|
Name |
Accession |
Description |
Interval |
E-value |
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
1-607 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 1225.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMGT----- 73
Cdd:PRK00290 1 MGKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFtKDGERLVGQPAKRQAVTNPeNTIFSIKRLMGRrdeev 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 74 -----------------DYKVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:PRK00290 81 qkdiklvpykivkadngDAWVEIDGKKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 137 LEVERIINEPTAAALAYGLDKtDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKK 216
Cdd:PRK00290 161 LEVLRIINEPTAAALAYGLDK-KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 217 ENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQD 296
Cdd:PRK00290 240 ENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINLPFITADASGPKHLEIKLTRAKFEELTEDLVERTIEPCKQALKD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 297 AGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVVLLDVTPLSLGIETMGG 376
Cdd:PRK00290 320 AGLSVSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLAGDVKDVLLLDVTPLSLGIETLGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 377 VFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNV 456
Cdd:PRK00290 400 VMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDIDANGIVHV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 457 RAKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKAN 536
Cdd:PRK00290 480 SAKDKGTGKEQSITITASSGLSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLKELGDKVPADEKEKIE 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 580854 537 DAKDALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYeeaaKAQQAQGGANAEGKADDNVVDAEYEEVNDD 607
Cdd:PRK00290 560 AAIKELKEALKGEDKEAIKAKTEELTQASQKLGEAMY----QQAQAAQGAAGAAAKDDDVVDAEFEEVKDD 626
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
3-574 |
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: 1040.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 3 KVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMGT------- 73
Cdd:TIGR02350 1 KIIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFtKNGERLVGQPAKRQAVTNPeNTIYSIKRFMGRrfdevte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 74 --------------DYKVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:TIGR02350 81 eakrvpykvvgdggDVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 140 ERIINEPTAAALAYGLDKTDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENG 219
Cdd:TIGR02350 161 LRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEFKKEEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 220 IDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGL 299
Cdd:TIGR02350 241 IDLSKDKMALQRLKEAAEKAKIELSSVLSTEINLPFITADASGPKHLEMTLTRAKFEELTADLVERTKEPVRQALKDAGL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 300 SASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVVLLDVTPLSLGIETMGGVFT 379
Cdd:TIGR02350 321 SASDIDEVILVGGSTRIPAVQELVKDFFGKEPNKSVNPDEVVAIGAAIQGGVLKGDVKDVLLLDVTPLSLGIETLGGVMT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 380 KLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVRAK 459
Cdd:TIGR02350 401 KLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDANGILHVSAK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 460 DLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAK 539
Cdd:TIGR02350 481 DKGTGKEQSITITASSGLSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLKEAGDKLPAEEKEKIEKAV 560
|
570 580 590
....*....|....*....|....*....|....*
gi 580854 540 DALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYE 574
Cdd:TIGR02350 561 AELKEALKGEDVEEIKAKTEELQQALQKLAEAMYQ 595
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
4-574 |
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: 919.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDY------- 75
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPkNTVFSVKRLIGRKFsdpvvqr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 76 -------------------KVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:pfam00012 81 dikhlpykvvklpngdagvEVRYLGETFTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 137 LEVERIINEPTAAALAYGLDKTDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKK 216
Cdd:pfam00012 161 LNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEFKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 217 ENGIDLSKDKMALQRLKDAAEKAKKDLSGvSSTQISLPFITAGEAGpLHLELTLTRAKFEELSSHLVERTMGPVRQALQD 296
Cdd:pfam00012 241 KYGIDLSKDKRALQRLREAAEKAKIELSS-NQTNINLPFITAMADG-KDVSGTLTRAKFEELVADLFERTLEPVEKALKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 297 AGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITG--DVKDVVLLDVTPLSLGIETM 374
Cdd:pfam00012 319 AGLSKSEIDEVVLVGGSTRIPAVQELVKEFFGKEPSKGVNPDEAVAIGAAVQAGVLSGtfDVKDFLLLDVTPLSLGIETL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 375 GGVFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIV 454
Cdd:pfam00012 399 GGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGIL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 455 NVRAKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKK 534
Cdd:pfam00012 479 TVSAKDKGTGKEQEITIEASEGLSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGDKVPEAEKSK 558
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 580854 535 ANDAKDALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYE 574
Cdd:pfam00012 559 VESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMYQ 598
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
1-578 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 876.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMG------ 72
Cdd:PRK13411 1 MGKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFgKSGDRLVGQLAKRQAVTNAeNTVYSIKRFIGrrwddt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 73 ------TDYK----------VEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:PRK13411 81 eeersrVPYTcvkgrddtvnVQIRGRNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDAGTIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 137 LEVERIINEPTAAALAYGLDKTDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKK 216
Cdd:PRK13411 161 LEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLVENFQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 217 ENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQD 296
Cdd:PRK13411 241 QEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINLPFITADETGPKHLEMELTRAKFEELTKDLVEATIEPMQQALKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 297 AGLSASEIDKVILVGGSTRIPAVQEAIKKE-TGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVVLLDVTPLSLGIETMG 375
Cdd:PRK13411 321 AGLKPEDIDRVILVGGSTRIPAVQEAIQKFfGGKQPDRSVNPDEAVALGAAIQAGVLGGEVKDLLLLDVTPLSLGIETLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 376 GVFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVN 455
Cdd:PRK13411 401 EVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFEIDVNGILK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 456 VRAKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKA 535
Cdd:PRK13411 481 VSAQDQGTGREQSIRITNTGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLKENGELISEELKQRA 560
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 580854 536 NDAKDALKAAIEKNEF--EEIKAKKDELQTIVQELSMKLYEEAAK 578
Cdd:PRK13411 561 EQKVEQLEAALTDPNIslEELKQQLEEFQQALLAIGAEVYQQGGS 605
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
1-603 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 850.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMG------ 72
Cdd:CHL00094 1 MGKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYtKKGDLLVGQIAKRQAVINPeNTFYSVKRFIGrkfsei 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 73 ------TDYKVEIEG------------KDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKI 134
Cdd:CHL00094 81 seeakqVSYKVKTDSngnikiecpalnKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAGKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 135 AGLEVERIINEPTAAALAYGLDKTDeDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEF 214
Cdd:CHL00094 161 AGLEVLRIINEPTAASLAYGLDKKN-NETILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIKEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 215 KKENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQAL 294
Cdd:CHL00094 240 KKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINLPFITATQTGPKHIEKTLTRAKFEELCSDLINRCRIPVENAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 295 QDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVVLLDVTPLSLGIETM 374
Cdd:CHL00094 320 KDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLLGKKPNQSVNPDEVVAIGAAVQAGVLAGEVKDILLLDVTPLSLGVETL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 375 GGVFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIV 454
Cdd:CHL00094 400 GGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 455 NVRAKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKK 534
Cdd:CHL00094 480 SVTAKDKGTGKEQSITIQGASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLKELKDKISEEKKEK 559
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 580854 535 ANDAKDALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYEEAAKAQQAqgganaegKADDNVVDAEYEE 603
Cdd:CHL00094 560 IENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVYSSTSTTDPA--------SNDDDVIDTDFSE 620
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
1-575 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 816.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDY--- 75
Cdd:PRK13410 1 MGRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFtKDGELLVGQLARRQLVLNPqNTFYNLKRFIGRRYdel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 76 ---------------------KVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKI 134
Cdd:PRK13410 81 dpeskrvpytirrneqgnvriKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAGRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 135 AGLEVERIINEPTAAALAYGLDKTdEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEF 214
Cdd:PRK13410 161 AGLEVERILNEPTAAALAYGLDRS-SSQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAEQF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 215 KKENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQAL 294
Cdd:PRK13410 240 LEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISLPFITATEDGPKHIETRLDRKQFESLCGDLLDRLLRPVKRAL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 295 QDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVVLLDVTPLSLGIETM 374
Cdd:PRK13410 320 KDAGLSPEDIDEVVLVGGSTRMPMVQQLVRTLIPREPNQNVNPDEVVAVGAAIQAGILAGELKDLLLLDVTPLSLGLETI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 375 GGVFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIV 454
Cdd:PRK13410 400 GGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDIDANGIL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 455 NVRAKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKD--LE--GKVDEE 530
Cdd:PRK13410 480 QVSATDRTTGREQSVTIQGASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNRALTLIAQAERRLRDaaLEfgPYFAER 559
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 580854 531 QVKKANDAKDALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYEE 575
Cdd:PRK13410 560 QRRAVESAMRDVQDSLEQDDDRELDLAVADLQEALYGLNREVRAE 604
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
4-486 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 802.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDYK---VE 78
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFpKDGEVLVGEAAKRQAVTNPgRTIRSIKRLLGRSLFdeaTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 79 IEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKT 158
Cdd:COG0443 81 VGGKRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARIAGLEVLRLLNEPTAAALAYGLDKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 159 DEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENGIDLSKDKMALQRLKDAAEK 238
Cdd:COG0443 161 KEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEFGKEEGIDLRLDPAALQRLREAAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 239 AKKDLSGVSSTQISLPFitageAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLSASEIDKVILVGGSTRIPA 318
Cdd:COG0443 241 AKIELSSADEAEINLPF-----SGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAGLSPSDIDAVLLVGGSTRMPA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 319 VQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDvvlLDVTPLSLGIETMGGVFTKLIDRNTTIPTSKSQVFST 398
Cdd:COG0443 316 VRERVKELFGKEPLKGVDPDEAVALGAAIQAGVLAGDVKD---LDVTPLSLGIETLGGVFTKLIPRNTTIPTAKSQVFST 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 399 AADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVRAKDLGTGKEQNITIKsssgls 478
Cdd:COG0443 393 AADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILSVSAKDLGTGKEQSITIK------ 466
|
....*...
gi 580854 479 dEEIERMV 486
Cdd:COG0443 467 -EEIERML 473
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
4-595 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 776.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDYK----- 76
Cdd:PTZ00400 43 IVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFtEDGQRLVGIVAKRQAVTNPeNTVFATKRLIGRRYDedatk 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 77 -------------------VEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGL 137
Cdd:PTZ00400 123 keqkilpykivrasngdawIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAGKIAGL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 138 EVERIINEPTAAALAYGLDKTDeDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKE 217
Cdd:PTZ00400 203 DVLRIINEPTAAALAFGMDKND-GKTIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIAEFKKQ 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 218 NGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDA 297
Cdd:PTZ00400 282 QGIDLKKDKLALQRLREAAETAKIELSSKTQTEINLPFITADQSGPKHLQIKLSRAKLEELTHDLLKKTIEPCEKCIKDA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 298 GLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVVLLDVTPLSLGIETMGGV 377
Cdd:PTZ00400 362 GVKKDELNDVILVGGMTRMPKVSETVKKIFGKEPSKGVNPDEAVAMGAAIQAGVLKGEIKDLLLLDVTPLSLGIETLGGV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 378 FTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVR 457
Cdd:PTZ00400 442 FTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDVDANGIMNIS 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 458 AKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKAND 537
Cdd:PTZ00400 522 AVDKSTGKKQEITIQSSGGLSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLSDLKDKISDADKDELKQ 601
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 580854 538 AKDALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYEEAAKAQQAQGGANAEGKADDN 595
Cdd:PTZ00400 602 KITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYKQGNSDNQQSEQSTNSEESEEK 659
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
3-603 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 763.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 3 KVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMG-------- 72
Cdd:PLN03184 40 KVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYtKNGDRLVGQIAKRQAVVNPeNTFFSVKRFIGrkmsevde 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 73 ----TDYKVEIE------------GKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:PLN03184 120 eskqVSYRVVRDengnvkldcpaiGKQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 137 LEVERIINEPTAAALAYGLDKTDeDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKK 216
Cdd:PLN03184 200 LEVLRIINEPTAASLAYGFEKKS-NETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASNFKK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 217 ENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQD 296
Cdd:PLN03184 279 DEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISLPFITATADGPKHIDTTLTRAKFEELCSDLLDRCKTPVENALRD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 297 AGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVVLLDVTPLSLGIETMGG 376
Cdd:PLN03184 359 AKLSFKDIDEVILVGGSTRIPAVQELVKKLTGKDPNVTVNPDEVVALGAAVQAGVLAGEVSDIVLLDVTPLSLGLETLGG 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 377 VFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNV 456
Cdd:PLN03184 439 VMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSV 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 457 RAKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKAN 536
Cdd:PLN03184 519 SATDKGTGKKQDITITGASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLKELGDKVPADVKEKVE 598
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 580854 537 DAKDALKAAIEKNEFEEIKAKKDELQTIVQELSMKLYEEAAK--------AQQAQGGANAEGKADDNVVDAEYEE 603
Cdd:PLN03184 599 AKLKELKDAIASGSTQKMKDAMAALNQEVMQIGQSLYNQPGAggagpapgGEAGSSSSSSSGGDGDDVIDADFTD 673
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
4-353 |
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: 695.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDYK----- 76
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFtKDGERLVGQPAKRQAVTNPeNTIFSIKRFMGRRYKeveve 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 77 -----------------VEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:cd10234 81 rkqvpypvvsagngdawVEIGGKEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKIAGLEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 140 ERIINEPTAAALAYGLDKtDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENG 219
Cdd:cd10234 161 LRIINEPTAAALAYGLDK-KKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEFKKEEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 220 IDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGL 299
Cdd:cd10234 240 IDLSKDKMALQRLKEAAEKAKIELSSVLETEINLPFITADASGPKHLEMKLTRAKFEELTEDLVERTIEPVEQALKDAKL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 580854 300 SASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVIT 353
Cdd:cd10234 320 SPSDIDEVILVGGSTRMPAVQELVKEFFGKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
4-610 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 676.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMG---------- 72
Cdd:PTZ00186 29 VIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPqSTFYAVKRLIGrrfedehiqk 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 73 ----TDYKV-----------EIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGL 137
Cdd:PTZ00186 109 diknVPYKIvragngdawvqDGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAGTIAGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 138 EVERIINEPTAAALAYGLDKTdEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKE 217
Cdd:PTZ00186 189 NVIRVVNEPTAAALAYGMDKT-KDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILEEFRKT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 218 NGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDA 297
Cdd:PTZ00186 268 SGIDLSKERMALQRVREAAEKAKCELSSAMETEVNLPFITANADGAQHIQMHISRSKFEGITQRLIERSIAPCKQCMKDA 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 298 GLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVVLLDVTPLSLGIETMGGV 377
Cdd:PTZ00186 348 GVELKEINDVVLVGGMTRMPKVVEEVKKFFQKDPFRGVNPDEAVALGAATLGGVLRGDVKGLVLLDVTPLSLGIETLGGV 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 378 FTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVR 457
Cdd:PTZ00186 428 FTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDIDANGICHVT 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 458 AKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQvKKAND 537
Cdd:PTZ00186 508 AKDKATGKTQNITITANGGLSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQLGEWKYVSDAEK-ENVKT 586
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 580854 538 AKDALKAAIEKNEF--EEIKAKKDELQTIVQELSMKLYEEAAKAQQAQGGANAEGKADDNvvdaEYEEVNDDQNK 610
Cdd:PTZ00186 587 LVAELRKAMENPNVakDDLAAATDKLQKAVMECGRTEYQQAAAANSGSSSNSGEQQQQQQ----QQQQQNSEEKK 657
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
5-590 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 607.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMG---------TD 74
Cdd:PTZ00009 7 IGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPeNTVFDAKRLIGrkfddsvvqSD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 75 YK---------------VEI----EGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:PTZ00009 87 MKhwpfkvttggddkpmIEVtyqgEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKDAGTIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 136 GLEVERIINEPTAAALAYGLDKTDE-DQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEF 214
Cdd:PTZ00009 167 GLNVLRIINEPTAAAIAYGLDKKGDgEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEFCVQDF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 215 KKEN-GIDLSKDKMALQRLKDAAEKAKKDLSgvSSTQISLPFITAGEAgpLHLELTLTRAKFEELSSHLVERTMGPVRQA 293
Cdd:PTZ00009 247 KRKNrGKDLSSNQRALRRLRTQCERAKRTLS--SSTQATIEIDSLFEG--IDYNVTISRARFEELCGDYFRNTLQPVEKV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 294 LQDAGLSASEIDKVILVGGSTRIPAVQEAIKK-ETGKEAHKGVNPDEVVALGAAIQGGVITGD----VKDVVLLDVTPLS 368
Cdd:PTZ00009 323 LKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDfFNGKEPCKSINPDEAVAYGAAVQAAILTGEqssqVQDLLLLDVTPLS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 369 LGIETMGGVFTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDI 448
Cdd:PTZ00009 403 LGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFDI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 449 DKNGIVNVRAKDLGTGKEQNITIKSSSG-LSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKD--LEG 525
Cdd:PTZ00009 483 DANGILNVSAEDKSTGKSNKITITNDKGrLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDekVKG 562
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 580854 526 KVDEEQVKKANDAKDALKAAIEKN---EFEEIKAKKDELQTIVQELSMKLYeeaakaqQAQGGANAEG 590
Cdd:PTZ00009 563 KLSDSDKATIEKAIDEALEWLEKNqlaEKEEFEHKQKEVESVCNPIMTKMY-------QAAGGGMPGG 623
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
5-567 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 579.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMG---TDYKVEIE 80
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPkNTISSVKRFMGrslADIQQRYP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 81 GKDY-------------------TPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVER 141
Cdd:PRK05183 102 HLPYqfvasengmplirtaqglkSPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLAGLNVLR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 142 IINEPTAAALAYGLDKTDEDqTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLvsefKKENGID 221
Cdd:PRK05183 182 LLNEPTAAAIAYGLDSGQEG-VIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWI----LEQAGLS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 222 LSKDKMALQRLKDAAEKAKKDLSGVSSTQISLpfitAGEAGplhlelTLTRAKFEELSSHLVERTMGPVRQALQDAGLSA 301
Cdd:PRK05183 257 PRLDPEDQRLLLDAARAAKEALSDADSVEVSV----ALWQG------EITREQFNALIAPLVKRTLLACRRALRDAGVEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 302 SEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDV--KDVVLLDVTPLSLGIETMGGVFT 379
Cdd:PRK05183 327 DEVKEVVMVGGSTRVPLVREAVGEFFGRTPLTSIDPDKVVAIGAAIQADILAGNKpdSDMLLLDVIPLSLGLETMGGLVE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 380 KLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVRAK 459
Cdd:PRK05183 407 KIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSVTAM 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 460 DLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAK 539
Cdd:PRK05183 487 EKSTGVEASIQVKPSYGLTDDEIARMLKDSMSHAEEDMQARALAEQKVEAERVLEALQAALAADGDLLSAAERAAIDAAM 566
|
570 580
....*....|....*....|....*...
gi 580854 540 DALKAAIEKNEFEEIKAKKDELQTIVQE 567
Cdd:PRK05183 567 AALREVAQGDDADAIEAAIKALDKATQE 594
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
4-564 |
0e+00 |
|
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act together as chaperones. HscA resembles DnaK but belongs in a separate clade. The apparent function is to aid assembly of iron-sulfur cluster proteins. Homologs from Buchnera and Wolbachia are clearly in the same clade but are highly derived and score lower than some examples of DnaK. [Protein fate, Protein folding and stabilization]
Pssm-ID: 273915 [Multi-domain] Cd Length: 599 Bit Score: 568.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMG--------- 72
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYlKDGGVEVGKEALAAAAEDPkNTISSVKRLMGrsiediktf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 73 --TDYKVEiEGKDY-----------TPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEV 139
Cdd:TIGR01991 81 siLPYRFV-DGPGEmvrlrtvqgtvTPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKDAARLAGLNV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 140 ERIINEPTAAALAYGLDKTDEDqTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVsefkKENG 219
Cdd:TIGR01991 160 LRLLNEPTAAAVAYGLDKASEG-IYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALAKWIL----KQLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 220 IDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLpfitagEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGL 299
Cdd:TIGR01991 235 ISADLNPEDQRLLLQAARAAKEALTDAESVEVDF------TLDGKDFKGKLTRDEFEALIQPLVQKTLSICRRALRDAGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 300 SASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDV--KDVVLLDVTPLSLGIETMGGV 377
Cdd:TIGR01991 309 SVEEIKGVVLVGGSTRMPLVRRAVAELFGQEPLTDIDPDQVVALGAAIQADLLAGNRigNDLLLLDVTPLSLGIETMGGL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 378 FTKLIDRNTTIPTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVR 457
Cdd:TIGR01991 389 VEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDADGLLTVS 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 458 AKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKAND 537
Cdd:TIGR01991 469 AQEQSTGVEQSIQVKPSYGLSDEEIERMLKDSFKHAEEDMYARALAEQKVEAERILEALQAALAADGDLLSEDERAAIDA 548
|
570 580
....*....|....*....|....*..
gi 580854 538 AKDALKAAIEKNEFEEIKAKKDELQTI 564
Cdd:TIGR01991 549 AMEALQKALQGDDADAIKAAIEALEEA 575
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
2-352 |
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: 558.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 2 SKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDYK--- 76
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFtADGERLVGMPAKRQAVTNPeNTLYATKRLIGRRFDdpe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 77 ---------------------VEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd11733 81 vqkdikmvpykivkasngdawVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAGQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 136 GLEVERIINEPTAAALAYGLDKTDeDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFK 215
Cdd:cd11733 161 GLNVLRIINEPTAAALAYGLDKKD-DKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVAEFK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 216 KENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQ 295
Cdd:cd11733 240 KEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINLPFITADASGPKHLNMKLTRAKFESLVGDLIKRTVEPCKKCLK 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 580854 296 DAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVI 352
Cdd:cd11733 320 DAGVSKSDIGEVLLVGGMTRMPKVQETVQEIFGKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
4-354 |
3.42e-173 |
|
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: 496.58 E-value: 3.42e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKR------------ 69
Cdd:cd11734 3 VIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFtKDGERLVGVPAKRQAVVNPeNTLFATKRligrkfddaevq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 70 ------------HMGTDYKVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGL 137
Cdd:cd11734 83 rdikevpykivkHSNGDAWVEARGQKYSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIAGL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 138 EVERIINEPTAAALAYGLDKTdEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKE 217
Cdd:cd11734 163 NVLRVINEPTAAALAYGLDKS-GDKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIVSEFKKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 218 NGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDA 297
Cdd:cd11734 242 SGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINLPFITADASGPKHINMKLTRAQFESLVKPLVDRTVEPCKKALKDA 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 580854 298 GLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITG 354
Cdd:cd11734 322 GVKTSEINEVILVGGMSRMPKVQETVKSIFGREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
4-352 |
2.10e-168 |
|
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: 484.41 E-value: 2.10e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDY------- 75
Cdd:cd10241 3 VIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPeNTVFDVKRLIGRKFddkevqk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 76 ------------------KVEIEG--KDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd10241 83 dikllpfkivnkngkpyiQVEVKGekKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGTIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 136 GLEVERIINEPTAAALAYGLDKTDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFK 215
Cdd:cd10241 163 GLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKLFK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 216 KENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEagplHLELTLTRAKFEELSSHLVERTMGPVRQALQ 295
Cdd:cd10241 243 KKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGE----DFSETLTRAKFEELNMDLFRKTLKPVQKVLE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 580854 296 DAGLSASEIDKVILVGGSTRIPAVQEAIKKE-TGKEAHKGVNPDEVVALGAAIQGGVI 352
Cdd:cd10241 319 DAGLKKSDIDEIVLVGGSTRIPKVQQLLKDFfNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
4-352 |
2.64e-168 |
|
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: 483.94 E-value: 2.64e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDY------- 75
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPeNTIFDVKRLIGRKFddpsvqs 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 76 -------KVEIEGKD--------------YTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd24028 81 dikhwpfKVVEDEDGkpkievtykgeektFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 135 AGLEVERIINEPTAAALAYGLDKTDE-DQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSE 213
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDKKSSgERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 214 FKKENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEagplHLELTLTRAKFEELSSHLVERTMGPVRQA 293
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGI----DFETTITRAKFEELCEDLFKKCLEPVEKV 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 294 LQDAGLSASEIDKVILVGGSTRIPAVQEAIKKE-TGKEAHKGVNPDEVVALGAAIQGGVI 352
Cdd:cd24028 317 LKDAKLSKDDIDEVVLVGGSTRIPKIQELLSEFfGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
5-352 |
3.09e-154 |
|
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: 447.02 E-value: 3.09e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIA-NAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDYK--VEI 79
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFdKDGEVLVGEEAKNQALLDPeNTIYSVKRLMGRDTKdkEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 80 EGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTD 159
Cdd:cd24029 81 GGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAELAGLNVLRLINEPTAAALAYGLDKEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 160 EDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENGI-DLSKDKMALQRLKDAAEK 238
Cdd:cd24029 161 KDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKIGIETGIlDDKEDERARARLREAAEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 239 AKKDLSGVSSTQISLPFITAGEagplHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLSASEIDKVILVGGSTRIPA 318
Cdd:cd24029 241 AKIELSSSDSTDILILDDGKGG----ELEIEITREEFEELIAPLIERTIDLLEKALKDAKLSPEDIDRVLLVGGSSRIPL 316
|
330 340 350
....*....|....*....|....*....|....
gi 580854 319 VQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVI 352
Cdd:cd24029 317 VREMLEEYFGREPISSVDPDEAVAKGAAIYAASL 350
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
1-354 |
7.99e-153 |
|
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: 444.35 E-value: 7.99e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSKVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDY--- 75
Cdd:cd10236 1 HRLAVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYgEDGKITVGEKAKENAITDPeNTISSVKRLMGRSLadv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 76 -------------------KVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd10236 81 keelpllpyrlvgdenelpRFRTGAGNLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 137 LEVERIINEPTAAALAYGLDKTDEdQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHlvseFKK 216
Cdd:cd10236 161 LNVLRLLNEPTAAALAYGLDQKKE-GTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFDHLLADW----ILK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 217 ENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLpfitagEAGPLHLELTLTRAKFEELSSHLVERTMGPVRQALQD 296
Cdd:cd10236 236 QIGIDARLDPAVQQALLQAARRAKEALSDADSASIEV------EVEGKDWEREITREEFEELIQPLVKRTLEPCRRALKD 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 580854 297 AGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITG 354
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; ... |
5-352 |
3.42e-145 |
|
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: 425.12 E-value: 3.42e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMG---------TD 74
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPtNTVFDAKRLIGrkfddpvvqSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 75 YK----------------VEIEG--KDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd10233 82 MKhwpfkvvsggdkpkiqVEYKGetKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 137 LEVERIINEPTAAALAYGLDK-TDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFK 215
Cdd:cd10233 162 LNVLRIINEPTAAAIAYGLDKkGKGERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 216 KENGIDLSKDKMALQRLKDAAEKAKKDLSgvSSTQISLpfitagEAGPLH----LELTLTRAKFEELSSHLVERTMGPVR 291
Cdd:cd10233 242 RKHKKDISGNPRALRRLRTACERAKRTLS--SSTQASI------EIDSLFegidFYTSITRARFEELCADLFRSTLEPVE 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 580854 292 QALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKE-TGKEAHKGVNPDEVVALGAAIQGGVI 352
Cdd:cd10233 314 KVLRDAKLDKSQIHEIVLVGGSTRIPKVQKLLQDFfNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
5-354 |
5.09e-140 |
|
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: 410.48 E-value: 5.09e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF-KNGERQVGEVAKRQSITNPN-TIMSIKRHMGTDYKVEIEGK 82
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVdEDGSILVGRAAKERLVTHPDrTAASFKRFMGTDKQYRLGNH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 83 DYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTDEDQ 162
Cdd:cd10235 81 TFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELAGLKVERLINEPTAAALAYGLHKREDET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 163 TILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENGIDLSKDKMALQRlkdAAEKAKKD 242
Cdd:cd10235 161 RFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFTHALADYFLKKHRLDFTSLSPSELAALRK---RAEQAKRQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 243 LSGVSSTQISLPFitAGEAgplhLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLSASEIDKVILVGGSTRIPAVQEA 322
Cdd:cd10235 238 LSSQDSAEIRLTY--RGEE----LEIELTREEFEELCAPLLERLRQPIERALRDAGLKPSDIDAVILVGGATRMPLVRQL 311
|
330 340 350
....*....|....*....|....*....|..
gi 580854 323 IKKETGKEAHKGVNPDEVVALGAAIQGGVITG 354
Cdd:cd10235 312 IARLFGRLPLSSLDPDEAVALGAAIQAALKAR 343
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
4-558 |
1.11e-126 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 385.75 E-value: 1.11e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGE-----VAKR------QSITNPNTIMS-IKRHM 71
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGNnkglrSIKRlfgktlKEILNTPALFSlVKDYL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 72 ---GTDYKVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTA 148
Cdd:PRK01433 101 dvnSSELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLAAKIAGFEVLRLIAEPTA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 149 AALAYGLDKtDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFkkengiDLSKDKMA 228
Cdd:PRK01433 181 AAYAYGLNK-NQKGCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLCNKF------DLPNSIDT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 229 LQrlkdAAEKAKKDLSGVSSTQISlpfitageagplhlELTLTRAKFEELSSHLVERTMGPVRQALQDAGlsASEIDKVI 308
Cdd:PRK01433 254 LQ----LAKKAKETLTYKDSFNND--------------NISINKQTLEQLILPLVERTINIAQECLEQAG--NPNIDGVI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 309 LVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITGDVKDVVLLDVTPLSLGIETMGGVFTKLIDRNTTI 388
Cdd:PRK01433 314 LVGGATRIPLIKDELYKAFKVDILSDIDPDKAVVWGAALQAENLIAPHTNSLLIDVVPLSLGMELYGGIVEKIIMRNTPI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 389 PTSKSQVFSTAADNQTAVDIHVLQGERPMSADNKTLGRFQLTDIPPAPRGVPQIEVSFDIDKNGIVNVRAKDLGTGKEQN 468
Cdd:PRK01433 394 PISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADGILSVSAYEKISNTSHA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 469 ITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAKDALKAAIE- 547
Cdd:PRK01433 474 IEVKPNHGIDKTEIDIMLENAYKNAKIDYTTRLLQEAVIEAEALIFNIERAIAELTTLLSESEISIINSLLDNIKEAVHa 553
|
570
....*....|....*..
gi 580854 548 ------KNEFEEIKAKK 558
Cdd:PRK01433 554 rdiiliNNSIKEFKSKI 570
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
5-352 |
2.58e-125 |
|
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: 374.32 E-value: 2.58e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGgEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDY-------- 75
Cdd:cd24093 2 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPrNTVFDAKRLIGRRFddesvqkd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 76 ---------------KVEI----EGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd24093 81 mktwpfkvidvngnpVIEVqylgETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 137 LEVERIINEPTAAALAYGLD--KTDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEF 214
Cdd:cd24093 161 LNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 215 KKENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEagplHLELTLTRAKFEELSSHLVERTMGPVRQAL 294
Cdd:cd24093 241 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGE----DFESSITRARFEDLNAALFKSTLEPVEQVL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 580854 295 QDAGLSASEIDKVILVGGSTRIPAVQEAIKK-ETGKEAHKGVNPDEVVALGAAIQGGVI 352
Cdd:cd24093 317 KDAKISKSQIDEVVLVGGSTRIPKVQKLLSDfFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
3-354 |
2.27e-112 |
|
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: 342.40 E-value: 2.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 3 KVIGIDLGTTNSCVAVLEG--GEPKVIANAEGNRTTPSVVAFK-NGERQVGEVAKRQSITNP-NTIMSIKRHMGTDY--- 75
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHAvtGEVEVIPDDDGHKSIPSVVAFTpDGGVLVGYDALAQAEHNPsNTIYDAKRFIGKTFtke 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 76 KVEIEGKDY-------------------------TPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKD 130
Cdd:cd10237 103 ELEEEAKRYpfkvvndnigsaffevplngstlvvSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 131 AGKIAGLEVERIINEPTAAALAYGLDKTDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHL 210
Cdd:cd10237 183 AANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 211 VSEFKKENGIDLsKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHL-ELTLTRAKFEELSSHLVERTMGP 289
Cdd:cd10237 263 IDRIAKKFGKTL-TDKEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLPSAFKVKfKEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 580854 290 VRQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVITG 354
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFFGKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
4-352 |
3.31e-101 |
|
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: 312.25 E-value: 3.31e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMGTD-------- 74
Cdd:cd10238 2 AFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNAsNTVVRVKQLLGRSfddpavqe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 75 -----------------YKVEIEGKD--YTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd10238 82 lkkeskckiiekdgkpgYEIELEEKKklVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 136 GLEVERIINEPTAAALAYGLDKTD--EDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSE 213
Cdd:cd10238 162 GFNVLRVISEPSAAALAYGIGQDDptENSNVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLASE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 214 FKKENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGeagpLHLELTLTRAKFEELSSHLVERTMGPVRQA 293
Cdd:cd10238 242 FKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDG----MDFQCNVSRARFESLCSSLFQQCLEPIQEV 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 294 LQDAGLSASEIDKVILVGGSTRIPAVQEAIKKE-TGKEAHKGVNPDEVVALGAAIQGGVI 352
Cdd:cd10238 318 LNSAGLTKEDIDKVILCGGSSRIPKLQQLIKDLfPSAEVLSSIPPDEVIAIGAAKQAGLL 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 ... |
5-348 |
2.55e-95 |
|
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: 297.16 E-value: 2.55e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDYK------- 76
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYkNTIRNFKRLIGLKFDdpevqke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 77 --------VEIEGKD-------------YTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd11732 81 ikllpfklVELEDGKvgievsyngeevvFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 136 GLEVERIINEPTAAALAYGLDK------TDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDH 209
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKsdllesEEKPRIVAFVDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 210 LVSEFKKENGIDLSKDKMALQRLKDAAEKAKKDLSgvsstqislpfitAGEAGPLHLE---------LTLTRAKFEELSS 280
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLS-------------ANGEAPLNVEclmedidfsGQIKREEFEELIQ 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 580854 281 HLVERTMGPVRQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQ 348
Cdd:cd11732 308 PLLARLEAPIKKALAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVFGKDLSTTLNADEAVARGCALQ 375
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
4-349 |
6.10e-94 |
|
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: 292.48 E-value: 6.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIA-NAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMGtdykveieg 81
Cdd:cd10230 2 VLGIDLGSEFIKVALVKPGVPFEIVlNEESKRKTPSAVAFRNGERLFGDDALALATRFPeNTFSYLKDLLG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 82 kdYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKT--- 158
Cdd:cd10230 73 --YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAEIAGLNVLSLINDNTAAALNYGIDRRfen 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 159 DEDQTILVYDLGGGTFDVSILE--------LGDGV----FEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENGI--DLSK 224
Cdd:cd10230 151 NEPQNVLFYDMGASSTSATVVEfssvkekdKGKNKtvpqVEVLGVGWDRTLGGLEFDLRLADHLADEFNEKHKKdkDVRT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 225 DKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGeagpLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLSASEI 304
Cdd:cd10230 231 NPRAMAKLLKEANRVKEVLSANTEAPASIESLYDD----IDFRTKITREEFEELCADLFERVVAPIEEALEKAGLTLDDI 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 580854 305 DKVILVGGSTRIPAVQEAIKKETGKEA-HKGVNPDEVVALGAAIQG 349
Cdd:cd10230 307 DSVELIGGGTRVPKVQEALKEALGRKElGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
1-349 |
5.08e-92 |
|
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: 288.83 E-value: 5.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSkVIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMG------- 72
Cdd:cd24095 1 MS-VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPkNTISQLKRLIGrkfddpe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 73 --TD-----YKVeIEGKD---------------YTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKD 130
Cdd:cd24095 80 vqRDlklfpFKV-TEGPDgeiginvnylgeqkvFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 131 AGKIAGLEVERIINEPTAAALAYGLDKTDEDQT----ILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVI 206
Cdd:cd24095 159 AAQIAGLNCLRLMNETTATALAYGIYKTDLPETdptnVVFVDVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 207 IDHLVSEFKKENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITagEAGPLHLEltLTRAKFEELSSHLVERT 286
Cdd:cd24095 239 FDHFAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLM--EDKDVKGM--ITREEFEELAAPLLERL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 580854 287 MGPVRQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQG 349
Cdd:cd24095 315 LEPLEKALADSGLTVDQIHSVEVVGSGSRIPAILKILTKFFGKEPSRTMNASECVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
5-348 |
1.23e-85 |
|
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: 271.84 E-value: 1.23e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMG----------- 72
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLkNTVSGFKRLLGrkfddpfvqke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 73 ---------------TDYKVEIEGKD--YTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIA 135
Cdd:cd10228 81 lkhlpykvvklpngsVGIKVQYLGEEhvFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 136 GLEVERIINEPTAAALAYGLDKTD---EDQT---ILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDH 209
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDlpaEEEKprnVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 210 LVSEFKKENGIDLSKDKMALQRLKDAAEKAKKDLSGvSSTQIslpfitageagPLHLEL---------TLTRAKFEELSS 280
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSA-NATEL-----------PLNIECfmddkdvsgKMKRAEFEELCA 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 580854 281 HLVERTMGPVRQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQ 348
Cdd:cd10228 309 PLFARVEVPLRSALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVFGKEPSTTLNQDEAVARGCALQ 376
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
4-352 |
1.06e-84 |
|
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: 268.46 E-value: 1.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVL-EGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMGTdykveieg 81
Cdd:cd10232 2 VIGISFGNSNSSIAIInKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPkNTVANFRDLLGT-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 82 KDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDK---- 157
Cdd:cd10232 74 TTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAAAAGLEVLQLIPEPAAAALAYDLRAetsg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 158 -TDEDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHLVSEFKKENGIDLSKDKMALQRLKDAA 236
Cdd:cd10232 154 dTIKDKTVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVGHFAKEFKKKTKTDPRKNARSLAKLRNAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 237 EKAKKDLSGVSSTQISLPFITAGeagpLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLSASEIDKVILVGGSTRI 316
Cdd:cd10232 234 EITKRALSQGTSAPCSVESLADG----IDFHSSINRTRYELLASKVFQQFADLVTDAIEKAGLDPLDIDEVLLAGGASRT 309
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 580854 317 PAVQEAIK----KETGKEAHKGVNPDEVVALGAAIQGGVI 352
Cdd:cd10232 310 PKLASNFEylfpESTIIRAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
5-348 |
4.26e-82 |
|
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: 263.08 E-value: 4.26e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITN-PNTIMSIKRHMGTDYK------- 76
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNfKNTVGSLKRLIGRTFSdpevaee 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 77 --------VEIEGK------------DYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAG 136
Cdd:cd24094 81 ekyftaklVDANGEvgaevnylgekhVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 137 LEVERIINEPTAAALAYGLDKTD-----EDQTILVY-DLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIIDHL 210
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKTDlpepeEKPRIVAFvDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 211 VSEFKKENGIDLSKDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITageaGPLHLELTLTRAKFEELSSHLVERTMGPV 290
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLM----NDIDVSSMLKREEFEELIAPLLERVTAPL 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 580854 291 RQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQ 348
Cdd:cd24094 317 EKALAQAGLTKDEIDFVELVGGTTRVPALKESISAFFGKPLSTTLNQDEAVARGAAFA 374
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
4-348 |
6.99e-71 |
|
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: 233.68 E-value: 6.99e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMG---TDYKVEI 79
Cdd:cd11737 2 VVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAkNTVQGFKRFHGrafSDPFVQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 80 -------------------------EGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd11737 82 ekpslayelvqlptgttgikvmymeEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 135 AGLEVERIINEPTAAALAYGLDKTD-----EDQTILVY-DLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIID 208
Cdd:cd11737 162 AGLNCLRLMNETTAVALAYGIYKQDlpapeEKPRNVVFvDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLVN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 209 HLVSEFKKENGIDLSKDKMALQRLKDAAEKAKKDLSGVSStqiSLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMG 288
Cdd:cd11737 242 HFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANAS---DLPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 289 PVRQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQ 348
Cdd:cd11737 319 PLRSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFFGKEVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
4-348 |
6.46e-69 |
|
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: 228.21 E-value: 6.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNP-NTIMSIKRHMGTDYKVEIEGK 82
Cdd:cd11739 2 VVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNAnNTVSNFKRFHGRAFNDPFVQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 83 D----------------------------YTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd11739 82 EkenlsydlvplknggvgvkvmyldeehhFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 135 AGLEVERIINEPTAAALAYGLDKTD-----EDQTILVY-DLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIID 208
Cdd:cd11739 162 VGLNCLRLMNDMTAVALNYGIYKQDlpapdEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 209 HLVSEFKKENGIDLSKDKMALQRLKDAAEKAKKDLsgvSSTQISLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMG 288
Cdd:cd11739 242 HFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLM---SSNSTDLPLNIECFMNDKDVSGKMNRSQFEELCADLLQRIEV 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 289 PVRQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQ 348
Cdd:cd11739 319 PLYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFFGKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
4-353 |
3.66e-66 |
|
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: 221.33 E-value: 3.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITN-PNTIMSIKRHMG---------- 72
Cdd:cd11738 2 VVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNaKNTIHGFKKFHGrafddpfvqa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 73 ----------------TDYKVEI--EGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKI 134
Cdd:cd11738 82 ekiklpyelqkmpngsTGVKVRYldEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 135 AGLEVERIINEPTAAALAYGLDKTD------EDQTILVYDLGGGTFDVSILELGDGVFEVRSTAGDNRLGGDDFDQVIID 208
Cdd:cd11738 162 AGLNCLRLMNETTAVALAYGIYKQDlpaleeKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 209 HLVSEFKKENGIDLSKDKMALQRLKDAAEKAKKDLSGVSStqiSLPFITAGEAGPLHLELTLTRAKFEELSSHLVERTMG 288
Cdd:cd11738 242 YFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANAS---DLPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEP 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 580854 289 PVRQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAIQGGVIT 353
Cdd:cd11738 319 PLKAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFFGKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
5-347 |
5.35e-59 |
|
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: 200.41 E-value: 5.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIanaegnrttpsvvafkngerqvgevakrqsitnpntimsiKRHMGTDYKVEIEGKDY 84
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPP----------------------------------------LVVLQLPWPGGDGGSSK 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 85 TPQ--EVSAIILQHLKSYAESYLGETVS-------KAVITVPAYFNDAERQATKDAGKIAGLEVE----RIINEPTAAAL 151
Cdd:cd10170 41 VPSvlEVVADFLRALLEHAKAELGDRIWelekapiEVVITVPAGWSDAAREALREAARAAGFGSDsdnvRLVSEPEAAAL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 152 AYGLDKTD-----EDQTILVYDLGGGTFDVSILELGDGVFEVR---STAGDNRLGGDDFDQVIIDHLVSEFKKENGIDLS 223
Cdd:cd10170 121 YALEDKGDllplkPGDVVLVCDAGGGTVDLSLYEVTSGSPLLLeevAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLGR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 224 KDKMALQRLKDAAEKAKKDLSGVSSTQISLPFITAGEAGPLHLElTLTRAKFEELSSHLVERTMGPVRQALQDAGLSAS- 302
Cdd:cd10170 201 SDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLPELGLE-KGTLLLTEEEIRDLFDPVIDKILELIEEQLEAKSg 279
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 580854 303 -EIDKVILVGGSTRIPAVQEAIKKETG----KEAHKGVNPDEVVALGAAI 347
Cdd:cd10170 280 tPPDAVVLVGGFSRSPYLRERLRERFGsagiIIVLRSDDPDTAVARGAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
5-346 |
2.31e-53 |
|
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: 187.48 E-value: 2.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAF------KNGERQVGEVAKRQSITNPNT---IMSIKRHMGTD- 74
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFprreeeGAESIYFGNDAIDAYLNDPEEgrlIKSVKSFLGSSl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 75 -YKVEIEGKDYTPQEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQAT-------KDAGKIAGLEVERIINEP 146
Cdd:cd10231 81 fDETTIFGRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDDaqaesrlRDAARRAGFRNVEFQYEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 147 TAAALAYGLDkTDEDQTILVYDLGGGTFDVSILELG----DGVFEVRSTAGDnRLGGDDFDQVIIDHLVS-EF------- 214
Cdd:cd10231 161 IAAALDYEQR-LDREELVLVVDFGGGTSDFSVLRLGpnrtDRRADILATSGV-GIGGDDFDRELALKKVMpHLgrgstyv 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 215 ---------------------------------------------KKENGIDLSKDKMAlQRLKDAAEKAKKDLSGVSST 249
Cdd:cd10231 239 sgdkglpvpawlyadlsnwhaisllytkktlrllldlrrdaadpeKIERLLSLVEDQLG-HRLFRAVEQAKIALSSADEA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 250 QISLPFItageagPLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGK 329
Cdd:cd10231 318 TLSFDFI------EISIKVTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFLTGGSSQSPAVRQALASLFGQ 391
|
410
....*....|....*..
gi 580854 330 EAHKGVNPDEVVALGAA 346
Cdd:cd10231 392 ARLVEGDEFGSVAAGLA 408
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
5-347 |
3.81e-27 |
|
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: 112.18 E-value: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGepkVIANaEgnrttPSVVAFKNGERQ---VGEVAKRQSITNPNTIMSIkRHM--G--TDYkv 77
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLN-E-----PSVVAVDKNTGKvlaVGEEAKKMLGRTPGNIVAI-RPLrdGviADF-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 78 eiegkdytpqEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGL-EVeRIINEPTAAALAYGLD 156
Cdd:cd10225 70 ----------EATEAMLRYFIRKAHRRRGFLRPRVVIGVPSGITEVERRAVKEAAEHAGArEV-YLIEEPMAAAIGAGLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 157 kTDEDQTILVYDLGGGTFDVSILELGdGVFEVRSTagdnRLGGDDFDQVIIDHLvsefKKENGIDLSkdkmalqrlKDAA 236
Cdd:cd10225 139 -IEEPRGSMVVDIGGGTTEIAVISLG-GIVTSRSV----RVAGDEMDEAIINYV----RRKYNLLIG---------ERTA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 237 EKAKKDLSGVSSTQISLPFITAG---EAGpLHLELTLTRAKFEELSSHLVERTMGPVRQALQDAG--LSASEIDK-VILV 310
Cdd:cd10225 200 ERIKIEIGSAYPLDEELSMEVRGrdlVTG-LPRTIEITSEEVREALEEPVNAIVEAVRSTLERTPpeLAADIVDRgIVLT 278
|
330 340 350
....*....|....*....|....*....|....*..
gi 580854 311 GGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAI 347
Cdd:cd10225 279 GGGALLRGLDELLREETGLPVHVADDPLTCVAKGAGK 315
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
1-347 |
2.25e-24 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 104.44 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSKVIGIDLGTTNSCVAVLEGG----EPKVIANaegNRTTPSVVAfkngerqVGEVAKRQSITNPNTIMSIK--RHmGTd 74
Cdd:PRK13930 7 FSKDIGIDLGTANTLVYVKGKGivlnEPSVVAI---DTKTGKVLA-------VGEEAKEMLGRTPGNIEAIRplKD-GV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 75 ykveIEgkDYtpqEVSAIILQHL--KSYAESYLGetVSKAVITVPAYFNDAERQATKDAGKIAGL-EVErIINEPTAAAL 151
Cdd:PRK13930 75 ----IA--DF---EATEAMLRYFikKARGRRFFR--KPRIVICVPSGITEVERRAVREAAEHAGArEVY-LIEEPMAAAI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 152 AYGLDKTDEDQTILVyDLGGGTFDVSILELGdGVFEVRSTagdnRLGGDDFDQVIIDHLvsefKKENGIDLSkdkmalqr 231
Cdd:PRK13930 143 GAGLPVTEPVGNMVV-DIGGGTTEVAVISLG-GIVYSESI----RVAGDEMDEAIVQYV----RRKYNLLIG-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 232 lKDAAEKAKKDLsgvsstqislpfitaGEAGPLHLELTLT---------RAKFEELSSHLVERTMGP--------VRQAL 294
Cdd:PRK13930 205 -ERTAEEIKIEI---------------GSAYPLDEEESMEvrgrdlvtgLPKTIEISSEEVREALAEplqqiveaVKSVL 268
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 580854 295 QD--AGLSASEIDK-VILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAI 347
Cdd:PRK13930 269 EKtpPELAADIIDRgIVLTGGGALLRGLDKLLSEETGLPVHIAEDPLTCVARGTGK 324
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
5-323 |
3.89e-23 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 102.63 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVAKRQSITNPNTIMS--IKRHMGTDYKVEIEGK 82
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREAVSEWLYRHLDVPAYDDERQalLRRAIRYNREEDIDVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 83 DYT--------------PQE---------------------------VSAIILqHLKSYAESYLGETVSKAVITVPAYFN 121
Cdd:PRK11678 83 AQSvffglaalaqyledPEEvyfvkspksflgasglkpqqvalfedlVCAMML-HIKQQAEAQLQAAITQAVIGRPVNFQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 122 -----DAERQAT---KDAGKIAGLEVERIINEPTAAalayGLD---KTDEDQTILVYDLGGGTFDVSILELGDGVFEVRS 190
Cdd:PRK11678 162 glggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA----GLDfeaTLTEEKRVLVVDIGGGTTDCSMLLMGPSWRGRAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 191 TAGD------NRLGGDDFD-----QVIIDHLVSEFKKENGIDL----------------------SKDKMALQRL-KDA- 235
Cdd:PRK11678 238 RSASllghsgQRIGGNDLDialafKQLMPLLGMGSETEKGIALpslpfwnavaindvpaqsdfysLANGRLLNDLiRDAr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 236 -----------------------AEKAKKDLSGVSSTQISLPFITAGeagplhLELTLTRAKFEELSSHLVERTMGPVRQ 292
Cdd:PRK11678 318 epekvarllkvwrqrlsyrlvrsAEEAKIALSDQAETRASLDFISDG------LATEISQQGLEEAISQPLARILELVQL 391
|
410 420 430
....*....|....*....|....*....|.
gi 580854 293 ALQDAGLSAseiDKVILVGGSTRIPAVQEAI 323
Cdd:PRK11678 392 ALDQAQVKP---DVIYLTGGSARSPLIRAAL 419
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
1-347 |
1.69e-22 |
|
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: 99.00 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSKVIGIDLGTTNSCVAVLEGGepkVIANaEgnrttPSVVAFKNGERQ---VGEVAKRqsitnpntimsikrhMgtdykv 77
Cdd:COG1077 6 FSKDIGIDLGTANTLVYVKGKG---IVLN-E-----PSVVAIDKKTGKvlaVGEEAKE---------------M------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 78 eiEGKdyTPQEVSAI-ILQH--LKSY--AESYLGETVSKA-----------VITVPAYFNDAERQATKDAGKIAGL-EVe 140
Cdd:COG1077 56 --LGR--TPGNIVAIrPLKDgvIADFevTEAMLKYFIKKVhgrrsffrprvVICVPSGITEVERRAVRDAAEQAGArEV- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 141 RIINEPTAAALAYGLDKTDEDQTILVyDLGGGTFDVSILELGDGVFEvRSTagdnRLGGDDFDQVIIDHLvsefKKENGI 220
Cdd:COG1077 131 YLIEEPMAAAIGAGLPIEEPTGNMVV-DIGGGTTEVAVISLGGIVVS-RSI----RVAGDELDEAIIQYV----RKKYNL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 221 DLSkDKMAlqrlkdaaEKAKkdlsgvsstqislpfITAGEAGPLHLELTLT---------RAKFEELSSHLVERTMGP-- 289
Cdd:COG1077 201 LIG-ERTA--------EEIK---------------IEIGSAYPLEEELTMEvrgrdlvtgLPKTITITSEEIREALEEpl 256
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 580854 290 ------VRQALQD--AGLSASEIDK-VILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAI 347
Cdd:COG1077 257 naiveaIKSVLEKtpPELAADIVDRgIVLTGGGALLRGLDKLLSEETGLPVHVAEDPLTCVARGTGK 323
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
2-347 |
4.13e-21 |
|
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: 94.54 E-value: 4.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 2 SKVIGIDLGTTNSCVAVLEGGepkVIANaegnrtTPSVVAFKNGERQ---VGEVAKRQSITNPNTIMSIkRHMG----TD 74
Cdd:pfam06723 1 SKDIGIDLGTANTLVYVKGKG---IVLN------EPSVVAINTKTKKvlaVGNEAKKMLGRTPGNIVAV-RPLKdgviAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 75 YkveiegkdytpqEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYG 154
Cdd:pfam06723 71 F------------EVTEAMLKYFIKKVHGRRSFSKPRVVICVPSGITEVERRAVKEAAKNAGAREVFLIEEPMAAAIGAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 155 LDkTDEDQTILVYDLGGGTFDVSILELGDGVfevrsTAGDNRLGGDDFDQVIIDHLVSEFKKENGIdlskdkmalqrlkD 234
Cdd:pfam06723 139 LP-VEEPTGNMVVDIGGGTTEVAVISLGGIV-----TSKSVRVAGDEFDEAIIKYIRKKYNLLIGE-------------R 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 235 AAEKAKKDLSGVSSTQISLPFITAG---EAGpLHLELTLTRAKFEELSSHLVERTMGPVRQALQD--AGLSASEIDK-VI 308
Cdd:pfam06723 200 TAERIKIEIGSAYPTEEEEKMEIRGrdlVTG-LPKTIEISSEEVREALKEPVSAIVEAVKEVLEKtpPELAADIVDRgIV 278
|
330 340 350
....*....|....*....|....*....|....*....
gi 580854 309 LVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAI 347
Cdd:pfam06723 279 LTGGGALLRGLDKLLSDETGLPVHIAEDPLTCVALGTGK 317
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
4-354 |
1.35e-20 |
|
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: 93.88 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAVL---EGGEPKVIANAEG------NRTTPSVVAFKNGERQV--GEVAKRQSITNPNT--------- 63
Cdd:cd10229 2 VVAIDFGTTYSGYAYSfitDPGDIHTMYNWWGaptgvsSPKTPTCLLLNPDGEFHsfGYEAREKYSDLAEDeehqwlyff 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 64 --IMSIKRHMGTDYKVEIE---GKDYTPQEVSAIILQHLKSYA------ESYLGETVSKA--VITVPAYFNDAERQATKD 130
Cdd:cd10229 82 kfKMMLLSEKELTRDTKVKavnGKSMPALEVFAEALRYLKDHAlkelrdRSGSSLDEDDIrwVLTVPAIWSDAAKQFMRE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 131 AGKIAGLEVE------RIINEPTAAALAYG-------LDKTDEDQTILVYDLGGGTFDVSILEL--GDGVFEV-RSTAGD 194
Cdd:cd10229 162 AAVKAGLISEenseqlIIALEPEAAALYCQkllaegeEKELKPGDKYLVVDCGGGTVDITVHEVleDGKLEELlKASGGP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 195 nrLGGDDFDQ--------VIIDHLVSEFKKENGIDlskdkmaLQRLKDAAEKAKKDLSgvsstqislpfitageagplhl 266
Cdd:cd10229 242 --WGSTSVDEefeelleeIFGDDFMEAFKQKYPSD-------YLDLLQAFERKKRSFK---------------------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 267 eLTLTRAKFEELSSHLVERTMGPVRQALQDAGLsaSEIDKVILVGGSTRIPAVQEAIKKETGKEaHKGVNPDEVVAlgAA 346
Cdd:cd10229 291 -LRLSPELMKSLFDPVVKKIIEHIKELLEKPEL--KGVDYIFLVGGFAESPYLQKAVKEAFSTK-VKIIIPPEPGL--AV 364
|
....*...
gi 580854 347 IQGGVITG 354
Cdd:cd10229 365 VKGAVLFG 372
|
|
| mreB |
TIGR00904 |
cell shape determining protein, MreB/Mrl family; MreB (mecillinam resistance) in E. coli (also ... |
5-345 |
1.43e-18 |
|
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: 87.08 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGG----EPKVIA-NAEGNRTTPSVVAfkngerqVGEVAKRQSITNPNTIMSI---KRHMGTDYk 76
Cdd:TIGR00904 5 IGIDLGTANTLVYVKGRGivlnEPSVVAiRTDRDAKTKSILA-------VGHEAKEMLGKTPGNIVAIrpmKDGVIADF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 77 veiegkdytpqEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLd 156
Cdd:TIGR00904 77 -----------EVTEKMIKYFIKQVHSRKSFFKPRIVICVPSGITPVERRAVKESALSAGAREVYLIEEPMAAAIGAGL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 157 KTDEDQTILVYDLGGGTFDVSILELGdGVFEVRSTagdnRLGGDDFDQVIIDHLVSEF------------KKENG----I 220
Cdd:TIGR00904 145 PVEEPTGSMVVDIGGGTTEVAVISLG-GIVVSRSI----RVGGDEFDEAIINYIRRTYnlligeqtaeriKIEIGsaypL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 221 DLSKDKMALqRLKDAAEKAKKDLSgVSSTQIS----LPFITAGEAgplhLELTLTRAKfEELSSHLVERTMgpvrqalqd 296
Cdd:TIGR00904 220 NDEPRKMEV-RGRDLVTGLPRTIE-ITSVEVRealqEPVNQIVEA----VKRTLEKTP-PELAADIVERGI--------- 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 580854 297 aglsaseidkvILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGA 345
Cdd:TIGR00904 284 -----------VLTGGGALLRNLDKLLSKETGLPVIVADDPLLCVAKGT 321
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
5-344 |
1.73e-16 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 81.11 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGG----EPKVIANaegNRTTPSVVAfkngerqVGEVAKRQSITNPNTIMSI---KRHMGTDYkv 77
Cdd:PRK13929 7 IGIDLGTANILVYSKNKGiilnEPSVVAV---DTETKAVLA-------IGTEAKNMIGKTPGKIVAVrpmKDGVIADY-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 78 eiegkdytpqEVSAIILQHLKSYAESYLGETVSK--AVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGL 155
Cdd:PRK13929 75 ----------DMTTDLLKQIMKKAGKNIGMTFRKpnVVVCTPSGSTAVERRAISDAVKNCGAKNVHLIEEPVAAAIGADL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 156 dKTDEDQTILVYDLGGGTFDVSILELGdGVFEVRSTagdnRLGGDDFDQVIIDH-------LVSEFKKENgIDLSKDKMA 228
Cdd:PRK13929 145 -PVDEPVANVVVDIGGGTTEVAIISFG-GVVSCHSI----RIGGDQLDEDIVSFvrkkynlLIGERTAEQ-VKMEIGYAL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 229 LQRLKDAAEKAKKDL-SGVSSTqislpfitageagpLHLELTLTRAKFEELSSHLVErtmgPVRQALQDA--GLSASEID 305
Cdd:PRK13929 218 IEHEPETMEVRGRDLvTGLPKT--------------ITLESKEIQGAMRESLLHILE----AIRATLEDCppELSGDIVD 279
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 580854 306 K-VILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALG 344
Cdd:PRK13929 280 RgVILTGGGALLNGIKEWLSEEIVVPVHVAANPLESVAIG 319
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
1-215 |
4.66e-15 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 76.86 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSKVIGIDLGTTNSCVAVLEGG----EPKVIANaegNRTTPSVVAfkngerqVGEVAKRQSITNPNTIMSIkRHMGtdyk 76
Cdd:PRK13928 2 FGRDIGIDLGTANVLVYVKGKGivlnEPSVVAI---DKNTNKVLA-------VGEEARRMVGRTPGNIVAI-RPLR---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 77 veiEG--KDYtpqEVSAIILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYG 154
Cdd:PRK13928 67 ---DGviADY---DVTEKMLKYFINKACGKRFFSKPRIMICIPTGITSVEKRAVREAAEQAGAKKVYLIEEPLAAAIGAG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 580854 155 LDKTDEDQTILVyDLGGGTFDVSILELGDGVfevrsTAGDNRLGGDDFDQVIIDHLVSEFK 215
Cdd:PRK13928 141 LDISQPSGNMVV-DIGGGTTDIAVLSLGGIV-----TSSSIKVAGDKFDEAIIRYIRKKYK 195
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
1-214 |
1.25e-12 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 69.35 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 1 MSKVIGIDLGTTNSCVAVLEGGepkVIANAegnrttPSVVAFKNGERQ---VGEVAKRQSITNPNTIMSIkRHM--G--T 73
Cdd:PRK13927 4 FSNDLGIDLGTANTLVYVKGKG---IVLNE------PSVVAIRTDTKKvlaVGEEAKQMLGRTPGNIVAI-RPMkdGviA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 74 DYkveiegkdytpqEVSAIILQHLksyaesylgetVSKA----------VITVPAYFNDAERQATKDAGKIAGL-EVeRI 142
Cdd:PRK13927 74 DF------------DVTEKMLKYF-----------IKKVhknfrpsprvVICVPSGITEVERRAVRESALGAGArEV-YL 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 580854 143 INEPTAAALAYGLDkTDEDQTILVYDLGGGTFDVSILELGDGVfevrsTAGDNRLGGDDFDQVIIDHLVSEF 214
Cdd:PRK13927 130 IEEPMAAAIGAGLP-VTEPTGSMVVDIGGGTTEVAVISLGGIV-----YSKSVRVGGDKFDEAIINYVRRNY 195
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
93-347 |
6.75e-11 |
|
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: 62.67 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 93 ILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTdedqtiLVYDLGGG 172
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG------AVVDIGGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 173 TFDVSILELGDGVFevrstAGDNRLGGDDFDQVIIDHLvsefkkenGIDLskdkmalqrlkDAAEKAKKDLSGvsstqis 252
Cdd:cd24047 122 TTGIAVLKDGKVVY-----TADEPTGGTHLSLVLAGNY--------GISF-----------EEAEIIKRDPAR------- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 253 lpfitageagplHLEL-TLTRAKFEELSShLVERtmgpvrqalqdaGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEA 331
Cdd:cd24047 171 ------------HKELlPVVRPVIEKMAS-IVKR------------HIKGYKVKDLYLVGGTCCLPGIEEVFEKETGLPV 225
|
250
....*....|....*.
gi 580854 332 HKGVNPDEVVALGAAI 347
Cdd:cd24047 226 YKPSNPLLVTPLGIAL 241
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
457-611 |
3.24e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 457 RAKDLGTGKEQNITIKSSSGLSDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKAN 536
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 580854 537 DAKdalKAAIEKNEFEEIKAKKDELQTivQELSMKLYEEAAKAQQAQGGANAEGKADDNVVDAEYEEVNDDQNKK 611
Cdd:PTZ00121 1435 EAK---KKAEEAKKADEAKKKAEEAKK--AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
93-346 |
4.46e-09 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 57.53 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 93 ILQHLKSYAESYLGETVSKAVITVPAYFNDAERQATKDAGKIAGLEVERIINEPTAAALAYGLDKTdedqtiLVYDLGGG 172
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG------AVVDIGGG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 173 TFDVSILELGDGVFEVrstagDNRLGGDDFDQVIIDHLvsefkkenGIDLskdkmalqrlkDAAEKAKKDlsgvsstqis 252
Cdd:PRK15080 146 TTGISILKDGKVVYSA-----DEPTGGTHMSLVLAGAY--------GISF-----------EEAEQYKRD---------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 253 lpfitageagplhleltltRAKFEELSSHL---VERTMGPVRQALQDaglsaSEIDKVILVGGSTRIPAVQEAIKKETGK 329
Cdd:PRK15080 192 -------------------PKHHKEIFPVVkpvVEKMASIVARHIEG-----QDVEDIYLVGGTCCLPGFEEVFEKQTGL 247
|
250
....*....|....*..
gi 580854 330 EAHKGVNPDEVVALGAA 346
Cdd:PRK15080 248 PVHKPQHPLFVTPLGIA 264
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
86-325 |
1.98e-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: 55.76 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 86 PQEVSAIILQhLKSYAESYLGETVSKAVITVPAYFNDAERQATKdagkiAGLEVERIINEPTAAALAYGLDKTdEDQTIL 165
Cdd:cd24004 45 ISKVAESIKE-LLKELEEKLGSKLKDVVIAIAKVVESLLNVLEK-----AGLEPVGLTLEPFAAANLLIPYDM-RDLNIA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 166 VYDLGGGTFDVSILELGdGVFEVRSTAgdnrLGGDDFDQVIIDHLVSEFKKengidlskdkmalqrlkdaAEKAKKDLS- 244
Cdd:cd24004 118 LVDIGAGTTDIALIRNG-GIEAYRMVP----LGGDDFTKAIAEGFLISFEE-------------------AEKIKRTYGi 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 245 --GVSSTQISLPFITAGEAgplhleLTLTRAKFEELSSHLVErtmgpvrqALQDAGLSASEIDKVILVGGSTRIPAVQEA 322
Cdd:cd24004 174 flLIEAKDQLGFTINKKEV------YDIIKPVLEELASGIAN--------AIEEYNGKFKLPDAVYLVGGGSKLPGLNEA 239
|
...
gi 580854 323 IKK 325
Cdd:cd24004 240 LAE 242
|
|
| ASKHA_NBD_ScArp9-like |
cd10208 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae actin-related protein 9 (Arp9) and ... |
142-326 |
5.66e-07 |
|
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: 51.92 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 142 IINEPTAAALAYGLdktdedQTILVYDLGGGTFDVSIlelgdgVFE---VRSTAGDNRLGGDDFDQviidHLVSEFKKEN 218
Cdd:cd10208 104 ILEAPLAALYAAGA------TSGIVVDIGHEKTDITP------IVDsqvVPHALVSIPIGGQDCTA----HLAQLLKSDE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 219 GIDLSKDKMALQRLKDAAEKAKKDlsgvsstqiSLPFITAGEAGPLH---LELTLTRAKF-EELSSHLVERTMGPVRQAL 294
Cdd:cd10208 168 PELKSQAESGEEATLDLAEALKKS---------PICEVLSDGADLASgteITVGKERFRAcEPLFKPSSLRVDLLIAAIA 238
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 580854 295 QDAGLSAS-EIDK-------VILVGGSTRIPAVQEAIKKE 326
Cdd:cd10208 239 GALVLNASdEPDKrpalwenIIIVGGGSRIRGLKEALLSE 278
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
480-611 |
6.00e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 480 EEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAKDALKAAIEKNEFEEIKAKKD 559
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 580854 560 ELQTIVQ------ELSMKLYEEAAKAQQAQGGANAEGKADDNVVDAEYEEVNDDQNKK 611
Cdd:PTZ00121 1382 AAKKKAEekkkadEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK 1439
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
483-594 |
1.74e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 483 ERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAK---DALKAAIEKNEFEEIKAKKD 559
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaeEAKKKAEEAKKADEAKKKAE 1480
|
90 100 110
....*....|....*....|....*....|....*
gi 580854 560 ELQTiVQELSMKLYEEAAKAQQAQGGANAEGKADD 594
Cdd:PTZ00121 1481 EAKK-ADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
480-611 |
1.98e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 480 EEIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDlEGKVDEEQVKKANDAK-----------DALKAAIEK 548
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-AAKKKAEEKKKADEAKkkaeedkkkadELKKAAAAK 1417
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 580854 549 NEFEEIKAKKDELQTiVQELSMKLyEEAAKAQQAQGGANAEGKADDNVVDAEYEEVNDDQNKK 611
Cdd:PTZ00121 1418 KKADEAKKKAEEKKK-ADEAKKKA-EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
|
| ASKHA_NBD_ParM-like |
cd10227 |
nucleotide-binding domain (NBD) of the plasmid segregation protein ParM-like domain family; ... |
5-226 |
5.09e-06 |
|
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: 48.29 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGE---PKVIANAEGNRTT------PSVVAFKNGERQVGEVAKRQSITNpntimsikRHMGTDY 75
Cdd:cd10227 1 IGIDIGNGNTKVVTGGGKEfkfPSAVAEARESSLDdglledDIIVEYNGKRYLVGELALREGGGG--------RSTGDDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 76 KveieGKDYTPqevsAIILQHLKSYAESYLGETvsKAVITVPA--YFNDAERQATKDAGKIAGLEVE-----------RI 142
Cdd:cd10227 73 K----KSEDAL----LLLLAALALLGDDEEVDV--NLVVGLPIseYKEEKKELKKKLLKGLHEFTFNgkerritindvKV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 143 INEPTAAALAYGLDKT-DEDQTILVYDLGGGTFDVSILElgDGVFEVRSTAGDNrlGGDDFDQVIIDHLVSEFKKENGID 221
Cdd:cd10227 143 LPEGAGAYLDYLLDDDeLEDGNVLVIDIGGGTTDILTFE--NGKPIEESSDTLP--GGEEALEKYADDILNELLKKLGDE 218
|
....*
gi 580854 222 LSKDK 226
Cdd:cd10227 219 LDSAD 223
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
483-602 |
1.01e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 483 ERMVKEAEENADADAKKKEEiEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAKDALKAAIEKNEFEEIKaKKDELQ 562
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK-KAEEDE 1687
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 580854 563 TIVQELSMKLYEEAAKAQQAQGGANAEGKADDNVVDAEYE 602
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
478-611 |
2.63e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 478 SDEEIERMVKEAEENADADAKKKEEIEVRNEADQLVfQTEKTLKDLEGKVDEEQVKKANDAKDAL-----KAAIEKNEFE 552
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM-KAEEAKKAEEAKIKAEELKKAEEEKKKVeqlkkKEAEEKKKAE 1650
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 580854 553 EIKAKKDELQTIVQELSMKLYEEAAKAQQAQGGANAEGKADDNVVDAEYEEVNDDQNKK 611
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
465-611 |
4.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 465 KEQNITIKSSSGLSDEEIERMV-----KEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLE-GKVDEEQVKKANDA 538
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVeqlkkKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeAKKAEEDEKKAAEA 1693
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 580854 539 KDalKAAIEKNEFEEIKAKKDELQTIVQELSMKLYEEAAKAQQAQGGANAEGKaddnvvDAEYEEVNDDQNKK 611
Cdd:PTZ00121 1694 LK--KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK------KAEEAKKDEEEKKK 1758
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
480-580 |
7.30e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 480 EEIERMVKEAEENADADAK------KKEEIEVRNEADQLVFQTEKTLKDLEGKVD--EEQVKKANDAKDALKAAIEKNE- 550
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKealleaKEEIHKLRNEFEKELRERRNELQKLEKRLLqkEENLDRKLELLEKREEELEKKEk 117
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 580854 551 -----FEEIKAKKDELQTIVQELSMKLYE------EAAKAQ 580
Cdd:PRK12704 118 eleqkQQELEKKEEELEELIEEQLQELERisgltaEEAKEI 158
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
480-610 |
9.43e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 480 EEIERMVKEAEENADAD-AKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAK--DALKAAIEKNEFEEIKA 556
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEeERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDEAKKAEEKKKADEAKK 1309
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 580854 557 KKDELQTiVQELSMKLYEEAAKAQQAQGGANaEGKADDNVVDAEYEEVNDDQNK 610
Cdd:PTZ00121 1310 KAEEAKK-ADEAKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEA 1361
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
483-611 |
9.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 483 ERMVKEAEENADADAKKKEEIEVRnEADQLVFQTEKTLKDLEGKVDEEQVKKANDAK----DALKAAIEKNEFEEIKAKK 558
Cdd:PTZ00121 1434 DEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKkkaeEAKKKADEAKKAAEAKKKA 1512
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 580854 559 DELQTIVQElsmKLYEEAAKAQQAQGGANA----EGKADDNVVDAE----YEEVNDDQNKK 611
Cdd:PTZ00121 1513 DEAKKAEEA---KKADEAKKAEEAKKADEAkkaeEKKKADELKKAEelkkAEEKKKAEEAK 1570
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
4-329 |
1.01e-04 |
|
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: 44.96 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 4 VIGIDLGTTNSCVAV--------------LEGGEPKVianaeGNRTTP-SVVAFKNGERQVGEVAKRQSI--TNPNTI-- 64
Cdd:cd11736 2 VVAIDFGTTSSGYAFsfssdpeaihmmrkWEGGDPGV-----ANQKTPtSLLLTPDGAFHSFGYTARDYYhdLDPEEArd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 65 ------MSIKRHMGTDYKVEIE-----GKDYTPQEVSAIIL--------QHLKSYAESYLGETVSKAVITVPAYFNDAER 125
Cdd:cd11736 77 wlyfekFKMKIHSTSDLTMETEleavnGKKVQALEVFAHALrffkehalQELKDQSPSLPEKDAVRWVLTVPAIWKQPAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 126 QATKDAGKIAGL------EVERIINEPTAAAL-AYGLDKtdedqtILVYDLGGGTFDVSI--LELGDGVFEVRSTAgdnr 196
Cdd:cd11736 157 QFMREAAYLAGLvspenpEQLLIALEPEAASIyCRKLDR------YIVADCGGGTVDLTVhqIEQPQGTLKELYKA---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 197 lGGDDFDQViidhlvsefkkenGIDLSKDKMALQRLKD---AAEKAKKDLSGVSSTqislpfiTAGEAGPLHLELTLTra 273
Cdd:cd11736 227 -SGGPYGAV-------------GVDLAFEKLLCQIFGEdfiATFKAKRPAAWVDLT-------IAFEARKRTAALRMS-- 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 580854 274 kfEELSSHLVERTMGPVRQALQDAgLSASEIDKV---ILVGGSTRIPAVQEAIKKETGK 329
Cdd:cd11736 284 --SEAMNELFQPTISQIIQHIDDL-MKKPEVKGIkflFLVGGFAESPMLQRAVQAAFGN 339
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
135-335 |
2.03e-04 |
|
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an essential cell division protein that assists in the assembly of the Z ring. It may serve as the principal membrane anchor for the Z ring. It is also required for the recruitment to the septal ring of the downstream cell division proteins FtsK, FtsQ, FtsL, FtsI and FtsN. FtsA binds ATP. FtsA interacts with FtsZ. This interaction plays an essential role in cell division.
Pssm-ID: 466898 [Multi-domain] Cd Length: 372 Bit Score: 44.06 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 135 AGLEVERIINEPTAAALAYgLDKTDEDQTILVYDLGGGTFDVSILElgDGVFevRSTAGdNRLGGDDFDQviidhlvsef 214
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEKELGVALIDIGGGTTDIAVFK--NGSL--RYTAV-IPVGGNHITN---------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 215 kkengiDLSkdkMALQRLKDAAEKAKKDLSGVSSTQIS--LPFITAGEAGPLHLELTLT------RAKFEELSSHlvert 286
Cdd:cd24048 236 ------DIA---IGLNTPFEEAERLKIKYGSALSEEADedEIIEIPGVGGREPREVSRRelaeiiEARVEEILEL----- 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 580854 287 mgpVRQALQDAGLSASEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGV 335
Cdd:cd24048 302 ---VKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGMPVRIGR 347
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
486-611 |
2.49e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 486 VKEAEENADADAKKKEEIEVRNEADQ-LVFQTEKTLKDLEGKVDEEQVKKANDAKDALKAAIEKNEFEEIKA----KKDE 560
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKnMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkKAEE 1630
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 580854 561 LQTIVQELSMKLYEEAAKAQQAQggaNAEgkaDDNVVDAEYEEVNDDQNKK 611
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELK---KAE---EENKIKAAEEAKKAEEDKK 1675
|
|
| ASKHA_NBD_PilM |
cd24049 |
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar ... |
5-342 |
2.50e-04 |
|
nucleotide-binding domain (NBD) of type IV pilus inner membrane component PilM and similar proteins; PilM is an inner membrane component of the type IV (T4S) secretion system that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility. PilN/PilO heterodimers form the foundation of the inner-membrane PilM/PilN/PilO/PilP complex which plays an essential role in the assembly of a functional T4 pilus. In turn, PilM associates with PilN and facilitates PilM functionally relevant structural changes that differentially impacts PilM binding to PilB, PilT, and PilC.
Pssm-ID: 466899 [Multi-domain] Cd Length: 339 Bit Score: 43.42 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 5 IGIDLGTTNSCVAVLEGGEPKVIANAEGNRTTPSVVAFKNGERQVGEVA-------KRQSITNPNTIMSIKRHMGTDYKV 77
Cdd:cd24049 1 LGIDIGSSSIKAVELKRSGGGLVLVAFAIIPLPEGAIVDGEIADPEALAealkkllKENKIKGKKVVVALPGSDVIVRTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 78 EIEGKDytPQEVSAIIlqhlKSYAESYLGETVSKAVI---TVPAYFNDAERQ-----ATK--------DAGKIAGLEVER 141
Cdd:cd24049 81 KLPKMP--EKELEEAI----RFEAEQYLPFPLEEVVLdyqILGEVEEGGEKLevlvvAAPkeivesylELLKEAGLKPVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 142 IINEPTAAALAYGLDK-TDEDQTILVYDLGGGTFDVSILElGDGVFEVRSTAgdnrLGGDDFDQVIIDHLvsefkkenGI 220
Cdd:cd24049 155 IDVESFALARALEYLLpDEEEETVALLDIGASSTTLVIVK-NGKLLFTRSIP----VGGNDITEAIAKAL--------GL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 221 DLskdkmalqrlkDAAEKAKKDLSgvsstqislpFITAGEAGPLHLELTLTRAKFEELSSHlVERTMGPVRQALQDagls 300
Cdd:cd24049 222 SF-----------EEAEELKREYG----------LLLEGEEGELKKVAEALRPVLERLVSE-IRRSLDYYRSQNGG---- 275
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 580854 301 aSEIDKVILVGGSTRIPAVQEAIKKETGKEAHKGvNPDEVVA 342
Cdd:cd24049 276 -EPIDKIYLTGGGSLLPGLDEYLSERLGIPVEIL-NPFSNIE 315
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
234-359 |
2.55e-04 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 44.05 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 234 DAAEKAKKDLSGVsstqISLPFITaGEAGP------------LHLELT---LTRAKFE----ELSSHLvertmgpvrQAL 294
Cdd:COG1070 324 ALAAEVPPGADGL----LFLPYLS-GERTPhwdpnargaffgLTLSHTrahLARAVLEgvafALRDGL---------EAL 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 580854 295 QDAGLsasEIDKVILVGGSTRIPAVQEAIKKETGKEAHKgVNPDEVVALGAAIQGGVITGDVKDV 359
Cdd:COG1070 390 EEAGV---KIDRIRATGGGARSPLWRQILADVLGRPVEV-PEAEEGGALGAALLAAVGLGLYDDL 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
465-583 |
4.40e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 465 KEQNITIKSSSGLSDEEIErmvKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLKDLEGKVDEEQvKKANDAKDA--L 542
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAK---KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA-KKADEAKKAeeA 1533
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 580854 543 KAAIEKNEFEEIKaKKDELQTiVQELsmKLYEEAAKAQQAQ 583
Cdd:PTZ00121 1534 KKADEAKKAEEKK-KADELKK-AEEL--KKAEEKKKAEEAK 1570
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
481-592 |
5.78e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.53 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 481 EIERMVKEAEENADADAKKKEEIEVRNEADQLVFQTEKTLK-----DLEGKVDEEQVKKANDAKDALKAAIEKNEFEEIK 555
Cdd:TIGR02794 93 ELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKakaeaEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
|
90 100 110
....*....|....*....|....*....|....*....
gi 580854 556 AKKDELQTIVQELSMKLYEE--AAKAQQAQGGANAEGKA 592
Cdd:TIGR02794 173 KKAEAEAKAKAEAEAKAKAEeaKAKAEAAKAKAAAEAAA 211
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
486-611 |
1.14e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 486 VKEAEENADADAKKKEEiEVRnEADQLVFQTEktlkdlEGKVDEEQVKKANDAK----DALKAAIEKNEFEEI-----KA 556
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAE-EKK-KADEAKKKAE------EAKKADEAKKKAEEAKkkadAAKKKAEEAKKAAEAakaeaEA 1354
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 580854 557 KKDELQTIVQEL---SMKLYEEAAKAQQAQGGANAEGKADDNVVDAEYEEVNDDQNKK 611
Cdd:PTZ00121 1355 AADEAEAAEEKAeaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK 1412
|
|
| ASKHA_ATPase-like |
cd00012 |
ATPase-like domain of the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily; The ASKHA ... |
109-173 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 580854 109 VSKAVITVPAYFNDAERQAT-----------KDAGKIAGLEVERIINEPTAAALAYGLDKTDEdqTILVYDLGGGT 173
Cdd:cd00012 13 AVPIVITVAAGDRDANRVATiteailllqtnAATFALFTGPPVRIVNEAVAAAIGALLTLGPE--GLLVVDLGGGT 86
|
|
| ASKHA_NBD_ParM_R1-like |
cd24022 |
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and ... |
159-338 |
1.56e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli plasmid segregation protein ParM and similar proteins from ParM domain family; Type II plasmid partition systems utilize ParM NTPases in coordination with a centromere-binding protein called ParR to mediate accurate DNA segregation, a process critical for plasmid retention. The family corresponds to a group of uncharacterized proteins similar to Escherichia coli ParM, also called ParA locus 36 kDa protein, or protein StbA. It is a plasmid-encoded protein involved in the control of plasmid partition and required for accurate segregation of low-copy-number plasmid R1.
Pssm-ID: 466872 [Multi-domain] Cd Length: 324 Bit Score: 41.10 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 159 DEDQTILVYDLGGGTFDVSILElgdgvfevrstagdnrlggddfDQVIIDHLVSEFKKENGIDLSKdkmalqRLKDAAeK 238
Cdd:cd24022 171 EEEGPVAVIDIGGTTTDIAVVS----------------------GGLSIDHARSGTIELGVLDVRD------ALKDAL-K 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 239 AKKDLSGVSSTQISLpFITAGEAGplhleltLTRAKFEELSSHL---VERTMGPVRQALQDAGLSASEIDKVILVGGSTR 315
Cdd:cd24022 222 KRFGLSSISDAELDR-ALRTGKFR-------LNGGKEVDVSDLVneaIAEVAERILNEIKRRLGDASDLDRVIFVGGGAE 293
|
170 180
....*....|....*....|...
gi 580854 316 IpaVQEAIKKETGKEAHKGVNPD 338
Cdd:cd24022 294 L--LEDELKEALGPNAIIVDEPE 314
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
476-583 |
4.34e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 476 GLSDEEIER---MVKEAEEN-----ADADAKKKEEIEVRNEADQLVFQTEKTLKDLEgkvdeEQVKKANDAKDALKAAIE 547
Cdd:PRK00409 498 GLPENIIEEakkLIGEDKEKlneliASLEELERELEQKAEEAEALLKEAEKLKEELE-----EKKEKLQEEEDKLLEEAE 572
|
90 100 110
....*....|....*....|....*....|....*...
gi 580854 548 KNEFEEIKAKKDELQTIVQELSMKLYEEAA--KAQQAQ 583
Cdd:PRK00409 573 KEAQQAIKEAKKEADEIIKELRQLQKGGYAsvKAHELI 610
|
|
| YjiL |
COG1924 |
Activator of 2-hydroxyglutaryl-CoA dehydratase (HSP70-class ATPase domain) [Lipid transport ... |
305-347 |
5.68e-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: 38.93 E-value: 5.68e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 580854 305 DKVILVGGSTRIPAVQEAIKKETGKEAHKGVNPDEVVALGAAI 347
Cdd:COG1924 212 EPVVFQGGVAKNDGVVRALEKELGKEVIVPPIPQLMGALGAAL 254
|
|
| NtpH |
COG2811 |
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal ... |
479-579 |
8.42e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit H [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit H is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 442060 [Multi-domain] Cd Length: 108 Bit Score: 36.43 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580854 479 DEEIERMVKEAEENAD-----ADAKKKEEI-EVRNEADQLVFQTEKTLKDLEGKVDEEQVKKANDAKDALKAAIEKNEFE 552
Cdd:COG2811 3 RPEVLKEIKEAEEEADeiieeAKEEREERIaEAREEAEEIIEQAEEEAEEEAQERLEEAREEAEAEAEEIIEEGEKEAEA 82
|
90 100
....*....|....*....|....*..
gi 580854 553 EIKAKKDELQTIVQELsMKLYEEAAKA 579
Cdd:COG2811 83 LKKKAEDKLDKAVELL-VEEFEEAVHA 108
|
|
| |
