLSERLGIpveilNPFSNIESKKsddeelkedaplfAVAIGLAL 339
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
98-336 |
4.44e-05 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar proteins; HSPA12B, predominantly expressed in endothelial cells, is required for angiogenesis, and may interact with known angiogenesis mediators. It may be important for host defense in microglia-mediated immune response. HSPA12B 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.
Pssm-ID: 466842 [Multi-domain] Cd Length: 361 Bit Score: 46.11 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 98 LQKLKADAEDYLGQEVKQAVITCPAYFTDAQRKATKDAGRIAGL------EVLRIINEPTAAALAfgVDKSDdeTILVFD 171
Cdd:cd11736 125 LQELKDQSPSLPEKDAVRWVLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIY--CRKLD--RYIVAD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 172 LGGGTFDVSVLEIYQIDGQPQIEVKATAGNNKLGGDDFDDEVIAWA------ISEFKK---SSGIDLSKDLQAMSRlkea 242
Cdd:cd11736 201 CGGGTVDLTVHQIEQPQGTLKELYKASGGPYGAVGVDLAFEKLLCQifgedfIATFKAkrpAAWVDLTIAFEARKR---- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 243 aeKAKIELSNTQQAQINLPFITMVdgqPAHLDLSLSKAKFEdligaliektmgptrqalkdskvgkdGIDKVLLIGGSTR 322
Cdd:cd11736 277 --TAALRMSSEAMNELFQPTISQI---IQHIDDLMKKPEVK--------------------------GIKFLFLVGGFAE 325
|
250
....*....|....
gi 663513430 323 VPAVQEAIRKELGK 336
Cdd:cd11736 326 SPMLQRAVQAAFGN 339
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
7-231 |
2.08e-04 |
|
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ParM is a plasmid-encoded bacterial homolog of actin, which polymerizes into filaments similar to F-actin, and plays a vital role in plasmid segregation. ParM filaments segregate plasmids paired at midcell into the individual daughter cells. This subfamily also contains Thermoplasma acidophilum Ta0583, an active ATPase at physiological temperatures, which has a propensity to form filaments. ParM-like proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466825 [Multi-domain] Cd Length: 263 Bit Score: 43.67 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 7 IGIDLGTTNCCVATIEGGE----SVV---IANSEGARTTPSVVAFTTEGER-LVGVSAKRQAVTNssrtilsvkREMGTD 78
Cdd:cd10227 1 IGIDIGNGNTKVVTGGGKEfkfpSAVaeaRESSLDDGLLEDDIIVEYNGKRyLVGELALREGGGG---------RSTGDD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 79 WKrKIDDAEytpqeisAFILQKLkADAEDYLGQEVKQAVITCPAYFTDAQRKATK------------DAGRIAGLEVLRI 146
Cdd:cd10227 72 KK-KSEDAL-------LLLLAAL-ALLGDDEEVDVNLVVGLPISEYKEEKKELKKkllkglheftfnGKERRITINDVKV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 147 INEPTAAALAFGVDKSD--DETILVFDLGGGTFDVSVLEiyqiDGQPQIEVKATagnnKLGGDDFDDEVIAWAISEFKKS 224
Cdd:cd10227 143 LPEGAGAYLDYLLDDDEleDGNVLVIDIGGGTTDILTFE----NGKPIEESSDT----LPGGEEALEKYADDILNELLKK 214
|
....*..
gi 663513430 225 SGIDLSK 231
Cdd:cd10227 215 LGDELDS 221
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
116-176 |
1.36e-03 |
|
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA superfamily, also known as actin-like ATPase domain superfamily, includes acetate and sugar kinases, heat-shock cognate 70 (Hsp70) and actin family proteins. They either function as conformational hydrolases (e.g. Hsp70, actin) that perform simple ATP hydrolysis, or as metabolite kinases (e.g. glycerol kinase) that catalyze the transfer of a phosphoryl group from ATP to their cognate substrates. Both activities depend on the presence of specific metal cations. ASKHA superfamily members share a common core fold that includes an actin-like ATPase domain consisting of two subdomains (denoted I _ II) with highly similar ribonuclease (RNase) H-like folds. The fold of each subdomain is characterized by a central five strand beta-sheet and flanking alpha-helices. The two subdomains form an active site cleft in which ATP binds at the bottom. Another common feature of ASKHA superfamily members is the coupling of phosphoryl-group transfer to conformational rearrangement, leading to domain closure. Substrate binding triggers protein motion.
Pssm-ID: 466786 [Multi-domain] Cd Length: 135 Bit Score: 39.37 E-value: 1.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663513430 116 AVITCPAYFTDAQRKAT-----------KDAGRIAGLEVLRIINEPTAAALAFGvDKSDDETILVFDLGGGT 176
Cdd:cd00012 16 IVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGAL-LTLGPEGLLVVDLGGGT 86
|
|
| ASKHA_NBD_ScArp9-like |
cd10208 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ... |
144-362 |
3.03e-03 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and similar proteins; Saccharomyces cerevisiae Arp9, also called actin-like protein 9, chromatin structure-remodeling complex protein ARP9, or SWI/SNF complex component ARP9, is a component of the chromatin structure remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. It is also part of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which is required for the positive and negative regulation of gene expression of many genes. Arp9 forms a stable heterodimer with Arp7 protein in both the RSC and SWI/SNF chromatin-remodeling complexes. It has been suggested that this dimer functions as a module with DNA bending proteins, to achieve correct architecture and facilitate complex-complex interactions. Fission yeast SWI/SNF and RSC complexes do not contain Arp7 and Arp8, but instead contain Arp9 and Arp42.
Pssm-ID: 466814 Cd Length: 356 Bit Score: 40.37 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 144 LRIINEPTAAALAFGVdksddETILVFDLGGGTFDVSVLeiyqIDGQPQIEVKATAGnnkLGGDDFDdeviAWAISEFKK 223
Cdd:cd10208 102 FAILEAPLAALYAAGA-----TSGIVVDIGHEKTDITPI----VDSQVVPHALVSIP---IGGQDCT----AHLAQLLKS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 224 SSGIDLSKDLQAMSRLKEAAEKAKielsntqqaQINLPFITMVDGQPAH-LDLSLSKAKF---EDLI-GALIEKTMGPTR 298
Cdd:cd10208 166 DEPELKSQAESGEEATLDLAEALK---------KSPICEVLSDGADLASgTEITVGKERFracEPLFkPSSLRVDLLIAA 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 299 QALKDSKVGKDGIDK-------VLLIGGSTRVPAVQEAIRKEL---------------------GKDP-----YKGINPD 345
Cdd:cd10208 237 IAGALVLNASDEPDKrpalwenIIIVGGGSRIRGLKEALLSELqqfhlisetsaspqqpriirlAKIPdyfpeWKKSGYE 316
|
250
....*....|....*..
gi 663513430 346 EAVALGAALQAGIIVGD 362
Cdd:cd10208 317 EAAFLGASIVAKLVFND 333
|
|
| FtsA |
COG0849 |
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning]; |
139-337 |
3.19e-03 |
|
Cell division ATPase FtsA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440610 [Multi-domain] Cd Length: 402 Bit Score: 40.12 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 139 AGLEVLRIINEPTAAALAFgvdKSDDE----TILVfDLGGGTFDVSVLEiyqiDGQpqieVKATAgnnklggddfddeVI 214
Cdd:COG0849 174 AGLEVEDLVLSPLASAEAV---LTEDEkelgVALV-DIGGGTTDIAVFK----DGA----LRHTA-------------VI 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663513430 215 AWAisefkkssGIDLSKDL-QAMSRLKEAAEKAKIELSNTQQAQINLP---FITMVDGQPAHldlSLSKAKFEDLIGALI 290
Cdd:COG0849 229 PVG--------GDHITNDIaIGLRTPLEEAERLKIKYGSALASLADEDetiEVPGIGGRPPR---EISRKELAEIIEARV 297
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 663513430 291 EKTMGPTRQALKDSKVGKDGIDKVLLIGGSTRVPAVQEAIRKELGKD 337
Cdd:COG0849 298 EEIFELVRKELKRSGYEEKLPAGVVLTGGGSQLPGLVELAEEILGLP 344
|
|
| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
309-354 |
4.80e-03 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.
Pssm-ID: 466886 [Multi-domain] Cd Length: 250 Bit Score: 39.06 E-value: 4.80e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 663513430 309 DGIDKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAAL 354
Cdd:cd24036 204 GVEDPVVLTGGVAKNPGVVKALEEKLGVEVIVPPNPQLVGALGAAL 249
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
304-356 |
5.07e-03 |
|
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport and metabolism];
Pssm-ID: 441527 [Multi-domain] Cd Length: 264 Bit Score: 39.32 E-value: 5.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 663513430 304 SKVGKDGI-DKVLLIGGSTRVPAVQEAIRKELGKDPYKGINPDEAVALGAALQA 356
Cdd:COG1924 203 NLVKRVGIgEPVVFQGGVAKNDGVVRALEKELGKEVIVPPIPQLMGALGAALLA 256
|
|
| |
