|
Name |
Accession |
Description |
Interval |
E-value |
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
52-654 |
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: 934.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQK 131
Cdd:pfam00012 1 VIGIDLGTTNSCVAVMEGGGPEVIANAEGNRTTPSVVAFTPKERLVGQAAKNQAVTNPKNTVFSVKRLIGRKFSDPVVQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 132 DIKHLPFNVVNKD-GKPAVEVSVKGEKkvFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTI 210
Cdd:pfam00012 81 DIKHLPYKVVKLPnGDAGVEVRYLGET--FTPEQISAMILQKLKETAEAYLGKPVTDAVITVPAYFNDAQRQATKDAGQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAF 290
Cdd:pfam00012 159 AGLNVLRIVNEPTAAALAYGLDKTDKERNIAVYDLGGGTFDVSILEIGRGVFEVKATNGDTHLGGEDFDLRLVDHLAEEF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 291 KKKHGIDVSDNNKALAKLKREAEKAKRALSS-QMSTRIEIDSF-VDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQD 368
Cdd:pfam00012 239 KKKYGIDLSKDKRALQRLREAAEKAKIELSSnQTNINLPFITAmADGKDVSGTLTRAKFEELVADLFERTLEPVEKALKD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 369 SGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSGEEGVEDIVLLDVNALTLGIET 448
Cdd:pfam00012 319 AGLSKSEIDEVVLVGGSTRIPAVQELVKEFF-GKEPSKGVNPDEAVAIGAAVQAGVLSGTFDVKDFLLLDVTPLSLGIET 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 449 TGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALDANGI 528
Cdd:pfam00012 398 LGGVMTKLIPRNTTIPTKKSQIFSTAADNQTAVEIQVYQGEREMAPDNKLLGSFELDGIPPAPRGVPQIEVTFDIDANGI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 529 LKVSATDKGTGKSESITITNDKGrLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNgDLGEKLEEED 608
Cdd:pfam00012 478 LTVSAKDKGTGKEQEITIEASEG-LSDDEIERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLE-EEGDKVPEAE 555
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 121575 609 KEtlldAANDVLEWLDDNFETAIAEDFDEKFESLSKVAYPITSKLY 654
Cdd:pfam00012 556 KS----KVESAIEWLKDELEGDDKEEIEAKTEELAQVSQKIGERMY 597
|
|
| PTZ00009 |
PTZ00009 |
heat shock 70 kDa protein; Provisional |
48-662 |
0e+00 |
|
heat shock 70 kDa protein; Provisional
Pssm-ID: 240227 [Multi-domain] Cd Length: 653 Bit Score: 914.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 48 NYGTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDR 127
Cdd:PTZ00009 2 TKGPAIGIDLGTTYSCVGVWKNENVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVARNPENTVFDAKRLIGRKFDDS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 128 SVQKDIKHLPFNVVNK-DGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKD 206
Cdd:PTZ00009 82 VVQSDMKHWPFKVTTGgDDKPMIEVTYQGEKKTFHPEEISSMVLQKMKEIAEAYLGKQVKDAVVTVPAYFNDSQRQATKD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 207 AGTIAGLNVLRIVNEPTAAAIAYGLDKSDK-EHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQ 285
Cdd:PTZ00009 162 AGTIAGLNVLRIINEPTAAAIAYGLDKKGDgEKNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVEF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 286 LIKAFKKKH-GIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEK 364
Cdd:PTZ00009 242 CVQDFKRKNrGKDLSSNQRALRRLRTQCERAKRTLSSSTQATIEIDSLFEGIDYNVTISRARFEELCGDYFRNTLQPVEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 365 VLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKGINPDEAVAYGAAVQAGVLSGEEG--VEDIVLLDVNAL 442
Cdd:PTZ00009 322 VLKDAGMDKRSVHEVVLVGGSTRIPKVQSLIKDFFNGKEPCKSINPDEAVAYGAAVQAAILTGEQSsqVQDLLLLDVTPL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 443 TLGIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFA 522
Cdd:PTZ00009 402 SLGLETAGGVMTKLIERNTTIPTKKSQIFTTYADNQPGVLIQVFEGERAMTKDNNLLGKFHLDGIPPAPRGVPQIEVTFD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 523 LDANGILKVSATDKGTGKSESITITNDKGRLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNGD-LG 601
Cdd:PTZ00009 482 IDANGILNVSAEDKSTGKSNKITITNDKGRLSKADIDRMVNEAEKYKAEDEANRERVEAKNGLENYCYSMKNTLQDEkVK 561
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121575 602 EKLEEEDKETLLDAANDVLEWLDDNfETAIAEDFDEKFESLSKVAYPITSKLYGGADGSGA 662
Cdd:PTZ00009 562 GKLSDSDKATIEKAIDEALEWLEKN-QLAEKEEFEHKQKEVESVCNPIMTKMYQAAGGGMP 621
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
50-663 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 892.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 50 GTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDrs 128
Cdd:PRK00290 2 GKIIGIDLGTTNSCVAVMEGGEPKVIENAEGARTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRLMGRRDEE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 129 VQKDIKHLPFNVVNKDGKPAVeVSVKGekKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAG 208
Cdd:PRK00290 80 VQKDIKLVPYKIVKADNGDAW-VEIDG--KKYTPQEISAMILQKLKKDAEDYLGEKVTEAVITVPAYFNDAQRQATKDAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 209 TIAGLNVLRIVNEPTAAAIAYGLDKsDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIK 288
Cdd:PRK00290 157 KIAGLEVLRIINEPTAAALAYGLDK-KGDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 289 AFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIE---IDSFVDG-IDLSETLTRAKFEELNLDLFKKTLKPVEK 364
Cdd:PRK00290 236 EFKKENGIDLRKDKMALQRLKEAAEKAKIELSSAQQTEINlpfITADASGpKHLEIKLTRAKFEELTEDLVERTIEPCKQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 365 VLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSGEegVEDIVLLDVNALTL 444
Cdd:PRK00290 316 ALKDAGLSVSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLAGD--VKDVLLLDVTPLSL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 445 GIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALD 524
Cdd:PRK00290 393 GIETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVTIHVLQGEREMAADNKSLGRFNLTGIPPAPRGVPQIEVTFDID 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 525 ANGILKVSATDKGTGKSESITITNDKGrLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNgDLGEKL 604
Cdd:PRK00290 473 ANGIVHVSAKDKGTGKEQSITITASSG-LSDEEIERMVKDAEANAEEDKKRKELVEARNQADSLIYQTEKTLK-ELGDKV 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121575 605 EEEDK---ETLLDAANDVLEwlDDNfetaiAEDFDEKFESLSKVAYPITSKLYGGADGSGAA 663
Cdd:PRK00290 551 PADEKekiEAAIKELKEALK--GED-----KEAIKAKTEELTQASQKLGEAMYQQAQAAQGA 605
|
|
| prok_dnaK |
TIGR02350 |
chaperone protein DnaK; Members of this family are the chaperone DnaK, of the DnaK-DnaJ-GrpE ... |
52-654 |
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: 821.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDrsVQ 130
Cdd:TIGR02350 2 IIGIDLGTTNSCVAVMEGGEPVVIPNAEGARTTPSVVAFTKNgERLVGQPAKRQAVTNPENTIYSIKRFMGRRFDE--VT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 KDIKHLPFNVVNKDGkpavEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTI 210
Cdd:TIGR02350 80 EEAKRVPYKVVGDGG----DVRVKVDGKEYTPQEISAMILQKLKKDAEAYLGEKVTEAVITVPAYFNDAQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAF 290
Cdd:TIGR02350 156 AGLEVLRIINEPTAAALAYGLDKSKKDEKILVFDLGGGTFDVSILEIGDGVFEVLSTAGDTHLGGDDFDQRIIDWLADEF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 291 KKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIE---IDSFVDG-IDLSETLTRAKFEELNLDLFKKTLKPVEKVL 366
Cdd:TIGR02350 236 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLSTEINlpfITADASGpKHLEMTLTRAKFEELTADLVERTKEPVRQAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 367 QDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSGEegVEDIVLLDVNALTLGI 446
Cdd:TIGR02350 316 KDAGLSASDIDEVILVGGSTRIPAVQELVKDFF-GKEPNKSVNPDEVVAIGAAIQGGVLKGD--VKDVLLLDVTPLSLGI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 447 ETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALDAN 526
Cdd:TIGR02350 393 ETLGGVMTKLIERNTTIPTKKSQVFSTAADNQPAVDIHVLQGERPMAADNKSLGRFELTGIPPAPRGVPQIEVTFDIDAN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 527 GILKVSATDKGTGKSESITITNDKGrLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNgDLGEKLEE 606
Cdd:TIGR02350 473 GILHVSAKDKGTGKEQSITITASSG-LSEEEIERMVKEAEANAEEDKKRKEEIEARNNADSLAYQAEKTLK-EAGDKLPA 550
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 121575 607 EDKETLLDAANDVLEWLDDNFETAIAedfdEKFESLSKVAYPITSKLY 654
Cdd:TIGR02350 551 EEKEKIEKAVAELKEALKGEDVEEIK----AKTEELQQALQKLAEAMY 594
|
|
| ASKHA_NBD_HSP70_BiP |
cd10241 |
nucleotide-binding domain (NBD) of binding-immunoglobulin protein (BiP) and similar proteins; ... |
50-425 |
0e+00 |
|
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: 794.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 50 GTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSV 129
Cdd:cd10241 1 GTVIGIDLGTTYSCVGVFKNGRVEIIANDQGNRITPSYVAFTDGERLIGDAAKNQATSNPENTVFDVKRLIGRKFDDKEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 130 QKDIKHLPFNVVNKDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGT 209
Cdd:cd10241 81 QKDIKLLPFKIVNKNGKPYIQVEVKGEKKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQRQATKDAGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 210 IAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKA 289
Cdd:cd10241 161 IAGLNVLRIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSLLTIDNGVFEVLATNGDTHLGGEDFDQRVMDHFIKL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 290 FKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDS 369
Cdd:cd10241 241 FKKKTGKDISKDKRAVQKLRREVEKAKRALSSQHQARIEIESLFDGEDFSETLTRAKFEELNMDLFRKTLKPVQKVLEDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 121575 370 GLEKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKGINPDEAVAYGAAVQAGVL 425
Cdd:cd10241 321 GLKKSDIDEIVLVGGSTRIPKVQQLLKDFFNGKEPSRGINPDEAVAYGAAVQAGIL 376
|
|
| PRK13411 |
PRK13411 |
molecular chaperone DnaK; Provisional |
50-660 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184039 [Multi-domain] Cd Length: 653 Bit Score: 715.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 50 GTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFT-DDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRS 128
Cdd:PRK13411 2 GKVIGIDLGTTNSCVAVLEGGKPIVIPNSEGGRTTPSIVGFGkSGDRLVGQLAKRQAVTNAENTVYSIKRFIGRRWDDTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 129 VQKdiKHLPFNVV-NKDGkpAVEVSVKGekKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDA 207
Cdd:PRK13411 82 EER--SRVPYTCVkGRDD--TVNVQIRG--RNYTPQEISAMILQKLKQDAEAYLGEPVTQAVITVPAYFTDAQRQATKDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 208 GTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLI 287
Cdd:PRK13411 156 GTIAGLEVLRIINEPTAAALAYGLDKQDQEQLILVFDLGGGTFDVSILQLGDGVFEVKATAGNNHLGGDDFDNCIVDWLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 288 KAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIdSFVDGID-----LSETLTRAKFEELNLDLFKKTLKPV 362
Cdd:PRK13411 236 ENFQQQEGIDLSQDKMALQRLREAAEKAKIELSSMLTTSINL-PFITADEtgpkhLEMELTRAKFEELTKDLVEATIEPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 363 EKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKGINPDEAVAYGAAVQAGVLSGEegVEDIVLLDVNAL 442
Cdd:PRK13411 315 QQALKDAGLKPEDIDRVILVGGSTRIPAVQEAIQKFFGGKQPDRSVNPDEAVALGAAIQAGVLGGE--VKDLLLLDVTPL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 443 TLGIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFA 522
Cdd:PRK13411 393 SLGIETLGEVFTKIIERNTTIPTSKSQVFSTATDGQTSVEIHVLQGERAMAKDNKSLGKFLLTGIPPAPRGVPQIEVSFE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 523 LDANGILKVSATDKGTGKSESITITNdKGRLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNgDLGE 602
Cdd:PRK13411 473 IDVNGILKVSAQDQGTGREQSIRITN-TGGLSSNEIERMRQEAEKYAEEDRRRKQLIELKNQADSLLYSYESTLK-ENGE 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 603 KLEEEDKeTLLDAANDVLEWL--DDNFETaiaEDFDEKFESLSKVAYPITSKLYGGADGS 660
Cdd:PRK13411 551 LISEELK-QRAEQKVEQLEAAltDPNISL---EELKQQLEEFQQALLAIGAEVYQQGGSQ 606
|
|
| DnaK |
COG0443 |
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones] ... |
52-562 |
0e+00 |
|
Molecular chaperone DnaK (HSP70) [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440212 [Multi-domain] Cd Length: 473 Bit Score: 695.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQ 130
Cdd:COG0443 1 AIGIDLGTTNSVVAVVEGGEPQVIPNAEGRRTLPSVVAFPKDgEVLVGEAAKRQAVTNPGRTIRSIKRLLGRSLFDEATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 kdikhlpfnvvnkdgkpavevsVKGekKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTI 210
Cdd:COG0443 81 ----------------------VGG--KRYSPEEISALILRKLKADAEAYLGEPVTRAVITVPAYFDDAQRQATKDAARI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAF 290
Cdd:COG0443 137 AGLEVLRLLNEPTAAALAYGLDKGKEEETILVYDLGGGTFDVSILRLGDGVFEVLATGGDTHLGGDDFDQALADYVAPEF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 291 KKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDsFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDSG 370
Cdd:COG0443 217 GKEEGIDLRLDPAALQRLREAAEKAKIELSSADEAEINLP-FSGGKHLDVELTRAEFEELIAPLVERTLDPVRQALADAG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 371 LEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSGEegVEDivlLDVNALTLGIETTG 450
Cdd:COG0443 296 LSPSDIDAVLLVGGSTRMPAVRERVKELF-GKEPLKGVDPDEAVALGAAIQAGVLAGD--VKD---LDVTPLSLGIETLG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 451 GVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALDANGILK 530
Cdd:COG0443 370 GVFTKLIPRNTTIPTAKSQVFSTAADNQTAVEIHVLQGERELAADNRSLGRFELTGIPPAPRGVPQIEVTFDIDANGILS 449
|
490 500 510
....*....|....*....|....*....|..
gi 121575 531 VSATDKGTGKSESITItndkgrltQEEIDRMV 562
Cdd:COG0443 450 VSAKDLGTGKEQSITI--------KEEIERML 473
|
|
| dnaK |
CHL00094 |
heat shock protein 70 |
50-663 |
0e+00 |
|
heat shock protein 70
Pssm-ID: 214360 [Multi-domain] Cd Length: 621 Bit Score: 691.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 50 GTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFT-DDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDrs 128
Cdd:CHL00094 2 GKVVGIDLGTTNSVVAVMEGGKPTVIPNAEGFRTTPSIVAYTkKGDLLVGQIAKRQAVINPENTFYSVKRFIGRKFSE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 129 VQKDIKHLPFNVVNkDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAG 208
Cdd:CHL00094 80 ISEEAKQVSYKVKT-DSNGNIKIECPALNKDFSPEEISAQVLRKLVEDASKYLGETVTQAVITVPAYFNDSQRQATKDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 209 TIAGLNVLRIVNEPTAAAIAYGLDKSDKEhQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIK 288
Cdd:CHL00094 159 KIAGLEVLRIINEPTAASLAYGLDKKNNE-TILVFDLGGGTFDVSILEVGDGVFEVLSTSGDTHLGGDDFDKKIVNWLIK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 289 AFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIE---IDSFVDG-IDLSETLTRAKFEELNLDLFKKTLKPVEK 364
Cdd:CHL00094 238 EFKKKEGIDLSKDRQALQRLTEAAEKAKIELSNLTQTEINlpfITATQTGpKHIEKTLTRAKFEELCSDLINRCRIPVEN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 365 VLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSGEegVEDIVLLDVNALTL 444
Cdd:CHL00094 318 ALKDAKLDKSDIDEVVLVGGSTRIPAIQELVKKLL-GKKPNQSVNPDEVVAIGAAVQAGVLAGE--VKDILLLDVTPLSL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 445 GIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALD 524
Cdd:CHL00094 395 GVETLGGVMTKIIPRNTTIPTKKSEVFSTAVDNQTNVEIHVLQGERELAKDNKSLGTFRLDGIPPAPRGVPQIEVTFDID 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 525 ANGILKVSATDKGTGKSESITITNdKGRLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNgDLGEKL 604
Cdd:CHL00094 475 ANGILSVTAKDKGTGKEQSITIQG-ASTLPKDEVERMVKEAEKNAAEDKEKREKIDLKNQAESLCYQAEKQLK-ELKDKI 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 121575 605 EEEDKETLldaaNDVLEWLDDNFETAIAEDFDEKFESLSKVAYPITSKLYGGADGSGAA 663
Cdd:CHL00094 553 SEEKKEKI----ENLIKKLRQALQNDNYESIKSLLEELQKALMEIGKEVYSSTSTTDPA 607
|
|
| ASKHA_NBD_HSP70_HSPA1 |
cd10233 |
nucleotide-binding domain (NBD) of 70-kDa heat shock protein 1 (HSPA1) and similar proteins; ... |
53-425 |
0e+00 |
|
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: 684.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQKD 132
Cdd:cd10233 2 IGIDLGTTYSCVGVWQNDKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFDDPVVQSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 133 IKHLPFNVVNKDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIAG 212
Cdd:cd10233 82 MKHWPFKVVSGGDKPKIQVEYKGETKTFTPEEISSMVLTKMKEIAEAYLGKKVKNAVITVPAYFNDSQRQATKDAGTIAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 213 LNVLRIVNEPTAAAIAYGLDKSDK-EHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAFK 291
Cdd:cd10233 162 LNVLRIINEPTAAAIAYGLDKKGKgERNVLIFDLGGGTFDVSLLTIEDGIFEVKATAGDTHLGGEDFDNRLVNHFVQEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 292 KKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDSGL 371
Cdd:cd10233 242 RKHKKDISGNPRALRRLRTACERAKRTLSSSTQASIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLRDAKL 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 121575 372 EKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKGINPDEAVAYGAAVQAGVL 425
Cdd:cd10233 322 DKSQIHEIVLVGGSTRIPKVQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAIL 375
|
|
| ASKHA_NBD_HSP70_HSPA1-like |
cd24028 |
nucleotide-binding domain (NBD) of the 70-kDa heat shock protein 1 (HSPA1)-like family; The ... |
52-425 |
0e+00 |
|
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: 679.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQK 131
Cdd:cd24028 1 AIGIDLGTTYSCVAVWRNGKVEIIPNDQGNRTTPSYVAFTDGERLVGEAAKNQAASNPENTIFDVKRLIGRKFDDPSVQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 132 DIKHLPFNVVNK-DGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTI 210
Cdd:cd24028 81 DIKHWPFKVVEDeDGKPKIEVTYKGEEKTFSPEEISAMILKKLKEIAEAYLGRPVTKAVITVPAYFNDAQRQATKDAATI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYGLD-KSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKA 289
Cdd:cd24028 161 AGLNVLRIINEPTAAALAYGLDkKSSGERNVLVFDLGGGTFDVSLLSIDNGVFEVKATAGDTHLGGEDFDNRLVEYLVEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 290 FKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDS 369
Cdd:cd24028 241 FKKKHGKDLRENPRAMRRLRSACERAKRTLSTSTSATIEIDSLYDGIDFETTITRAKFEELCEDLFKKCLEPVEKVLKDA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 121575 370 GLEKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKGINPDEAVAYGAAVQAGVL 425
Cdd:cd24028 321 KLSKDDIDEVVLVGGSTRIPKIQELLSEFFGGKELCKSINPDEAVAYGAAIQAAIL 376
|
|
| PTZ00400 |
PTZ00400 |
DnaK-type molecular chaperone; Provisional |
50-662 |
0e+00 |
|
DnaK-type molecular chaperone; Provisional
Pssm-ID: 240403 [Multi-domain] Cd Length: 663 Bit Score: 678.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 50 GTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRS 128
Cdd:PTZ00400 41 GDIVGIDLGTTNSCVAIMEGSQPKVIENSEGMRTTPSVVAFTEDgQRLVGIVAKRQAVTNPENTVFATKRLIGRRYDEDA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 129 VQKDIKHLPFNVVNKDGKPAvevSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAG 208
Cdd:PTZ00400 121 TKKEQKILPYKIVRASNGDA---WIEAQGKKYSPSQIGAFVLEKMKETAESYLGRKVKQAVITVPAYFNDSQRQATKDAG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 209 TIAGLNVLRIVNEPTAAAIAYGLDKSDKEhQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIK 288
Cdd:PTZ00400 198 KIAGLDVLRIINEPTAAALAFGMDKNDGK-TIAVYDLGGGTFDISILEILGGVFEVKATNGNTSLGGEDFDQRILNYLIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 289 AFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIdSFVDG-----IDLSETLTRAKFEELNLDLFKKTLKPVE 363
Cdd:PTZ00400 277 EFKKQQGIDLKKDKLALQRLREAAETAKIELSSKTQTEINL-PFITAdqsgpKHLQIKLSRAKLEELTHDLLKKTIEPCE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 364 KVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSGEegVEDIVLLDVNALT 443
Cdd:PTZ00400 356 KCIKDAGVKKDELNDVILVGGMTRMPKVSETVKKIF-GKEPSKGVNPDEAVAMGAAIQAGVLKGE--IKDLLLLDVTPLS 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 444 LGIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFAL 523
Cdd:PTZ00400 433 LGIETLGGVFTRLINRNTTIPTKKSQVFSTAADNQTQVGIKVFQGEREMAADNKLLGQFDLVGIPPAPRGVPQIEVTFDV 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 524 DANGILKVSATDKGTGKSESITITNDKGrLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNgDLGEK 603
Cdd:PTZ00400 513 DANGIMNISAVDKSTGKKQEITIQSSGG-LSDEEIEKMVKEAEEYKEQDEKKKELVDAKNEAETLIYSVEKQLS-DLKDK 590
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 121575 604 LEEEDKETLldaaNDVLEWLDDNFETAIAEDFDEKFESLSKVAYPITSKLYGGADGSGA 662
Cdd:PTZ00400 591 ISDADKDEL----KQKITKLRSTLSSEDVDSIKDKTKQLQEASWKISQQAYKQGNSDNQ 645
|
|
| PRK13410 |
PRK13410 |
molecular chaperone DnaK; Provisional |
50-626 |
0e+00 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 184038 [Multi-domain] Cd Length: 668 Bit Score: 675.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 50 GTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFT-DDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRS 128
Cdd:PRK13410 2 GRIVGIDLGTTNSVVAVMEGGKPVVIANAEGMRTTPSVVGFTkDGELLVGQLARRQLVLNPQNTFYNLKRFIGRRYDELD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 129 vqKDIKHLPFNVvNKDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAG 208
Cdd:PRK13410 82 --PESKRVPYTI-RRNEQGNVRIKCPRLEREFAPEELSAMILRKLADDASRYLGEPVTGAVITVPAYFNDSQRQATRDAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 209 TIAGLNVLRIVNEPTAAAIAYGLDKSDkEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIK 288
Cdd:PRK13410 159 RIAGLEVERILNEPTAAALAYGLDRSS-SQTVLVFDLGGGTFDVSLLEVGNGVFEVKATSGDTQLGGNDFDKRIVDWLAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 289 AFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIE---IDSFVDG-IDLSETLTRAKFEELNLDLFKKTLKPVEK 364
Cdd:PRK13410 238 QFLEKEGIDLRRDRQALQRLTEAAEKAKIELSGVSVTDISlpfITATEDGpKHIETRLDRKQFESLCGDLLDRLLRPVKR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 365 VLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESyFDGKKASKGINPDEAVAYGAAVQAGVLSGEegVEDIVLLDVNALTL 444
Cdd:PRK13410 318 ALKDAGLSPEDIDEVVLVGGSTRMPMVQQLVRT-LIPREPNQNVNPDEVVAVGAAIQAGILAGE--LKDLLLLDVTPLSL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 445 GIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALD 524
Cdd:PRK13410 395 GLETIGGVMKKLIPRNTTIPVRRSDVFSTSENNQSSVEIHVWQGEREMASDNKSLGRFKLSGIPPAPRGVPQVQVAFDID 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 525 ANGILKVSATDKGTGKSESITITNdKGRLTQEEIDRMVEEAEKFASEDASIKAKVESRNKlenyAHSLKNQ-------VN 597
Cdd:PRK13410 475 ANGILQVSATDRTTGREQSVTIQG-ASTLSEQEVNRMIQEAEAKADEDRRRRERIEKRNR----ALTLIAQaerrlrdAA 549
|
570 580
....*....|....*....|....*....
gi 121575 598 GDLGEKLEEEDKETLLDAANDVLEWLDDN 626
Cdd:PRK13410 550 LEFGPYFAERQRRAVESAMRDVQDSLEQD 578
|
|
| PTZ00186 |
PTZ00186 |
heat shock 70 kDa precursor protein; Provisional |
50-633 |
0e+00 |
|
heat shock 70 kDa precursor protein; Provisional
Pssm-ID: 140213 [Multi-domain] Cd Length: 657 Bit Score: 630.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 50 GTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSV 129
Cdd:PTZ00186 27 GDVIGVDLGTTYSCVATMDGDKARVLENSEGFRTTPSVVAFKGSEKLVGLAAKRQAITNPQSTFYAVKRLIGRRFEDEHI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 130 QKDIKHLPFNVVNK-DGKPAVEvsvKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAG 208
Cdd:PTZ00186 107 QKDIKNVPYKIVRAgNGDAWVQ---DGNGKQYSPSQIGAFVLEKMKETAENFLGHKVSNAVVTCPAYFNDAQRQATKDAG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 209 TIAGLNVLRIVNEPTAAAIAYGLDKSdKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIK 288
Cdd:PTZ00186 184 TIAGLNVIRVVNEPTAAALAYGMDKT-KDSLIAVYDLGGGTFDISVLEIAGGVFEVKATNGDTHLGGEDFDLALSDYILE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 289 AFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIE---IDSFVDGID-LSETLTRAKFEELNLDLFKKTLKPVEK 364
Cdd:PTZ00186 263 EFRKTSGIDLSKERMALQRVREAAEKAKCELSSAMETEVNlpfITANADGAQhIQMHISRSKFEGITQRLIERSIAPCKQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 365 VLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSGEegVEDIVLLDVNALTL 444
Cdd:PTZ00186 343 CMKDAGVELKEINDVVLVGGMTRMPKVVEEVKKFF-QKDPFRGVNPDEAVALGAATLGGVLRGD--VKGLVLLDVTPLSL 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 445 GIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALD 524
Cdd:PTZ00186 420 GIETLGGVFTRMIPKNTTIPTKKSQTFSTAADNQTQVGIKVFQGEREMAADNQMMGQFDLVGIPPAPRGVPQIEVTFDID 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 525 ANGILKVSATDKGTGKSESITITNDKGrLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQvngdLGE-- 602
Cdd:PTZ00186 500 ANGICHVTAKDKATGKTQNITITANGG-LSKEQIEQMIRDSEQHAEADRVKRELVEVRNNAETQLTTAERQ----LGEwk 574
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 121575 603 ---KLEEEDKETLL----------DAANDVLEWLDDNFETAIAE 633
Cdd:PTZ00186 575 yvsDAEKENVKTLVaelrkamenpNVAKDDLAAATDKLQKAVME 618
|
|
| PLN03184 |
PLN03184 |
chloroplast Hsp70; Provisional |
52-663 |
0e+00 |
|
chloroplast Hsp70; Provisional
Pssm-ID: 215618 [Multi-domain] Cd Length: 673 Bit Score: 616.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDrsVQ 130
Cdd:PLN03184 41 VVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKNgDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMSE--VD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 KDIKHLPFNVVNKD-GKPAVEVSVKGekKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGT 209
Cdd:PLN03184 119 EESKQVSYRVVRDEnGNVKLDCPAIG--KQFAAEEISAQVLRKLVDDASKFLNDKVTKAVITVPAYFNDSQRTATKDAGR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 210 IAGLNVLRIVNEPTAAAIAYGLDKSDKEhQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKA 289
Cdd:PLN03184 197 IAGLEVLRIINEPTAASLAYGFEKKSNE-TILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRIVDWLASN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 290 FKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIE---IDSFVDG---IDLseTLTRAKFEELNLDLFKKTLKPVE 363
Cdd:PLN03184 276 FKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTSISlpfITATADGpkhIDT--TLTRAKFEELCSDLLDRCKTPVE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 364 KVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESyFDGKKASKGINPDEAVAYGAAVQAGVLSGEegVEDIVLLDVNALT 443
Cdd:PLN03184 354 NALRDAKLSFKDIDEVILVGGSTRIPAVQELVKK-LTGKDPNVTVNPDEVVALGAAVQAGVLAGE--VSDIVLLDVTPLS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 444 LGIETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFAL 523
Cdd:PLN03184 431 LGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDI 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 524 DANGILKVSATDKGTGKSESITITNdKGRLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNgDLGEK 603
Cdd:PLN03184 511 DANGILSVSATDKGTGKKQDITITG-ASTLPKDEVERMVQEAEKFAKEDKEKRDAVDTKNQADSVVYQTEKQLK-ELGDK 588
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 604 LEEEDKETLLDAANDvlewLDDNFETAIAEDFDEKFESLSKVAYPITSKLYGGADGSGAA 663
Cdd:PLN03184 589 VPADVKEKVEAKLKE----LKDAIASGSTQKMKDAMAALNQEVMQIGQSLYNQPGAGGAG 644
|
|
| ASKHA_NBD_HSP70_DnaK-like |
cd10234 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein DnaK and similar ... |
52-426 |
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: 562.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQ 130
Cdd:cd10234 1 IIGIDLGTTNSCVAVMEGGKPTVIPNAEGGRTTPSVVAFTKDgERLVGQPAKRQAVTNPENTIFSIKRFMGRRYKEVEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 KDIKHLPfnvVNKDGKPAVEVSVKGekKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTI 210
Cdd:cd10234 81 RKQVPYP---VVSAGNGDAWVEIGG--KEYTPEEISAFILQKLKKDAEAYLGEKVTKAVITVPAYFNDSQRQATKDAGKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYGLDKsDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAF 290
Cdd:cd10234 156 AGLEVLRIINEPTAAALAYGLDK-KKDEKILVYDLGGGTFDVSILEIGDGVFEVLSTNGDTHLGGDDFDQRIIDYLADEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 291 KKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIE---IDSFVDG-IDLSETLTRAKFEELNLDLFKKTLKPVEKVL 366
Cdd:cd10234 235 KKEEGIDLSKDKMALQRLKEAAEKAKIELSSVLETEINlpfITADASGpKHLEMKLTRAKFEELTEDLVERTIEPVEQAL 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 367 QDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLS 426
Cdd:cd10234 315 KDAKLSPSDIDEVILVGGSTRMPAVQELVKEFF-GKEPNKGVNPDEVVAIGAAIQGGVLA 373
|
|
| ASKHA_NBD_HSP70_Ssb |
cd24093 |
nucleotide-binding domain (NBD) of Saccharmoyces cerevisiae Hsp70 chaperone Ssb and similar ... |
53-425 |
0e+00 |
|
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: 561.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNgKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQKD 132
Cdd:cd24093 2 IGIDLGTTYSCVATYES-SVEIIANEQGNRVTPSFVAFTPEERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 133 IKHLPFNVVNKDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIAG 212
Cdd:cd24093 81 MKTWPFKVIDVNGNPVIEVQYLGETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 213 LNVLRIVNEPTAAAIAYGLD--KSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAF 290
Cdd:cd24093 161 LNVLRIINEPTAAAIAYGLGagKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 291 KKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDSG 370
Cdd:cd24093 241 KKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSITRARFEDLNAALFKSTLEPVEQVLKDAK 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 121575 371 LEKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKGINPDEAVAYGAAVQAGVL 425
Cdd:cd24093 321 ISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAIL 375
|
|
| hscA |
PRK05183 |
chaperone protein HscA; Provisional |
53-631 |
0e+00 |
|
chaperone protein HscA; Provisional
Pssm-ID: 235360 [Multi-domain] Cd Length: 616 Bit Score: 545.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDrsVQKD 132
Cdd:PRK05183 22 VGIDLGTTNSLVATVRSGQAEVLPDEQGRVLLPSVVRYLEDGIEVGYEARANAAQDPKNTISSVKRFMGRSLAD--IQQR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 133 IKHLPFN-VVNKDGKPAVEVsVKGEKkvfTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIA 211
Cdd:PRK05183 100 YPHLPYQfVASENGMPLIRT-AQGLK---SPVEVSAEILKALRQRAEETLGGELDGAVITVPAYFDDAQRQATKDAARLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 212 GLNVLRIVNEPTAAAIAYGLDkSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKafk 291
Cdd:PRK05183 176 GLNVLRLLNEPTAAAIAYGLD-SGQEGVIAVYDLGGGTFDISILRLSKGVFEVLATGGDSALGGDDFDHLLADWILE--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 292 kKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIdsfvdgIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDSGL 371
Cdd:PRK05183 252 -QAGLSPRLDPEDQRLLLDAARAAKEALSDADSVEVSV------ALWQGEITREQFNALIAPLVKRTLLACRRALRDAGV 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 372 EKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSGEEGVEDIVLLDVNALTLGIETTGG 451
Cdd:PRK05183 325 EADEVKEVVMVGGSTRVPLVREAVGEFF-GRTPLTSIDPDKVVAIGAAIQADILAGNKPDSDMLLLDVIPLSLGLETMGG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 452 VMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALDANGILKV 531
Cdd:PRK05183 404 LVEKIIPRNTTIPVARAQEFTTFKDGQTAMAIHVVQGERELVADCRSLARFELRGIPPMAAGAARIRVTFQVDADGLLSV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 532 SATDKGTGKSESITITNDKGrLTQEEIDRMVEEAEKFASEDAS----IKAKVESRNKLENYAHSLknQVNGDLgekLEEE 607
Cdd:PRK05183 484 TAMEKSTGVEASIQVKPSYG-LTDDEIARMLKDSMSHAEEDMQaralAEQKVEAERVLEALQAAL--AADGDL---LSAA 557
|
570 580
....*....|....*....|....
gi 121575 608 DKETLLDAANDVLEWLDDNFETAI 631
Cdd:PRK05183 558 ERAAIDAAMAALREVAQGDDADAI 581
|
|
| HscA |
TIGR01991 |
Fe-S protein assembly chaperone HscA; The Heat Shock Cognate proteins HscA and HscB act ... |
52-644 |
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: 531.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGlkyndRSvQ 130
Cdd:TIGR01991 1 AVGIDLGTTNSLVASVRSGVPEVLPDAEGRVLLPSVVRYLKDgGVEVGKEALAAAAEDPKNTISSVKRLMG-----RS-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 KDIK---HLPFNVV-NKDGKPAVEVsVKGEKkvfTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKD 206
Cdd:TIGR01991 75 EDIKtfsILPYRFVdGPGEMVRLRT-VQGTV---TPVEVSAEILKKLKQRAEESLGGDLVGAVITVPAYFDDAQRQATKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 207 AGTIAGLNVLRIVNEPTAAAIAYGLDKSdKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVrql 286
Cdd:TIGR01991 151 AARLAGLNVLRLLNEPTAAAVAYGLDKA-SEGIYAVYDLGGGTFDVSILKLTKGVFEVLATGGDSALGGDDFDHALA--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 287 iKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDsfVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVL 366
Cdd:TIGR01991 227 -KWILKQLGISADLNPEDQRLLLQAARAAKEALTDAESVEVDFT--LDGKDFKGKLTRDEFEALIQPLVQKTLSICRRAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 367 QDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSGEEGVEDIVLLDVNALTLGI 446
Cdd:TIGR01991 304 RDAGLSVEEIKGVVLVGGSTRMPLVRRAVAELF-GQEPLTDIDPDQVVALGAAIQADLLAGNRIGNDLLLLDVTPLSLGI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 447 ETTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALDAN 526
Cdd:TIGR01991 383 ETMGGLVEKIIPRNTPIPVARAQEFTTYKDGQTAMVIHVVQGERELVEDCRSLARFELRGIPPMVAGAARIRVTFQVDAD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 527 GILKVSATDKGTGKSESITITNDKGrLTQEEIDRMVEEAEKFASEDAS----IKAKVESRNKLENYAHSLKNqvNGDLge 602
Cdd:TIGR01991 463 GLLTVSAQEQSTGVEQSIQVKPSYG-LSDEEIERMLKDSFKHAEEDMYaralAEQKVEAERILEALQAALAA--DGDL-- 537
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 121575 603 kLEEEDKETLLDAANDVLEWLDDNFETAIaEDFDEKFESLSK 644
Cdd:TIGR01991 538 -LSEDERAAIDAAMEALQKALQGDDADAI-KAAIEALEEATD 577
|
|
| ASKHA_NBD_HSP70_HSPA9 |
cd11733 |
nucleotide-binding domain (NBD) of human mitochondrial heat shock 70 kDa protein 9 (HSPA9) and ... |
50-425 |
1.83e-175 |
|
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: 504.88 E-value: 1.83e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 50 GTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRS 128
Cdd:cd11733 1 GDVIGIDLGTTNSCVAVMEGKTPKVIENAEGARTTPSVVAFTADgERLVGMPAKRQAVTNPENTLYATKRLIGRRFDDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 129 VQKDIKHLPFNVVNKDGKPAvevSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAG 208
Cdd:cd11733 81 VQKDIKMVPYKIVKASNGDA---WVEAHGKKYSPSQIGAFVLTKMKETAESYLGRPVKNAVITVPAYFNDSQRQATKDAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 209 TIAGLNVLRIVNEPTAAAIAYGLDKSDkEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIK 288
Cdd:cd11733 158 QIAGLNVLRIINEPTAAALAYGLDKKD-DKIIAVYDLGGGTFDISILEIQKGVFEVKATNGDTFLGGEDFDNALLNYLVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 289 AFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIdSFVDgID------LSETLTRAKFEELNLDLFKKTLKPV 362
Cdd:cd11733 237 EFKKEQGIDLSKDNLALQRLREAAEKAKIELSSSLQTDINL-PFIT-ADasgpkhLNMKLTRAKFESLVGDLIKRTVEPC 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 121575 363 EKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVL 425
Cdd:cd11733 315 KKCLKDAGVSKSDIGEVLLVGGMTRMPKVQETVQEIF-GKAPSKGVNPDEAVAMGAAIQGGVL 376
|
|
| ASKHA_NBD_HSP70_Ssc1_3 |
cd11734 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae mitochondrial heat shock protein ... |
50-427 |
3.36e-160 |
|
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: 466.15 E-value: 3.36e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 50 GTVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRS 128
Cdd:cd11734 1 GPVIGIDLGTTNSCVAVMEGKTPRVIENAEGARTTPSVVAFTKDgERLVGVPAKRQAVVNPENTLFATKRLIGRKFDDAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 129 VQKDIKHLPFNVV-NKDGKPAVEVsvKGEKkvFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDA 207
Cdd:cd11734 81 VQRDIKEVPYKIVkHSNGDAWVEA--RGQK--YSPSQIGAFVLGKMKETAEGYLGKPVKNAVVTVPAYFNDSQRQATKDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 208 GTIAGLNVLRIVNEPTAAAIAYGLDKSDkEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLI 287
Cdd:cd11734 157 GQIAGLNVLRVINEPTAAALAYGLDKSG-DKVIAVYDLGGGTFDISILEIQKGVFEVKSTNGDTHLGGEDFDIALVRHIV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 288 KAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIE---IDSFVDG---IDLseTLTRAKFEELNLDLFKKTLKP 361
Cdd:cd11734 236 SEFKKESGIDLSKDRMAIQRIREAAEKAKIELSSTLQTDINlpfITADASGpkhINM--KLTRAQFESLVKPLVDRTVEP 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121575 362 VEKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSG 427
Cdd:cd11734 314 CKKALKDAGVKTSEINEVILVGGMSRMPKVQETVKSIF-GREPSKGVNPDEAVAIGAAIQGGVLSG 378
|
|
| ASKHA_NBD_HSP70_HscA |
cd10236 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscA and similar ... |
52-427 |
2.57e-150 |
|
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: 440.50 E-value: 2.57e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLI-GDAAKNQVAANPQNTIFDIKRLIGLKYNDrsVQ 130
Cdd:cd10236 4 AVGIDLGTTNSLVATVRSGQPEVLPDEKGEALLPSVVHYGEDGKITvGEKAKENAITDPENTISSVKRLMGRSLAD--VK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 KDIKHLPFNVVNKDGkpAVEVSVKGEKkVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTI 210
Cdd:cd10236 82 EELPLLPYRLVGDEN--ELPRFRTGAG-NLTPVEISAEILKELKQRAEETLGGELTGAVITVPAYFDDAQRQATKDAARL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYGLDKsDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDykivRQLIKAF 290
Cdd:cd10236 159 AGLNVLRLLNEPTAAALAYGLDQ-KKEGTIAVYDLGGGTFDISILRLSDGVFEVLATGGDTALGGDDFD----HLLADWI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 291 KKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDsfVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDSG 370
Cdd:cd10236 234 LKQIGIDARLDPAVQQALLQAARRAKEALSDADSASIEVE--VEGKDWEREITREEFEELIQPLVKRTLEPCRRALKDAG 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 121575 371 LEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSG 427
Cdd:cd10236 312 LEPADIDEVVLVGGSTRIPLVRQRVAEFF-GREPLTSINPDEVVALGAAIQADILAG 367
|
|
| ASKHA_NBD_HSP70_DnaK_HscA_HscC |
cd24029 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone proteins DnaK, HscA, HscC and ... |
53-426 |
7.73e-145 |
|
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: 425.84 E-value: 7.73e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILA-NEQGNRITPSYVAFTDDER-LIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSvq 130
Cdd:cd24029 1 VGIDLGTTNSAVAYWDGNGAEVIIeNSEGKRTTPSVVYFDKDGEvLVGEEAKNQALLDPENTIYSVKRLMGRDTKDKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 kdikhlpfnvvnkdgkpavevsvKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTI 210
Cdd:cd24029 79 -----------------------EIGGKEYTPEEISAEILKKLKEDAEEQLGGEVKGAVITVPAYFNDKQRKATKKAAEL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAF 290
Cdd:cd24029 136 AGLNVLRLINEPTAAALAYGLDKEGKDGTILVYDLGGGTFDVSILEIENGKFEVLATGGDNFLGGDDFDEAIAELILEKI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 291 KKKHGIDVSD-NNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDS 369
Cdd:cd24029 216 GIETGILDDKeDERARARLREAAEEAKIELSSSDSTDILILDDGKGGELEIEITREEFEELIAPLIERTIDLLEKALKDA 295
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 121575 370 GLEKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKgINPDEAVAYGAAVQAGVLS 426
Cdd:cd24029 296 KLSPEDIDRVLLVGGSSRIPLVREMLEEYFGREPISS-VDPDEAVAKGAAIYAASLA 351
|
|
| ASKHA_NBD_HSP70_HSPA13 |
cd10237 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 13 (HSPA13) and similar proteins; ... |
51-427 |
9.50e-143 |
|
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: 422.52 E-value: 9.50e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 51 TVIGIDLGTTYSCVAVMK--NGKTEILANEQGNRITPSYVAFTDDER-LIGDAAKNQVAANPQNTIFDIKRLIGLKYNDR 127
Cdd:cd10237 23 KIVGIDLGTTYSCVGVYHavTGEVEVIPDDDGHKSIPSVVAFTPDGGvLVGYDALAQAEHNPSNTIYDAKRFIGKTFTKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 128 SVQKDIKHLPFNVVN-KDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKD 206
Cdd:cd10237 103 ELEEEAKRYPFKVVNdNIGSAFFEVPLNGSTLVVSPEDIGSLILLKLKKAAEAYLGVPVAKAVISVPAEFDEKQRNATRK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 207 AGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQL 286
Cdd:cd10237 183 AANLAGLEVLRVINEPTAAAMAYGLHKKSDVNNVLVVDLGGGTLDVSLLNVQGGMFLTRAMAGNNHLGGQDFNQRLFQYL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 287 IKAFKKKHGIDVSDnNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDG-----IDLSETLTRAKFEELNLDLFKKTLKP 361
Cdd:cd10237 263 IDRIAKKFGKTLTD-KEDIQRLRQAVEEVKLNLTNHNSASLSLPLQISLpsafkVKFKEEITRDLFETLNEDLFQRVLEP 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121575 362 VEKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLSG 427
Cdd:cd10237 342 IRQVLAEVELGKEDVDEIVLVGGSTRIPRVRQLVREFF-GKDPNTSVDPELAVVTGVAIQAGIIGG 406
|
|
| ASKHA_NBD_HSP70_HSPA14 |
cd10238 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 14 (HSPA14) and similar proteins; ... |
51-425 |
4.44e-139 |
|
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: 412.02 E-value: 4.44e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 51 TVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQ 130
Cdd:cd10238 1 AAFGVHFGNTNACVAVYKDGRTDVVANDAGDRVTPAVVAFTDNEKIVGLAAKQGLIRNASNTVVRVKQLLGRSFDDPAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 KDIKHLPFNVVNKDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTI 210
Cdd:cd10238 81 ELKKESKCKIIEKDGKPGYEIELEEKKKLVSPKEVAKLIFKKMKEIAQSHGGSDVIDVVLTVPLDFDEDQRNALKEAAEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYGLDKSDKEHQ--IIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIK 288
Cdd:cd10238 161 AGFNVLRVISEPSAAALAYGIGQDDPTENsnVLVYRLGGTSLDVTVLSVNNGMYRVLATRTDDNLGGDDFTEALAEHLAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 289 AFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQD 368
Cdd:cd10238 241 EFKRQWKQDVRENKRAMAKLMNAAEVCKHVLSTLNTATCSVESLYDGMDFQCNVSRARFESLCSSLFQQCLEPIQEVLNS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 121575 369 SGLEKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKGINPDEAVAYGAAVQAGVL 425
Cdd:cd10238 321 AGLTKEDIDKVILCGGSSRIPKLQQLIKDLFPSAEVLSSIPPDEVIAIGAAKQAGLL 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 ... |
53-422 |
1.48e-135 |
|
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: 403.09 E-value: 1.48e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQKD 132
Cdd:cd11732 1 VGIDFGNQNSVVAAARRGGIDIVLNEVSNRKTPTLVGFTEKERLIGEAAKSQQKSNYKNTIRNFKRLIGLKFDDPEVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 133 IKHLPFNVVN-KDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIA 211
Cdd:cd11732 81 IKLLPFKLVElEDGKVGIEVSYNGEEVVFSPEQVLAMLLGKLKEIAEAANKGEVKDCVISVPGYYTDAQRRALLDAAEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 212 GLNVLRIVNEPTAAAIAYGLDKSDK-----EHQIIVY-DLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQ 285
Cdd:cd11732 161 GLNCLRLINETTAAALDYGIYKSDLleseeKPRIVAFvDMGHSSTQVSIAAFTKGKLKVLSTAFDRNLGGRDFDRALVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 286 LIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKV 365
Cdd:cd11732 241 FAEEFKKKYKIDPLENPKARLRLLDACEKLKKVLSANGEAPLNVECLMEDIDFSGQIKREEFEELIQPLLARLEAPIKKA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 121575 366 LQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQA 422
Cdd:cd11732 321 LAQAGLTKEDLHSVEIVGGGTRVPAVKEAIAEVF-GKDLSTTLNADEAVARGCALQA 376
|
|
| ASKHA_NBD_HSP70_HscC |
cd10235 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein HscC and similar ... |
53-423 |
5.85e-127 |
|
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: 379.67 E-value: 5.85e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDD-ERLIGDAAKNQVAANPQNTIFDIKRLIGlkyNDRSVqk 131
Cdd:cd10235 1 IGIDLGTTNSLVAVWRDGGAELIPNALGEYLTPSVVSVDEDgSILVGRAAKERLVTHPDRTAASFKRFMG---TDKQY-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 132 dikHLpfnvvnkdgkpavevsvkgEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIA 211
Cdd:cd10235 76 ---RL-------------------GNHTFRAEELSALVLKSLKEDAEAYLGEPVTEAVISVPAYFNDEQRKATKDAGELA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 212 GLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDykivRQLIKAFK 291
Cdd:cd10235 134 GLKVERLINEPTAAALAYGLHKREDETRFLVFDLGGGTFDVSVLELFEGVIEVHASAGDNFLGGEDFT----HALADYFL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 292 KKHGIDV-SDNNKALAKLKREAEKAKRALSSQMSTriEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVLQDSG 370
Cdd:cd10235 210 KKHRLDFtSLSPSELAALRKRAEQAKRQLSSQDSA--EIRLTYRGEELEIELTREEFEELCAPLLERLRQPIERALRDAG 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 121575 371 LEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAG 423
Cdd:cd10235 288 LKPSDIDAVILVGGATRMPLVRQLIARLF-GRLPLSSLDPDEAVALGAAIQAA 339
|
|
| ASKHA_NBD_HSP70_HSPA4_like |
cd10228 |
nucleotide-binding domain (NBD) of the heat shock 70 kDa protein 4 (HSPA4)-like subfamily; ... |
53-422 |
2.00e-125 |
|
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: 377.00 E-value: 2.00e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQKD 132
Cdd:cd10228 1 VGFDFGNLSCYIAVARAGGIETIANEYSDRCTPSVVSFGEKNRSMGVAAKNQAITNLKNTVSGFKRLLGRKFDDPFVQKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 133 IKHLPFNVVN-KDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIA 211
Cdd:cd10228 81 LKHLPYKVVKlPNGSVGIKVQYLGEEHVFTPEQVTAMLLTKLKETAETALKTKVVDCVISVPSYFTDAERRAVLDAAQIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 212 GLNVLRIVNEPTAAAIAYGLDKSD------KEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQ 285
Cdd:cd10228 161 GLNCLRLLNDTTAVALAYGIYKQDlpaeeeKPRNVVFVDMGHSSLQVSVCAFNKGKLKVLATAADPNLGGRDFDELLVEH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 286 LIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMST-RIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEK 364
Cdd:cd10228 241 FAEEFKTKYKIDVKSKPRALLRLLTECEKLKKLMSANATElPLNIECFMDDKDVSGKMKRAEFEELCAPLFARVEVPLRS 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 121575 365 VLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQA 422
Cdd:cd10228 321 ALADSKLKPEDIHSVEIVGGSTRIPAIKEIIKKVF-GKEPSTTLNQDEAVARGCALQC 377
|
|
| ASKHA_NBD_HSP70_AtHsp70-14-like |
cd24095 |
nucleotide-binding domain (NBD) of Arabidopsis thaliana heat shock 70 kDa protein 14-16 and ... |
52-426 |
2.53e-121 |
|
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: 367.02 E-value: 2.53e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQK 131
Cdd:cd24095 3 VVGIDFGNENCVVAVARKGGIDVVLNEESNRETPSMVSFGEKQRFLGEAAAASILMNPKNTISQLKRLIGRKFDDPEVQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 132 DIKHLPFNVVN-KDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTI 210
Cdd:cd24095 83 DLKLFPFKVTEgPDGEIGINVNYLGEQKVFTPEQILAMLLSNLKRIAEKNLKTPVTDCVISVPVYFTDAQRRAMLDAAQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYGLDKSDKE-----HQIIVyDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQ 285
Cdd:cd24095 163 AGLNCLRLMNETTATALAYGIYKTDLPetdptNVVFV-DVGHSSTQVCVVAFKKGQLKVLSHAFDRNLGGRDFDEVLFDH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 286 LIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKV 365
Cdd:cd24095 242 FAAEFKEKYKIDVKSNKKASLRLRAACEKVKKILSANPEAPLNIECLMEDKDVKGMITREEFEELAAPLLERLLEPLEKA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121575 366 LQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLS 426
Cdd:cd24095 322 LADSGLTVDQIHSVEVVGSGSRIPAILKILTKFF-GKEPSRTMNASECVARGCALQCAMLS 381
|
|
| ASKHA_NBD_HSP70_HYOU1 |
cd10230 |
nucleotide-binding domain (NBD) of hypoxia up-regulated protein 1 (HYOU1) and similar proteins; ... |
51-422 |
1.07e-111 |
|
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: 340.63 E-value: 1.07e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 51 TVIGIDLGTTYSCVAVMKNGKT-EILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGlkyndrsv 129
Cdd:cd10230 1 AVLGIDLGSEFIKVALVKPGVPfEIVLNEESKRKTPSAVAFRNGERLFGDDALALATRFPENTFSYLKDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 130 qkdikhlpfnvvnkdgkpavevsvkgekkvFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGT 209
Cdd:cd10230 73 ------------------------------YSVEELVAMILEYAKSLAESFAGEPIKDAVITVPPFFTQAQRQALLDAAE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 210 IAGLNVLRIVNEPTAAAIAYGLDK---SDKEHQIIVYDLGGGTFDVSLLSI------------ENGVFEVQATSGDTHLG 274
Cdd:cd10230 123 IAGLNVLSLINDNTAAALNYGIDRrfeNNEPQNVLFYDMGASSTSATVVEFssvkekdkgknkTVPQVEVLGVGWDRTLG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 275 GEDFDYKIVRQLIKAFKKKHGI--DVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNL 352
Cdd:cd10230 203 GLEFDLRLADHLADEFNEKHKKdkDVRTNPRAMAKLLKEANRVKEVLSANTEAPASIESLYDDIDFRTKITREEFEELCA 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 353 DLFKKTLKPVEKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFDGKKASKGINPDEAVAYGAAVQA 422
Cdd:cd10230 283 DLFERVVAPIEEALEKAGLTLDDIDSVELIGGGTRVPKVQEALKEALGRKELGKHLNADEAAALGAAFYA 352
|
|
| ASKHA_NBD_HSP70_ScSse |
cd24094 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae heat shock protein homolog Sse and ... |
53-426 |
8.05e-110 |
|
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: 337.04 E-value: 8.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQKD 132
Cdd:cd24094 1 VGLDLGNLNSVIAVARNRGIDIIVNEVSNRSTPSLVGFGPKSRYLGEAAKTQETSNFKNTVGSLKRLIGRTFSDPEVAEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 133 IKHLPFNVVNKDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIAG 212
Cdd:cd24094 81 EKYFTAKLVDANGEVGAEVNYLGEKHVFSATQLAAMYLGKLKDTTQAELKAPVSDVVISVPGWFTDEQRRAILDAAEIAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 213 LNVLRIVNEPTAAAIAYGLDKSD------KEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQL 286
Cdd:cd24094 161 LNPLRLMNDTTAAALGYGITKTDlpepeeKPRIVAFVDIGHSSYTVSIVAFKKGQLTVKGTAYDRHFGGRDFDKALTDHF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 287 IKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEKVL 366
Cdd:cd24094 241 ADEFKEKYKIDVRSNPKAYFRLLAAAEKLKKVLSANAQAPLNVESLMNDIDVSSMLKREEFEELIAPLLERVTAPLEKAL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 367 QDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLS 426
Cdd:cd24094 321 AQAGLTKDEIDFVELVGGTTRVPALKESISAFF-GKPLSTTLNQDEAVARGAAFACAILS 379
|
|
| hscA |
PRK01433 |
chaperone protein HscA; Provisional |
52-576 |
1.51e-107 |
|
chaperone protein HscA; Provisional
Pssm-ID: 234955 [Multi-domain] Cd Length: 595 Bit Score: 338.37 E-value: 1.51e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDaaknqvaanpQNTIFDIKRLIG--LK--YNDR 127
Cdd:PRK01433 21 AVGIDFGTTNSLIAIATNRKVKVIKSIDDKELIPTTIDFTSNNFTIGN----------NKGLRSIKRLFGktLKeiLNTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 128 SVQKDIKHLPfnVVNKDgkpavEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDA 207
Cdd:PRK01433 91 ALFSLVKDYL--DVNSS-----ELKLNFANKQLRIPEIAAEIFIYLKNQAEEQLKTNITKAVITVPAHFNDAARGEVMLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 208 GTIAGLNVLRIVNEPTAAAIAYGLDKSDKeHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLI 287
Cdd:PRK01433 164 AKIAGFEVLRLIAEPTAAAYAYGLNKNQK-GCYLVYDLGGGTFDVSILNIQEGIFQVIATNGDNMLGGNDIDVVITQYLC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 288 KAFKKKHGIDVSdnnkalaklkREAEKAKRALSSQmstrieiDSFVDGIdlsETLTRAKFEELNLDLFKKTLKPVEKVLQ 367
Cdd:PRK01433 243 NKFDLPNSIDTL----------QLAKKAKETLTYK-------DSFNNDN---ISINKQTLEQLILPLVERTINIAQECLE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 368 DSGLEKkdVDDIVLVGGSTRIPKVQQLLESYFDGKKASKgINPDEAVAYGAAVQAGVLSGEEgvEDIVLLDVNALTLGIE 447
Cdd:PRK01433 303 QAGNPN--IDGVILVGGATRIPLIKDELYKAFKVDILSD-IDPDKAVVWGAALQAENLIAPH--TNSLLIDVVPLSLGME 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 448 TTGGVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLGKFELTGIPPAPRGVPQIEVTFALDANG 527
Cdd:PRK01433 378 LYGGIVEKIIMRNTPIPISVVKEFTTYADNQTGIQFHILQGEREMAADCRSLARFELKGLPPMKAGSIRAEVTFAIDADG 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 121575 528 ILKVSATDKGTGKSESITITNDKGrLTQEEIDRMVEEAEKFASEDASIK 576
Cdd:PRK01433 458 ILSVSAYEKISNTSHAIEVKPNHG-IDKTEIDIMLENAYKNAKIDYTTR 505
|
|
| ASKHA_NBD_HSP70_ScSsz1p-like |
cd10232 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae ribosome-associated complex ... |
51-425 |
1.05e-96 |
|
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: 301.59 E-value: 1.05e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 51 TVIGIDLGTTYSCVA-VMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGlkyndrsv 129
Cdd:cd10232 1 VVIGISFGNSNSSIAiINKDGRAEVIANEDGDRQIPSILAYHGDEEYHGSQAKAQLVRNPKNTVANFRDLLG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 130 qkdikhlpfnvvnkdgkpavevsvkgeKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGT 209
Cdd:cd10232 73 ---------------------------TTTLTVSEVTTRYLRRLKESAEDYLGKKVTGAVLSVPTDFTEKQKAALVAAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 210 IAGLNVLRIVNEPTAAAIAYGLDKSDKEHQ-----IIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVR 284
Cdd:cd10232 126 AAGLEVLQLIPEPAAAALAYDLRAETSGDTikdktVVVADLGGTRSDVTVVAVRGGLYTILATVHDYELGGVALDDVLVG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 285 QLIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPVEK 364
Cdd:cd10232 206 HFAKEFKKKTKTDPRKNARSLAKLRNAAEITKRALSQGTSAPCSVESLADGIDFHSSINRTRYELLASKVFQQFADLVTD 285
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121575 365 VLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFDG---KKASKGINPDEAVAYGAAVQAGVL 425
Cdd:cd10232 286 AIEKAGLDPLDIDEVLLAGGASRTPKLASNFEYLFPEstiIRAPTQINPDELIARGAALQASLI 349
|
|
| ASKHA_NBD_HSP70_HSPA4 |
cd11737 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ... |
51-424 |
9.94e-92 |
|
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: 289.92 E-value: 9.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 51 TVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQ 130
Cdd:cd11737 1 SVVGFDLGFQSCYVAVARAGGIETVANEYSDRSTPACVSFGPKNRSIGAAAKSQVISNAKNTVQGFKRFHGRAFSDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 KDIKHLPFNVVN-KDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGT 209
Cdd:cd11737 81 AEKPSLAYELVQlPTGTTGIKVMYMEEERNFTIEQVTAMLLTKLKETAESALKKPVVDCVVSVPCFYTDAERRSVMDATQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 210 IAGLNVLRIVNEPTAAAIAYGLDKSD------KEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIV 283
Cdd:cd11737 161 IAGLNCLRLMNETTAVALAYGIYKQDlpapeeKPRNVVFVDMGHSAYQVSVCAFNKGKLKVLATAFDPTLGGRKFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 284 RQLIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMST-RIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPV 362
Cdd:cd11737 241 NHFCEEFGKKYKLDIKSKIRALLRLFQECEKLKKLMSANASDlPLNIECFMNDIDVSGTMNRGQFEEMCADLLARVEPPL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 121575 363 EKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGV 424
Cdd:cd11737 321 RSVLEQAKLKKEDIYAVEIVGGATRIPAVKERISKFF-GKEVSTTLNADEAVARGCALQCAI 381
|
|
| ASKHA_NBD_HSP70_HSPH1 |
cd11739 |
nucleotide-binding domain (NBD) of heat shock 105kDa/110kDa protein 1 (HSPH1) and similar ... |
51-421 |
6.07e-91 |
|
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: 287.91 E-value: 6.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 51 TVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQ 130
Cdd:cd11739 1 SVVGFDVGFQNCYIAVARAGGIETVANEFSDRCTPSVVSFGSKNRTIGVAAKNQQITNANNTVSNFKRFHGRAFNDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 KDIKHLPFNVVN-KDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGT 209
Cdd:cd11739 81 KEKENLSYDLVPlKNGGVGVKVMYLDEEHHFSIEQITAMLLTKLKETAENNLKKPVTDCVISVPSFFTDAERRSVLDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 210 IAGLNVLRIVNEPTAAAIAYGLDK-----SDKEHQIIVY-DLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIV 283
Cdd:cd11739 161 IVGLNCLRLMNDMTAVALNYGIYKqdlpaPDEKPRIVVFvDMGHSAFQVSACAFNKGKLKVLGTAFDPYLGGRNFDEKLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 284 RQLIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQmSTRI--EIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKP 361
Cdd:cd11739 241 EHFCAEFKTKYKLDVKSKIRALLRLYQECEKLKKLMSSN-STDLplNIECFMNDKDVSGKMNRSQFEELCADLLQRIEVP 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 362 VEKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQ 421
Cdd:cd11739 320 LYSLMEQTQLKVEDISAVEIVGGATRIPAVKERIAKFF-GKDVSTTLNADEAVARGCALQ 378
|
|
| ASKHA_NBD_HSP70_HSPA4L |
cd11738 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4L (HSPA4L) and similar proteins; ... |
51-426 |
9.23e-89 |
|
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: 282.19 E-value: 9.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 51 TVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDAAKNQVAANPQNTIFDIKRLIGLKYNDRSVQ 130
Cdd:cd11738 1 SVVGIDVGFQNCYIAVARSGGIETIANEYSDRCTPACVSLGSRNRAIGNAAKSQIVTNAKNTIHGFKKFHGRAFDDPFVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 131 KDIKHLPFNVVN-KDGKPAVEVSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGT 209
Cdd:cd11738 81 AEKIKLPYELQKmPNGSTGVKVRYLDEERVFAIEQVTGMLLTKLKETSENALKKPVADCVISVPSFFTDAERRSVMDAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 210 IAGLNVLRIVNEPTAAAIAYGLDKSD------KEHQIIVYDLGGGTFDVSLLSIENGVFEVQATSGDTHLGGEDFDYKIV 283
Cdd:cd11738 161 IAGLNCLRLMNETTAVALAYGIYKQDlpaleeKPRNVVFVDMGHSAYQVSICAFNKGKLKVLATTFDPYLGGRNFDEVLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 284 RQLIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMST-RIEIDSFVDGIDLSETLTRAKFEELNLDLFKKTLKPV 362
Cdd:cd11738 241 DYFCEEFKTKYKLNVKENIRALLRLYQECEKLKKLMSANASDlPLNIECFMNDIDVSSKMNRAQFEELCASLLARVEPPL 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121575 363 EKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAAVQAGVLS 426
Cdd:cd11738 321 KAVMEQAKLQREDIYSIEIVGGATRIPAVKERIAKFF-GKDISTTLNADEAVARGCALQCAILS 383
|
|
| ASKHA_NBD_HSP70 |
cd10170 |
nucleotide-binding domain (NBD) of the HSP70 family; HSP70 (70-kDa heat shock protein) family ... |
53-420 |
1.95e-56 |
|
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: 195.02 E-value: 1.95e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILA---------NEQGNRITPSYVaftdderligdaaknqvaanpqntifdikrliglk 123
Cdd:cd10170 1 VGIDFGTTYSGVAYALLGPGEPPLvvlqlpwpgGDGGSSKVPSVL----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 124 yndrsvqkdikhlpfnvvnkdgkpavevsvkgekkvftpeEISGMILGKMKQIAEDYLGTKV-------THAVVTVPAYF 196
Cdd:cd10170 46 ----------------------------------------EVVADFLRALLEHAKAELGDRIwelekapIEVVITVPAGW 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 197 NDAQRQATKDAGTIAGL----NVLRIVNEPTAAAIAYGLDKSDKEHQ-----IIVYDLGGGTFDVSLLSIENGVFEVQ-- 265
Cdd:cd10170 86 SDAAREALREAARAAGFgsdsDNVRLVSEPEAAALYALEDKGDLLPLkpgdvVLVCDAGGGTVDLSLYEVTSGSPLLLee 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 266 -ATSGDTHLGGEDFDYKIVRQLIKAFKKKHGIDVSDNNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLS---ET 341
Cdd:cd10170 166 vAPGGGALLGGTDIDEAFEKLLREKLGDKGKDLGRSDADALAKLLREFEEAKKRFSGGEEDERLVPSLLGGGLPElglEK 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 342 LTRAKFEELNLDLFKKTLKPVEKVLQD--SGLEKKDVDDIVLVGGSTRIPKVQQLLESYFDG---KKASKGINPDEAVAY 416
Cdd:cd10170 246 GTLLLTEEEIRDLFDPVIDKILELIEEqlEAKSGTPPDAVVLVGGFSRSPYLRERLRERFGSagiIIVLRSDDPDTAVAR 325
|
....
gi 121575 417 GAAV 420
Cdd:cd10170 326 GAAL 329
|
|
| ASKHA_NBD_HSP70_YegD-like |
cd10231 |
nucleotide-binding domain (NBD) of Escherichia coli chaperone protein YegD and similar ... |
53-420 |
2.13e-40 |
|
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: 152.81 E-value: 2.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDE------RLIGDAAKNQVAANPQNTifdikRLIglkynd 126
Cdd:cd10231 1 IGLDFGTSNSSLAVADDGKTDLVPFEGDSPTLPSLLYFPRREeegaesIYFGNDAIDAYLNDPEEG-----RLI------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 127 RSVQKDI--KHLPFNVVNkdgkpavevsvkgeKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQAT 204
Cdd:cd10231 70 KSVKSFLgsSLFDETTIF--------------GRRYPFEDLVAAILRHLKRRAERQLGEEIDSVVVGRPVHFSGVGAEDD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 205 -------KDAGTIAGLNVLRIVNEPTAAAIAYGLDkSDKEHQIIVYDLGGGTFDVSLL----SIENGVFEVQATSGDtHL 273
Cdd:cd10231 136 aqaesrlRDAARRAGFRNVEFQYEPIAAALDYEQR-LDREELVLVVDFGGGTSDFSVLrlgpNRTDRRADILATSGV-GI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 274 GGEDFDYKIVRQLIK-----------------------------------------AFKKKHGIDVSDNNKALA------ 306
Cdd:cd10231 214 GGDDFDRELALKKVMphlgrgstyvsgdkglpvpawlyadlsnwhaisllytkktlRLLLDLRRDAADPEKIERllslve 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 307 -----KLKREAEKAKRALSSQMSTRIEIDSFVDGIDlsETLTRAKFEELNLDLFKKTLKPVEKVLQDSGLEKKDVDDIVL 381
Cdd:cd10231 294 dqlghRLFRAVEQAKIALSSADEATLSFDFIEISIK--VTITRDEFETAIAFPLARILEALERTLNDAGVKPSDVDRVFL 371
|
410 420 430
....*....|....*....|....*....|....*....
gi 121575 382 VGGSTRIPKVQQLLESYFDGKKASKGiNPDEAVAYGAAV 420
Cdd:cd10231 372 TGGSSQSPAVRQALASLFGQARLVEG-DEFGSVAAGLAL 409
|
|
| ASKHA_NBD_HSP70_HSPA12 |
cd10229 |
nucleotide-binding domain (NBD) of heat shock 70 kDa proteins HSPA12A, HSPA12B and similar ... |
52-419 |
8.12e-19 |
|
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: 88.87 E-value: 8.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 52 VIGIDLGTTYSCVAVMKNGKTEILA---------NEQGNRITPSYVAFTDDERL--IGDAAKnqvaanpqntifdiKRLI 120
Cdd:cd10229 2 VVAIDFGTTYSGYAYSFITDPGDIHtmynwwgapTGVSSPKTPTCLLLNPDGEFhsFGYEAR--------------EKYS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 121 GLKYNDRS----VQKDIKHLPFNVvnKDGKPAVEVSVKGEK----KVFTpeeisgMILGKMKQ-----IAEDYLGTKVTH 187
Cdd:cd10229 68 DLAEDEEHqwlyFFKFKMMLLSEK--ELTRDTKVKAVNGKSmpalEVFA------EALRYLKDhalkeLRDRSGSSLDED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 188 A---VVTVPAYFNDAQRQATKDAGTIAGL------NVLRIVNEPTAAAIAYG-LDKSDKEHQI------IVYDLGGGTFD 251
Cdd:cd10229 140 DirwVLTVPAIWSDAAKQFMREAAVKAGLiseensEQLIIALEPEAAALYCQkLLAEGEEKELkpgdkyLVVDCGGGTVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 252 VSLLSIEN--GVFEVQATSGDtHLGGEDFD--------YKIVRQLIKAFKKKHGIDvsdnnkaLAKLKREAEKAKRalss 321
Cdd:cd10229 220 ITVHEVLEdgKLEELLKASGG-PWGSTSVDeefeelleEIFGDDFMEAFKQKYPSD-------YLDLLQAFERKKR---- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 322 qmSTRIEIdsfvdgidlsetlTRAKFEELNLDLFKKTLKPVEKVLQdsGLEKKDVDDIVLVGGSTRIPKVQQLLESYFDG 401
Cdd:cd10229 288 --SFKLRL-------------SPELMKSLFDPVVKKIIEHIKELLE--KPELKGVDYIFLVGGFAESPYLQKAVKEAFST 350
|
410 420
....*....|....*....|..
gi 121575 402 KkasKGI----NPDEAVAYGAA 419
Cdd:cd10229 351 K---VKIiippEPGLAVVKGAV 369
|
|
| ASKHA_NBD_MreB-like |
cd10225 |
nucleotide-binding domain (NBD) of the cell shape-determining proteins MreB, Mbl, MreBH and ... |
53-420 |
4.50e-17 |
|
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: 82.52 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGkteILANEqgnritPSYVAF---TDDERLIGDAAKNQVAANPQN--TIFDIKRliGLKYNDR 127
Cdd:cd10225 2 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAVdknTGKVLAVGEEAKKMLGRTPGNivAIRPLRD--GVIADFE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 128 SVQKDIKHLpfnvVNKdgkpavevsVKGEKKVFTPeeisgmilgkmkqiaedylgtkvtHAVVTVPAYFNDAQRQATKDA 207
Cdd:cd10225 71 ATEAMLRYF----IRK---------AHRRRGFLRP------------------------RVVIGVPSGITEVERRAVKEA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 208 GTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVyDLGGGTFDVSLLSIeNGVfeVQATSgdTHLGGEDFDYKIvrqlI 287
Cdd:cd10225 114 AEHAGAREVYLIEEPMAAAIGAGLPIEEPRGSMVV-DIGGGTTEIAVISL-GGI--VTSRS--VRVAGDEMDEAI----I 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 288 KAFKKKHGIDVSDnnkalaklkREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAkfEELNLDLFKKTLKP------ 361
Cdd:cd10225 184 NYVRRKYNLLIGE---------RTAERIKIEIGSAYPLDEELSMEVRGRDLVTGLPRT--IEITSEEVREALEEpvnaiv 252
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 362 --VEKVLQDSGLE-KKDVDD--IVLVGGSTRIPKVQQLLESYFdgkkaskGI------NPDEAVAYGAAV 420
Cdd:cd10225 253 eaVRSTLERTPPElAADIVDrgIVLTGGGALLRGLDELLREET-------GLpvhvadDPLTCVAKGAGK 315
|
|
| MreB |
COG1077 |
Cell shape-determining ATPase MreB, actin-like superfamily [Cell cycle control, cell division, ... |
53-419 |
2.28e-15 |
|
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: 77.81 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGkteILANEqgnritPSYVAFTDDER---LIGDAAKNQVAANPQNTI------------FDIk 117
Cdd:COG1077 10 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAIDKKTGkvlAVGEEAKEMLGRTPGNIVairplkdgviadFEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 118 rliglkyndrsVQKDIKHLpfnvVNKdgkpavevsVKGEKKVFTPeeisgmilgkmkqiaedylgtkvtHAVVTVPAYFN 197
Cdd:COG1077 80 -----------TEAMLKYF----IKK---------VHGRRSFFRP------------------------RVVICVPSGIT 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 198 DAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVyDLGGGTFDVSLLSIeNGVfeVQATSgdTHLGGED 277
Cdd:COG1077 112 EVERRAVRDAAEQAGAREVYLIEEPMAAAIGAGLPIEEPTGNMVV-DIGGGTTEVAVISL-GGI--VVSRS--IRVAGDE 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 278 FDYKIVRQLikafKKKHGIDVSDnnkalaklkREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKfeELNLDLFKK 357
Cdd:COG1077 186 LDEAIIQYV----RKKYNLLIGE---------RTAEEIKIEIGSAYPLEEELTMEVRGRDLVTGLPKTI--TITSEEIRE 250
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121575 358 TL-KPVEKVLQ--DSGLEK------KDVDD--IVLVGGSTRIPKVQQLLESYFdgkkaskGI------NPDEAVAYGAA 419
Cdd:COG1077 251 ALeEPLNAIVEaiKSVLEKtppelaADIVDrgIVLTGGGALLRGLDKLLSEET-------GLpvhvaeDPLTCVARGTG 322
|
|
| PRK11678 |
PRK11678 |
putative chaperone; Provisional |
53-395 |
1.71e-13 |
|
putative chaperone; Provisional
Pssm-ID: 236954 [Multi-domain] Cd Length: 450 Bit Score: 72.97 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDE-------RLIGDAAKNQVAANPQNTIFDIKRLIGLKYN 125
Cdd:PRK11678 3 IGFDYGTANCSVAVMRDGKPRLLPLENDSTYLPSTLCAPTREavsewlyRHLDVPAYDDERQALLRRAIRYNREEDIDVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 126 DRSVQkdikhlpFnvvnkdGKPAVEVSVKGEKKVF--------------TPEEIS-------GMILgKMKQIAEDYLGTK 184
Cdd:PRK11678 83 AQSVF-------F------GLAALAQYLEDPEEVYfvkspksflgasglKPQQVAlfedlvcAMML-HIKQQAEAQLQAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 185 VTHAVVTVPAYFN-----DAQRQAT---KDAGTIAGLNVLRIVNEPTAAaiayGLD---KSDKEHQIIVYDLGGGTFDVS 253
Cdd:PRK11678 149 ITQAVIGRPVNFQglggeEANRQAEgilERAAKRAGFKDVEFQFEPVAA----GLDfeaTLTEEKRVLVVDIGGGTTDCS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 254 LLSI----------ENGVFevqATSGdTHLGGEDFD-YKIVRQLIKAF----KKKHGI--------------DVS----- 299
Cdd:PRK11678 225 MLLMgpswrgradrSASLL---GHSG-QRIGGNDLDiALAFKQLMPLLgmgsETEKGIalpslpfwnavainDVPaqsdf 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 300 ---DNNKALAKLKRE-------------------------AEKAKRALSSQMSTRIEIDSFVDGidLSETLTRAKFEELN 351
Cdd:PRK11678 301 yslANGRLLNDLIRDarepekvarllkvwrqrlsyrlvrsAEEAKIALSDQAETRASLDFISDG--LATEISQQGLEEAI 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 121575 352 LDLFKKTLKPVEKVLQDSGlEKKDVddIVLVGGSTRIP----KVQQLL 395
Cdd:PRK11678 379 SQPLARILELVQLALDQAQ-VKPDV--IYLTGGSARSPliraALAQQL 423
|
|
| PRK13930 |
PRK13930 |
rod shape-determining protein MreB; Provisional |
53-419 |
2.09e-10 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237564 [Multi-domain] Cd Length: 335 Bit Score: 62.84 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGkteILANEqgnritPSYVAF-TDDERL--IGDAAKNQVAANPQNtIFDIKRLiglkyndrsv 129
Cdd:PRK13930 11 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAIdTKTGKVlaVGEEAKEMLGRTPGN-IEAIRPL---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 130 qkdikhlpfnvvnKDGKPA-VEVSVKgekkvftpeeisgMILGKMKQIAEDYLGTKVtHAVVTVPAYFNDAQRQATKDAG 208
Cdd:PRK13930 71 -------------KDGVIAdFEATEA-------------MLRYFIKKARGRRFFRKP-RIVICVPSGITEVERRAVREAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 209 TIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVyDLGGGTFDVSLLSIeNGVfevqATSGDTHLGGEDFDYKIVRQLik 288
Cdd:PRK13930 124 EHAGAREVYLIEEPMAAAIGAGLPVTEPVGNMVV-DIGGGTTEVAVISL-GGI----VYSESIRVAGDEMDEAIVQYV-- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 289 afKKKHGIDVSDnnkalaklkREAEKAKR----ALSSQMSTRIEidsfVDGIDLSETLtrAKFEELNLDLFKKTLK-PVE 363
Cdd:PRK13930 196 --RRKYNLLIGE---------RTAEEIKIeigsAYPLDEEESME----VRGRDLVTGL--PKTIEISSEEVREALAePLQ 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121575 364 KVLQ--DSGLEK------KDVDD--IVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGAA 419
Cdd:PRK13930 259 QIVEavKSVLEKtppelaADIIDrgIVLTGGGALLRGLDKLLSEET-GLPVHIAEDPLTCVARGTG 323
|
|
| MreB_Mbl |
pfam06723 |
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two ... |
53-418 |
1.96e-09 |
|
MreB/Mbl protein; This family consists of bacterial MreB and Mbl proteins as well as two related archaeal sequences. MreB is known to be a rod shape-determining protein in bacteria and goes to make up the bacterial cytoskeleton. Genes coding for MreB/Mbl are only found in elongated bacteria, not in coccoid forms. It has been speculated that constituents of the eukaryotic cytoskeleton (tubulin, actin) may have evolved from prokaryotic precursor proteins closely related to today's bacterial proteins FtsZ and MreB/Mbl.
Pssm-ID: 399596 [Multi-domain] Cd Length: 327 Bit Score: 59.49 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 53 IGIDLGTTYSCVAVMKNGkteILANEqgnritPSYVAF-TDDERLI--GDAAKNQVAANPQN----------TIFDIkrl 119
Cdd:pfam06723 4 IGIDLGTANTLVYVKGKG---IVLNE------PSVVAInTKTKKVLavGNEAKKMLGRTPGNivavrplkdgVIADF--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 120 iglkyndRSVQKDIKHLPFNVVNKDGKPAVEVsvkgekkvftpeeisgmilgkmkqiaedylgtkvthaVVTVPAYFNDA 199
Cdd:pfam06723 72 -------EVTEAMLKYFIKKVHGRRSFSKPRV-------------------------------------VICVPSGITEV 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 200 QRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVyDLGGGTFDVSLLSIENGVfevqaTSGDTHLGGEDFD 279
Cdd:pfam06723 108 ERRAVKEAAKNAGAREVFLIEEPMAAAIGAGLPVEEPTGNMVV-DIGGGTTEVAVISLGGIV-----TSKSVRVAGDEFD 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 280 YKIvrqlIKAFKKKHGIDVSDnnkalaklkREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRaKFEELNLDLFKKTL 359
Cdd:pfam06723 182 EAI----IKYIRKKYNLLIGE---------RTAERIKIEIGSAYPTEEEEKMEIRGRDLVTGLPK-TIEISSEEVREALK 247
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 121575 360 KPVEKVLQDSG--LEK------KDVDD--IVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYGA 418
Cdd:pfam06723 248 EPVSAIVEAVKevLEKtppelaADIVDrgIVLTGGGALLRGLDKLLSDET-GLPVHIAEDPLTCVALGT 315
|
|
| PRK13928 |
PRK13928 |
rod shape-determining protein Mbl; Provisional |
48-296 |
2.90e-08 |
|
rod shape-determining protein Mbl; Provisional
Pssm-ID: 237563 [Multi-domain] Cd Length: 336 Bit Score: 56.06 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 48 NYGTVIGIDLGTtySCVAVMKNGKTEILaNEqgnritPSYVAFTDDERLI---GDAAKNQVAANPQNtIFDIKRLIGLKY 124
Cdd:PRK13928 1 MFGRDIGIDLGT--ANVLVYVKGKGIVL-NE------PSVVAIDKNTNKVlavGEEARRMVGRTPGN-IVAIRPLRDGVI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 125 NDRSV-QKDIKHLpfnvVNKdgkpavevsVKGEKKVFTPeeisgmilgkmkqiaedylgtKVthaVVTVPAYFNDAQRQA 203
Cdd:PRK13928 71 ADYDVtEKMLKYF----INK---------ACGKRFFSKP---------------------RI---MICIPTGITSVEKRA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 204 TKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVyDLGGGTFDVSLLSIENGVfevqaTSGDTHLGGEDFDYKIV 283
Cdd:PRK13928 114 VREAAEQAGAKKVYLIEEPLAAAIGAGLDISQPSGNMVV-DIGGGTTDIAVLSLGGIV-----TSSSIKVAGDKFDEAII 187
|
250
....*....|...
gi 121575 284 RQLikafKKKHGI 296
Cdd:PRK13928 188 RYI----RKKYKL 196
|
|
| PRK15080 |
PRK15080 |
ethanolamine utilization protein EutJ; Provisional |
169-410 |
8.49e-08 |
|
ethanolamine utilization protein EutJ; Provisional
Pssm-ID: 237904 [Multi-domain] Cd Length: 267 Bit Score: 54.07 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 169 ILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSdkehqiIVYDLGGG 248
Cdd:PRK15080 72 IVRRLKATLEEKLGRELTHAATAIPPGTSEGDPRAIINVVESAGLEVTHVLDEPTAAAAVLGIDNG------AVVDIGGG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 249 TFDVSLLsiENG--VFEVQATSGDTHLggedfdykivrQLIKAfkKKHGIDVSDNNkalaKLKREAEKAKRALSsqmstr 326
Cdd:PRK15080 146 TTGISIL--KDGkvVYSADEPTGGTHM-----------SLVLA--GAYGISFEEAE----QYKRDPKHHKEIFP------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 327 ieidsfvdgidlsetltrakfeelnldlfkkTLKPV-EKV--LQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKK 403
Cdd:PRK15080 201 -------------------------------VVKPVvEKMasIVARHIEGQDVEDIYLVGGTCCLPGFEEVFEKQT-GLP 248
|
....*..
gi 121575 404 ASKGINP 410
Cdd:PRK15080 249 VHKPQHP 255
|
|
| ASKHA_NBD_EutJ |
cd24047 |
nucleotide-binding domain (NBD) of ethanolamine utilization protein EutJ and similar proteins; ... |
169-410 |
8.53e-08 |
|
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: 53.81 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 169 ILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSdkehqiIVYDLGGG 248
Cdd:cd24047 48 IVRKLKETLEKKLGVELTSAATAFPPGTGERDARAIRNVLEGAGLEVSNVVDEPTAANAVLGIRDG------AVVDIGGG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 249 TFDVSLLSIENGVFEVQATSGDTHLggedfdykivrQLIKAfkKKHGIDVSdnnkalaklkrEAEKAKRalssqmstrie 328
Cdd:cd24047 122 TTGIAVLKDGKVVYTADEPTGGTHL-----------SLVLA--GNYGISFE-----------EAEIIKR----------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 329 idsfvdgidlsetlTRAKFEELnldlfKKTLKPV-EKV--LQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFdGKKAS 405
Cdd:cd24047 167 --------------DPARHKEL-----LPVVRPViEKMasIVKRHIKGYKVKDLYLVGGTCCLPGIEEVFEKET-GLPVY 226
|
....*
gi 121575 406 KGINP 410
Cdd:cd24047 227 KPSNP 231
|
|
| ASKHA_NBD_HSP70_HSPA12A |
cd11735 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar ... |
179-402 |
2.21e-07 |
|
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12A (HSPA12A) and similar proteins; HSPA12A is an adapter protein for SORL1, but not SORT1. It delays SORL1 internalization and affects SORL1 subcellular localization. HSPA12A belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). No co-chaperones have yet been identified for HSPA12A.
Pssm-ID: 466841 [Multi-domain] Cd Length: 413 Bit Score: 53.86 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 179 DYLGTKVTHA----VVTVPAYFNDAQRQATKDAGTIAGLNV------LRIVNEPTAAAIAYgldKSDKEHQI---IVYDL 245
Cdd:cd11735 130 DQAGSEFDNSdvrwVITVPAIWKQPAKQFMRQAAYKAGLASpenpeqLIIALEPEAASIYC---RKLRLHQMdryVVVDC 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 246 GGGTFDVSLLSI---ENGVFEVQATSGDTHlGGEDFDYKIVRQLIKAFkkkhGIDVSDNnkalAKLKREA---------E 313
Cdd:cd11735 207 GGGTVDLTVHQIrlpEGHLKELYKASGGPY-GSLGVDYEFEKLLCKIF----GEDFIDQ----FKIKRPAawvdlmiafE 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 314 KAKRALSSQMSTRIEID---SFVD-----------------GIDL----SETLTRAKFEELNlDLFKKTLKPVEKVLQDS 369
Cdd:cd11735 278 SRKRAAAPDRTNPLNITlpfSFIDyykkfrghsvehalrksNVDFvkwsSQGMLRMSPDAMN-ALFKPTIDHIIQHLTDL 356
|
250 260 270
....*....|....*....|....*....|....*.
gi 121575 370 gLEKKDVDDI---VLVGGSTRIPKVQQLLESYFDGK 402
Cdd:cd11735 357 -FQKPEVSGVkflFLVGGFAESPLLQQAVQNAFGDQ 391
|
|
| ASKHA_NBD_HSP70_HSPA12B |
cd11736 |
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 12B (HSPA12B) and similar ... |
189-399 |
7.55e-06 |
|
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: 48.81 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 189 VVTVPAYFNDAQRQATKDAGTIAGL------NVLRIVNEPTAAAIAygldkSDKEHQIIVYDLGGGTFDVSLLSIE--NG 260
Cdd:cd11736 144 VLTVPAIWKQPAKQFMREAAYLAGLvspenpEQLLIALEPEAASIY-----CRKLDRYIVADCGGGTVDLTVHQIEqpQG 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 261 VF-EVQATSGD---------------THLGGEDFdykivrqlIKAFKKKHgidvsdnNKALAKLKREAEKAKRALSSQMS 324
Cdd:cd11736 219 TLkELYKASGGpygavgvdlafekllCQIFGEDF--------IATFKAKR-------PAAWVDLTIAFEARKRTAALRMS 283
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 121575 325 TrieidsfvdgidlsetltrakfEELNlDLFKKTLKPVEKVLQDSgLEKKDVDDI---VLVGGSTRIPKVQQLLESYF 399
Cdd:cd11736 284 S----------------------EAMN-ELFQPTISQIIQHIDDL-MKKPEVKGIkflFLVGGFAESPMLQRAVQAAF 337
|
|
| ASKHA_NBD_FtsA |
cd24048 |
nucleotide-binding domain (NBD) of cell division protein FtsA and similar proteins; FtsA is an ... |
211-425 |
2.07e-05 |
|
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: 47.14 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 211 AGLNVLRIVNEPTAAAIAYgLDKSDKEHQIIVYDLGGGTFDVSLLsiENGVFEvqatsgDTH---LGGEDFDYKIVRQLi 287
Cdd:cd24048 172 AGLEVDDIVLSPLASAEAV-LTEDEKELGVALIDIGGGTTDIAVF--KNGSLR------YTAvipVGGNHITNDIAIGL- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 288 kafkkkhGIDVSdnnkalaklkrEAEKAKR----ALSSQMSTRIEIDSFVDGIDLSETLTR--------AKFEELnLDLf 355
Cdd:cd24048 242 -------NTPFE-----------EAERLKIkygsALSEEADEDEIIEIPGVGGREPREVSRrelaeiieARVEEI-LEL- 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 121575 356 kktlkpVEKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFD-----GKKASKGINPDEAVAYGAAVQAGVL 425
Cdd:cd24048 302 ------VKKELKESGYEDLLPGGIVLTGGGSQLPGLVELAEEVFGmpvriGRPKNIGGLPEEVNDPAYATAVGLL 370
|
|
| PRK13929 |
PRK13929 |
rod-share determining protein MreBH; Provisional |
51-417 |
6.11e-05 |
|
rod-share determining protein MreBH; Provisional
Pssm-ID: 184403 [Multi-domain] Cd Length: 335 Bit Score: 45.67 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 51 TVIGIDLGTTYSCVAVMKNGkteILANEqgnritPSYVAF---TDDERLIGDAAKNQVAANPQNtIFDIKRLiglkyndr 127
Cdd:PRK13929 5 TEIGIDLGTANILVYSKNKG---IILNE------PSVVAVdteTKAVLAIGTEAKNMIGKTPGK-IVAVRPM-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 128 svqkdikhlpfnvvnKDGkpavevsvkgekkVFTPEEISGMILGKMKQIAEDYLGTKV--THAVVTVPAYFNDAQRQATK 205
Cdd:PRK13929 67 ---------------KDG-------------VIADYDMTTDLLKQIMKKAGKNIGMTFrkPNVVVCTPSGSTAVERRAIS 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 206 DAGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVyDLGGGTFDVSLLSIeNGVfevqATSGDTHLGGEDFDYKIVRQ 285
Cdd:PRK13929 119 DAVKNCGAKNVHLIEEPVAAAIGADLPVDEPVANVVV-DIGGGTTEVAIISF-GGV----VSCHSIRIGGDQLDEDIVSF 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 286 LikafKKKHGIDVSDnnkalaklkREAEKAK----RALSSQMSTRIEI--DSFVDGIDLSETLTRAKFEELNLDLFKKTL 359
Cdd:PRK13929 193 V----RKKYNLLIGE---------RTAEQVKmeigYALIEHEPETMEVrgRDLVTGLPKTITLESKEIQGAMRESLLHIL 259
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 121575 360 KPVEKVLQDSGLE-KKDVDD--IVLVGGSTRIPKVQQLLESYFdGKKASKGINPDEAVAYG 417
Cdd:PRK13929 260 EAIRATLEDCPPElSGDIVDrgVILTGGGALLNGIKEWLSEEI-VVPVHVAANPLESVAIG 319
|
|
| PRK13927 |
PRK13927 |
rod shape-determining protein MreB; Provisional |
189-344 |
7.88e-05 |
|
rod shape-determining protein MreB; Provisional
Pssm-ID: 237562 [Multi-domain] Cd Length: 334 Bit Score: 45.47 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 189 VVTVPAYFNDAQRQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVyDLGGGTFDVSLLSIeNGVfevqATS 268
Cdd:PRK13927 100 VICVPSGITEVERRAVRESALGAGAREVYLIEEPMAAAIGAGLPVTEPTGSMVV-DIGGGTTEVAVISL-GGI----VYS 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 121575 269 GDTHLGGEDFDYKIvrqlIKAFKKKHGIDVSDnnkalaklkREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTR 344
Cdd:PRK13927 174 KSVRVGGDKFDEAI----INYVRRNYNLLIGE---------RTAERIKIEIGSAYPGDEVLEMEVRGRDLVTGLPK 236
|
|
| ASKHA_NBD_PilM-like |
cd24004 |
nucleotide-binding domain (NBD) of the PilM-like domain family; The PilM-like family includes ... |
155-400 |
1.14e-04 |
|
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: 44.59 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 155 GEKKVFTPEEISgMILGKMKQIAEDYLGTKVTHAVVTVP----AYFNDAQRqatkdagtiAGLNVLRIVNEPTAAA---I 227
Cdd:cd24004 38 GDGQIHDISKVA-ESIKELLKELEEKLGSKLKDVVIAIAkvveSLLNVLEK---------AGLEPVGLTLEPFAAAnllI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 228 AYGLDKSDkehqIIVYDLGGGTFDVSLlsIENGVFEvqaTSGDTHLGGEDFDYKIVRQLIKAFKkkhgidvsdnnkalak 307
Cdd:cd24004 108 PYDMRDLN----IALVDIGAGTTDIAL--IRNGGIE---AYRMVPLGGDDFTKAIAEGFLISFE---------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 121575 308 lkrEAEKAKRALSSQMSTRI--EIDSFVDGIDLSETLTRAkFEELNLDLFKKtlkpVEKVLQDSGLEKKdvddIVLVGGS 385
Cdd:cd24004 163 ---EAEKIKRTYGIFLLIEAkdQLGFTINKKEVYDIIKPV-LEELASGIANA----IEEYNGKFKLPDA----VYLVGGG 230
|
250
....*....|....*
gi 121575 386 TRIPKVQQLLESYFD 400
Cdd:cd24004 231 SKLPGLNEALAEKLG 245
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
365-428 |
5.73e-03 |
|
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: 39.82 E-value: 5.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 121575 365 VLQDSGLEkkdVDDIVLVGGSTRIPKVQQLLESYFdGKKASKgINPDEAVAYGAAVQAGVLSGE 428
Cdd:COG1070 388 ALEEAGVK---IDRIRATGGGARSPLWRQILADVL-GRPVEV-PEAEEGGALGAALLAAVGLGL 446
|
|
| |
