|
Name |
Accession |
Description |
Interval |
E-value |
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
6-849 |
0e+00 |
|
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent chaperone ClpB. This protein belongs to the AAA family, ATPases associated with various cellular activities (pfam00004). This molecular chaperone does not act as a protease, but rather serves to disaggregate misfolded and aggregated proteins. [Protein fate, Protein folding and stabilization]
Pssm-ID: 274529 [Multi-domain] Cd Length: 850 Bit Score: 1584.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 6 FTTKFQEALSEAQSLAIGKDNQFIEPVHLLTALLNQQGGSIAPILTASGVNVALLRNELKTELNKLPQVIGNGGDVQLSR 85
Cdd:TIGR03346 1 LTEKFQEALQAAQSLALGRDHQQIEPEHLLKALLDQEGGLARPLLQKAGVNVGALRQALEKELERLPKVSGPGGQVYLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 86 QLINLLNLCDKFAQQNQDKFISSELFLLAALEERGTISDILKKCGAKKEQISQAIQHIRGGQNVNDQNAEESRQALEKYT 165
Cdd:TIGR03346 81 DLNRLLNLAEKLAQKRGDEFISSEHLLLALLDDKGTLGKLLKEAGATADALEAAINAVRGGQKVTDANAEDQYEALEKYA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 166 IDLTARAESGKLDPVIGRDEEIRRAIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGEVPEGLKNKRVLSLDMGAL 245
Cdd:TIGR03346 161 RDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPEGLKNKRLLALDMGAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 246 IAGAKYRGEFEERLKAVLNELSKEEGRVILFIDEIHTMVGAGKTDGAMDAGNLLKPSLARGELHCVGATTLDEYRQYIEK 325
Cdd:TIGR03346 241 IAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLKPALARGELHCIGATTLDEYRKYIEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 326 DAALERRFQKVFVDEPSVEDTIAILRGLKERYEIHHHVDITDPAIVAAATLSHRYISDRQLPDKAIDLIDEAASSIRMEI 405
Cdd:TIGR03346 321 DAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRYITDRFLPDKAIDLIDEAAARIRMEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 406 DSKPEPLDRLERRIIQLKLEQQALQKEEDEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLSGSQHIKQELDTAKTE 485
Cdd:TIGR03346 401 DSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEEQWKAEKASIQGIQQIKEEIEQVRLE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 486 LEQARRAGDLAKMSELQYGRIPALEKQLEQAETSEGKEM-TLLRYRVTDEEIAEVLSKATGIPVSKMMEGEKEKLLRMEE 564
Cdd:TIGR03346 481 LEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGEEQnRLLREEVTAEEIAEVVSRWTGIPVSKMLEGEREKLLHMEE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 565 ELHKRVIGQNEAVDAVANAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKTLAKFLFDSEDAMVRIDMSEFMEKHSVS 644
Cdd:TIGR03346 561 ELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALAEFLFDSEDAMVRIDMSEYMEKHSVA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 645 RLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHADVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDL 724
Cdd:TIGR03346 641 RLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRLTDGQGRTVDFRNTVIIMTSNLGSDF 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 725 IQ-GNKDESYSEMKALVMSVVSQHFRPEFINRIDETVVFHPLGKENIRAIASIQLERLAKRMETRGYELVFTDALLDFIG 803
Cdd:TIGR03346 721 IQeLAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQLGRLRKRLAERKITLELSDAALDFLA 800
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 491878479 804 EVGYDPIYGARPLKRAIQQEIENSLAQQILSGALLPGKVVTIDYAN 849
Cdd:TIGR03346 801 EAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEG 846
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
1-856 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 1511.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 1 MNIEKFTTKFQEALSEAQSLAIGKDNQFIEPVHLLTALLNQQGGSIAPILTASGVNVALLRNELKTELNKLPQVIGNGGD 80
Cdd:PRK10865 1 MRLDRLTNKFQLALADAQSLALGHDNQFIEPLHLMSALLNQEGGSVRPLLTSAGINAGQLRTDINQALSRLPQVEGTGGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 81 VQLSRQLINLLNLCDKFAQQNQDKFISSELFLLAALEERGTISDILKKCGAKKEQISQAIQHIRGGQNVNDQNAEESRQA 160
Cdd:PRK10865 81 VQPSQDLVRVLNLCDKLAQKRGDNFISSELFVLAALESRGTLADILKAAGATTANITQAIEQMRGGESVNDQGAEDQRQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 161 LEKYTIDLTARAESGKLDPVIGRDEEIRRAIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGEVPEGLKNKRVLSL 240
Cdd:PRK10865 161 LKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGLKGRRVLAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 241 DMGALIAGAKYRGEFEERLKAVLNELSKEEGRVILFIDEIHTMVGAGKTDGAMDAGNLLKPSLARGELHCVGATTLDEYR 320
Cdd:PRK10865 241 DMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVGATTLDEYR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 321 QYIEKDAALERRFQKVFVDEPSVEDTIAILRGLKERYEIHHHVDITDPAIVAAATLSHRYISDRQLPDKAIDLIDEAASS 400
Cdd:PRK10865 321 QYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAIDLIDEAASS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 401 IRMEIDSKPEPLDRLERRIIQLKLEQQALQKEEDEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLSGSQHIKQELD 480
Cdd:PRK10865 401 IRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGTQTIKAELE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 481 TAKTELEQARRAGDLAKMSELQYGRIPALEKQLEQAETSEGKEMTLLRYRVTDEEIAEVLSKATGIPVSKMMEGEKEKLL 560
Cdd:PRK10865 481 QAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTMRLLRNKVTDAEIAEVLARWTGIPVSRMLESEREKLL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 561 RMEEELHKRVIGQNEAVDAVANAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKTLAKFLFDSEDAMVRIDMSEFMEK 640
Cdd:PRK10865 561 RMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVRIDMSEFMEK 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHADVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
Cdd:PRK10865 641 HSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNL 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 721 GSDLIQGNKDE-SYSEMKALVMSVVSQHFRPEFINRIDETVVFHPLGKENIRAIASIQLERLAKRMETRGYELVFTDALL 799
Cdd:PRK10865 721 GSDLIQERFGElDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGYEIHISDEAL 800
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 491878479 800 DFIGEVGYDPIYGARPLKRAIQQEIENSLAQQILSGALLPGKVVTIDYANAEVQARQ 856
Cdd:PRK10865 801 KLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRIVAVQ 857
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1-852 |
0e+00 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 1500.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 1 MNIEKFTTKFQEALSEAQSLAIGKDNQFIEPVHLLTALLNQQGGSIAPILTASGVNVALLRNELKTELNKLPQVIGNGGD 80
Cdd:COG0542 1 MNFEKFTEKAQEALEAAQELARRLGHQEVEPEHLLLALLEQGEGLAAKLLRKLGVDLDALREELEEALGRLPKVSGSSGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 81 VQLSRQLINLLNLCDKFAQQNQDKFISSELFLLAALEER-GTISDILKKCGAKKEQISQAIQHIRGGQNVNDQNAEESRQ 159
Cdd:COG0542 81 PYLSPRLKRVLELAELEARKLGDEYISTEHLLLALLREGeGVAARILKKLGITLEALREALEELRGGSRVTSQNPESKTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 160 ALEKYTIDLTARAESGKLDPVIGRDEEIRRAIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGEVPEGLKNKRVLS 239
Cdd:COG0542 161 ALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGDVPESLKDKRVLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 240 LDMGALIAGAKYRGEFEERLKAVLNELSKEEGRVILFIDEIHTMVGAGKTDGAMDAGNLLKPSLARGELHCVGATTLDEY 319
Cdd:COG0542 241 LDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALARGELRCIGATTLDEY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 320 RQYIEKDAALERRFQKVFVDEPSVEDTIAILRGLKERYEIHHHVDITDPAIVAAATLSHRYISDRQLPDKAIDLIDEAAS 399
Cdd:COG0542 321 RKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDRFLPDKAIDLIDEAAA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 400 SIRMEIDSKPEPLDRLERRIIQLKLEQQALQKEEDEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLSGSQHIKQEL 479
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 480 DTakteleqarragdlakmselQYGRIPALEKQLEQAETSEGKEMTLLRYRVTDEEIAEVLSKATGIPVSKMMEGEKEKL 559
Cdd:COG0542 481 EQ--------------------RYGKIPELEKELAELEEELAELAPLLREEVTEEDIAEVVSRWTGIPVGKLLEGEREKL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 560 LRMEEELHKRVIGQNEAVDAVANAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKTLAKFLFDSEDAMVRIDMSEFME 639
Cdd:COG0542 541 LNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLFGDEDALIRIDMSEYME 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 640 KHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHADVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSN 719
Cdd:COG0542 621 KHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRNTIIIMTSN 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 720 LGSDLIQ--GNKDESYSEMKALVMSVVSQHFRPEFINRIDETVVFHPLGKENIRAIASIQLERLAKRMETRGYELVFTDA 797
Cdd:COG0542 701 IGSELILdlAEDEPDYEEMKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRLRKRLAERGITLELTDA 780
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 491878479 798 LLDFIGEVGYDPIYGARPLKRAIQQEIENSLAQQILSGALLPGKVVTIDYANAEV 852
Cdd:COG0542 781 AKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGEL 835
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
3-846 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 856.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 3 IEKFTTKFQEALSEAQSLAIGKDNQFIEPVHLLTALLNQQGGSIAPILTASGVNVALLRNELKtelnklpQVIGNG-GDV 81
Cdd:CHL00095 2 FERFTEKAIKVIMLSQEEARRLGHNFVGTEQILLGLIGEGTGIAARALKSMGVTLKDARIEVE-------KIIGRGtGFV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 82 QLSRQLI----NLLNLCDKFAQQNQDKFISSELFLLAALEER-GTISDILKKCGAK----KEQISQAIQHIRGGQNVNDQ 152
Cdd:CHL00095 75 AVEIPFTprakRVLEMSLEEARDLGHNYIGTEHLLLALLEEGeGVAARVLENLGVDlskiRSLILNLIGEIIEAILGAEQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 153 NaEESRQALEKYTIDLTARAESGKLDPVIGRDEEIRRAIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGEVPEGL 232
Cdd:CHL00095 155 S-RSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVPDIL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 233 KNKRVLSLDMGALIAGAKYRGEFEERLKAVLNELsKEEGRVILFIDEIHTMVGAGKTDGAMDAGNLLKPSLARGELHCVG 312
Cdd:CHL00095 234 EDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEI-QENNNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQCIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 313 ATTLDEYRQYIEKDAALERRFQKVFVDEPSVEDTIAILRGLKERYEIHHHVDITDPAIVAAATLSHRYISDRQLPDKAID 392
Cdd:CHL00095 313 ATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDKAID 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 393 LIDEAASSIRMEIDSKPEPLDRLERriiqlklEQQALQKEEDEASRKRLEMLEKELAEKEREYaeleevwksekatlsgS 472
Cdd:CHL00095 393 LLDEAGSRVRLINSRLPPAARELDK-------ELREILKDKDEAIREQDFETAKQLRDREMEV----------------R 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 473 QHIKQELDTAKTEleqarragdlakmselqygripalekqleqaetsegKEMTLLRYRVTDEEIAEVLSKATGIPVSKMM 552
Cdd:CHL00095 450 AQIAAIIQSKKTE------------------------------------EEKRLEVPVVTEEDIAEIVSAWTGIPVNKLT 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 553 EGEKEKLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKTLAKFLFDSEDAMVRI 632
Cdd:CHL00095 494 KSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDAMIRL 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 633 DMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHADVFNILLQVLDDGRLTDGQGRTVDFRNT 712
Cdd:CHL00095 574 DMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTIDFKNT 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 713 VVIMTSNLGSDLIQ-------------GNKDESYSEMKALVMSVVSQHFRPEFINRIDETVVFHPLGKENIRAIASIQLE 779
Cdd:CHL00095 654 LIIMTSNLGSKVIEtnsgglgfelsenQLSEKQYKRLSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAEIMLK 733
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491878479 780 RLAKRMETRGYELVFTDALLDFIGEVGYDPIYGARPLKRAIQQEIENSLAQQILSGALLPGKVVTID 846
Cdd:CHL00095 734 NLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVD 800
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
12-844 |
0e+00 |
|
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, an ATPase associated with chaperone-related functions. These ClpB homologs, designated ClpV1, are a key component of the bacterial pathogenicity-associated type VI secretion system. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274528 [Multi-domain] Cd Length: 852 Bit Score: 795.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 12 EALSEAQSLAIGKDNQFIEPVHLLTALLNQQGGSIAPILTASGVNVALLRNELKTELNKLPqvIGNGGDVQLSRQLINLL 91
Cdd:TIGR03345 7 RALEQAAALCVARGHPEVELEHWLLALLDQPDSDLAAILRHFGVDLGRLKADLARALDKLP--RGNTRTPVFSPHLVELL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 92 NLCDKFAQ-QNQDKFISSELFLLAALEER------GTISDILKKCGAkkEQISQAIQHIRGGQN-----------VNDQN 153
Cdd:TIGR03345 85 QEAWLLASlELGDGRIRSGHLLLALLTDPelrrllGSISPELAKIDR--EALREALPALVEGSAeasaaaadaapAGAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 154 AEESRQALEKYTIDLTARAESGKLDPVIGRDEEIRRAIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGEVPEGLK 233
Cdd:TIGR03345 163 GAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPALR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 234 NKRVLSLDMGALIAGAKYRGEFEERLKAVLNELSKEEGRVILFIDEIHTMVGAGKTDGAMDAGNLLKPSLARGELHCVGA 313
Cdd:TIGR03345 243 NVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRTIAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 314 TTLDEYRQYIEKDAALERRFQKVFVDEPSVEDTIAILRGLKERYEIHHHVDITDPAIVAAATLSHRYISDRQLPDKAIDL 393
Cdd:TIGR03345 323 TTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAVSL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 394 IDEAASSIRMEIDSKPEPLDRLERRIIQLKLEQQALQKEE--DEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLSG 471
Cdd:TIGR03345 403 LDTACARVALSQNATPAALEDLRRRIAALELELDALEREAalGADHDERLAELRAELAALEAELAALEARWQQEKELVEA 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 472 SQHIKQELDTAktelEQARRAGDLAKMSELQygripALEKQLEQAETsegkEMTLLRYRVTDEEIAEVLSKATGIPVSKM 551
Cdd:TIGR03345 483 ILALRAELEAD----ADAPADDDDALRAQLA-----ELEAALASAQG----EEPLVFPEVDAQAVAEVVADWTGIPVGRM 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 552 MEGEKEKLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKTLAKFLFDSEDAMVR 631
Cdd:TIGR03345 550 VRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQNLIT 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 632 IDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHADVFNILLQVLDDGRLTDGQGRTVDFRN 711
Cdd:TIGR03345 630 INMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREIDFKN 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 712 TVVIMTSNLGSDLI-----QGNKDESYSEMKALVMSVVSQHFRPEFINRIdeTVV-FHPLGKENIRAIASIQLERLAKRM 785
Cdd:TIGR03345 710 TVILLTSNAGSDLImalcaDPETAPDPEALLEALRPELLKVFKPAFLGRM--TVIpYLPLDDDVLAAIVRLKLDRIARRL 787
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 786 ETR-GYELVFTDALLDFIGEVGYDPIYGARPLKRAIQQEIENSLAQQILSgALLPGKVVT 844
Cdd:TIGR03345 788 KENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILE-RLAAGEPIE 846
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
6-846 |
0e+00 |
|
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 274241 [Multi-domain] Cd Length: 730 Bit Score: 745.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 6 FTTKFQEALSEAQSLAIGKDNQFIEPVHLLTALLNQQGGsiAPILTASGVNVALLRNELKTELNKLPQVIGNGGDVQlSR 85
Cdd:TIGR02639 1 ISEELERILSDALEEAKERRHEFVTLEHLLLALLDDNEA--IEILEECGGDVELLRKRLEDYLEENLPVIPEDIDEE-PE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 86 QLINLLNLCDKFAQ--QNQDKFISSELFLLAAL--EERGTISDILKKCGAKKEQISQAIQHIRGGQNVNDQNA------E 155
Cdd:TIGR02639 78 QTVGVQRVIQRALLhvKSAGKKEIDIGDLLVALfdEEDSHASYFLKSQGITRLDILNYISHGISKDDGKDQLGeeagkeE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 156 ESRQ-ALEKYTIDLTARAESGKLDPVIGRDEEIRRAIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGEVPEGLKN 234
Cdd:TIGR02639 158 EKGQdALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKVPERLKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 235 KRVLSLDMGALIAGAKYRGEFEERLKAVLNELSKEEGRvILFIDEIHTMVGAGKT-DGAMDAGNLLKPSLARGELHCVGA 313
Cdd:TIGR02639 238 AKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNA-ILFIDEIHTIVGAGATsGGSMDASNLLKPALSSGKIRCIGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 314 TTLDEYRQYIEKDAALERRFQKVFVDEPSVEDTIAILRGLKERYEIHHHVDITDPAIVAAATLSHRYISDRQLPDKAIDL 393
Cdd:TIGR02639 317 TTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLPDKAIDV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 394 IDEAASSIRMEIDSKPepldrlerriiqlkleqqalqkeedeasrkrlemlekelaekereyaeleevwksekatlsgsq 473
Cdd:TIGR02639 397 IDEAGAAFRLRPKAKK---------------------------------------------------------------- 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 474 hikqeldtakteleqarragdlakmselqygripalekqleqaetsegkemtllRYRVTDEEIAEVLSKATGIPVSKMME 553
Cdd:TIGR02639 413 ------------------------------------------------------KANVNVKDIENVVAKMAKIPVKTVSS 438
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 554 GEKEKLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKTLAKFLfdsEDAMVRID 633
Cdd:TIGR02639 439 DDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---GVHLLRFD 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 634 MSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHADVFNILLQVLDDGRLTDGQGRTVDFRNTV 713
Cdd:TIGR02639 516 MSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRKADFRNVI 595
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 714 VIMTSNLGSDLIQ------GNKDESYSEMKAlvmsvVSQHFRPEFINRIDETVVFHPLGKENIRAIASIQLERLAKRMET 787
Cdd:TIGR02639 596 LIMTSNAGASEMSkppigfGGENRESKSLKA-----IKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQLNE 670
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 491878479 788 RGYELVFTDALLDFIGEVGYDPIYGARPLKRAIQQEIENSLAQQILSGALLPGKVVTID 846
Cdd:TIGR02639 671 KNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKIS 729
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
13-853 |
9.40e-180 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 536.34 E-value: 9.40e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 13 ALSEAQSLAIGKDNQFIEPVHLLTALLNQQGGSIApiLTASGVNVALLRNELKTELNKLPQVIGNGGDVQLSRQLINLLN 92
Cdd:PRK11034 9 SLNMAFARAREHRHEFMTVEHLLLALLSNPSAREA--LEACSVDLVALRQELEAFIEQTTPVLPASEEERDTQPTLSFQR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 93 LCDK--FAQQNQDKFISSELFLLAAL--EERGTISDILKKCGAKKEQISQAIQH-------IRGGQNVNDQNAEE---SR 158
Cdd:PRK11034 87 VLQRavFHVQSSGRSEVTGANVLVAIfsEQESQAAYLLRKHEVSRLDVVNFISHgtrkdepSQSSDPGSQPNSEEqagGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 159 QALEKYTIDLTARAESGKLDPVIGRDEEIRRAIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNGEVPEGLKNKRVL 238
Cdd:PRK11034 167 ERMENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 239 SLDMGALIAGAKYRGEFEERLKAVLNELSKEEgRVILFIDEIHTMVGAGKTDGA-MDAGNLLKPSLARGELHCVGATTLD 317
Cdd:PRK11034 247 SLDIGSLLAGTKYRGDFEKRFKALLKQLEQDT-NSILFIDEIHTIIGAGAASGGqVDAANLIKPLLSSGKIRVIGSTTYQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 318 EYRQYIEKDAALERRFQKVFVDEPSVEDTIAILRGLKERYEIHHHVDITDPAIVAAATLSHRYISDRQLPDKAIDLIDEA 397
Cdd:PRK11034 326 EFSNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 398 ASSIRMEidskpepldrlerriiqlkleqqalqkeedEASRKRlemlekelaeKEREYAELEEVwksekatlsgsqhikq 477
Cdd:PRK11034 406 GARARLM------------------------------PVSKRK----------KTVNVADIESV---------------- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 478 eldtakteleqarragdLAKMSelqygRIPalEKQLEQAetsegkemtllryrvtdeeiaevlskatgipvskmmegEKE 557
Cdd:PRK11034 430 -----------------VARIA-----RIP--EKSVSQS--------------------------------------DRD 447
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 558 KLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKTLAKFLfDSEdaMVRIDMSEF 637
Cdd:PRK11034 448 TLKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL-GIE--LLRFDMSEY 524
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 638 MEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHADVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMT 717
Cdd:PRK11034 525 MERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMT 604
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 718 SNLGS--------DLIQgnKDESYSemkalVMSVVSQHFRPEFINRIDETVVFHPLGKENIRAIASIQLERLAKRMETRG 789
Cdd:PRK11034 605 TNAGVreterksiGLIH--QDNSTD-----AMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKG 677
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491878479 790 YELVFTDALLDFIGEVGYDPIYGARPLKRAIQQEIENSLAQQILSGALLPGKVVTIDYANAEVQ 853
Cdd:PRK11034 678 VSLEVSQEARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNE 741
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
558-762 |
7.14e-112 |
|
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410907 [Multi-domain] Cd Length: 178 Bit Score: 339.15 E-value: 7.14e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 558 KLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKTLAKFLFDSEDAMVRIDMSEF 637
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 638 MEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHADVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMT 717
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491878479 718 SNlgsdliqgnkdesysemkalvmsvvsqHFRPEFINRIDETVVF 762
Cdd:cd19499 161 SN---------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
596-759 |
3.63e-94 |
|
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400187 [Multi-domain] Cd Length: 168 Bit Score: 292.56 E-value: 3.63e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 596 RPIGSFLFLGPTGVGKTELCKTLAKFLFDSEDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVIL 675
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 676 LDEVEKAHADVFNILLQVLDDGRLTDGQGRTVDFRNTVVIMTSNLGSDLIQGNK----DESYSEMKALVMSVVSQHFRPE 751
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKISDASrlgdSPDYELLKEEVMDLLKKGFIPE 160
|
....*...
gi 491878479 752 FINRIDET 759
Cdd:pfam07724 161 FLGRLPII 168
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
342-445 |
5.47e-47 |
|
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.
Pssm-ID: 465544 [Multi-domain] Cd Length: 104 Bit Score: 162.66 E-value: 5.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 342 SVEDTIAILRGLKERYEIHHHVDITDPAIVAAATLSHRYISDRQLPDKAIDLIDEAASSIRMEIDSKPEPLDRLERRIIQ 421
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 491878479 422 LKLEQQALQKEEDEASRKRLEMLE 445
Cdd:pfam17871 81 LEIEKEALEREQDFEKAERLAKLE 104
|
|
| ClpB_D2-small |
pfam10431 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
765-845 |
1.13e-28 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA, pfam00004) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerization, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilize the functional assembly. The domain is associated with two Clp_N, pfam02861, at the N-terminus as well as AAA, pfam00004 and AAA_2, pfam07724.
Pssm-ID: 463090 [Multi-domain] Cd Length: 81 Bit Score: 109.42 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 765 LGKENIRAIASIQLERLAKRMETRGYELVFTDALLDFIGEVGYDPIYGARPLKRAIQQEIENSLAQQILSGALLPGKVVT 844
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 491878479 845 I 845
Cdd:pfam10431 81 V 81
|
|
| ClpB_D2-small |
smart01086 |
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, ... |
765-853 |
8.25e-27 |
|
C-terminal, D2-small domain, of ClpB protein; This is the C-terminal domain of ClpB protein, referred to as the D2-small domain, and is a mixed alpha-beta structure. Compared with the D1-small domain (included in AAA) it lacks the long coiled-coil insertion, and instead of helix C4 contains a beta-strand (e3) that is part of a three stranded beta-pleated sheet. In Thermophilus the whole protein forms a hexamer with the D1-small and D2-small domains located on the outside of the hexamer, with the long coiled-coil being exposed on the surface. The D2-small domain is essential for oligomerisation, forming a tight interface with the D2-large domain of a neighbouring subunit and thereby providing enough binding energy to stabilise the functional assembly. The domain is associated with two Clp_N at the N-terminus as well as AAA and AAA_2.
Pssm-ID: 198154 [Multi-domain] Cd Length: 90 Bit Score: 104.45 E-value: 8.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 765 LGKENIRAIASIQLERLAKRMETRGYELVFTDALLDFIGEVGYDPIYGARPLKRAIQQEIENSLAQQILSGALLPGKVVT 844
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
....*....
gi 491878479 845 IDYANAEVQ 853
Cdd:smart01086 81 VDVDDGELV 89
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
181-341 |
8.93e-23 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 95.29 E-value: 8.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 181 IGRDEEIRRAIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNgevpeglKNKRVLSLDMGALIAGAKYRGEFEERLK 260
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFR-------PGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 261 AVLNELSKEEGRVILFIDEIHTMvGAGKTDGAMDAGNLLKPSLA-RGELHCVGATTLDEYRQyieKDAALERRFQKVFVD 339
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEIDSL-SRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGD---LDRALYDRLDIRIVI 149
|
..
gi 491878479 340 EP 341
Cdd:cd00009 150 PL 151
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
571-764 |
1.86e-19 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 85.66 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 571 IGQNEAVDAVANAIRRsraglsdpnRPIGSFLFLGPTGVGKTELCKTLAKFLFDSEDAMVRIDMSEFMEKHSVSRLVGAP 650
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 651 PGYVgyeeggyLTEAVRRRPYSVILLDEVEKAHADVFNILLQVLDDGRLTdgqgrTVDFRNTVVIMTSNLGSDLIqgnkd 730
Cdd:cd00009 72 LVRL-------LFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGD----- 134
|
170 180 190
....*....|....*....|....*....|....
gi 491878479 731 esysemkalvmsvvsqhFRPEFINRIDETVVFHP 764
Cdd:cd00009 135 -----------------LDRALYDRLDIRIVIPL 151
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
602-728 |
7.48e-14 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 69.71 E-value: 7.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 602 LFLGPTGVGKTELCKTLAKFLFDSEDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGY----LTEAVRRRPYSVILLD 677
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 491878479 678 EVEKAHADVFNILLQVLDDGRLTDGQGRtvdFRNTVVIMTSNLGSDLIQGN 728
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKS---EKNLTVILTTNDEKDLGPAL 133
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
204-337 |
5.33e-13 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 66.46 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 204 LIGEPGVGKTAIVEGLAQRIvngevpeglkNKRVLSLDMGALIagAKYRGEFEERLKAVLNELsKEEGRVILFIDEIHTM 283
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELV--SKYVGESEKRLRELFEAA-KKLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491878479 284 VGAGKTDGAMDAGNLL--------KPSLARGELHCVGATTldeyrqYIEK-DAALERRFQKVF 337
Cdd:pfam00004 70 AGSRGSGGDSESRRVVnqllteldGFTSSNSKVIVIAATN------RPDKlDPALLGRFDRII 126
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
600-719 |
1.05e-12 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 65.78 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 600 SFLFLGPTGVGKTELCKTLAKFLFDSEDAMVRidMSEFMEKhsvSRLVGA--PPGYVGYEEGGYLTEAVRRRpySVILLD 677
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQ--LTRDTTE---EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAVLD 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 491878479 678 EVEKAHADVFNILLQVLDDGRLTDGQGRT---VDFRNTVVIMTSN 719
Cdd:pfam07728 74 EINRANPDVLNSLLSLLDERRLLLPDGGElvkAAPDGFRLIATMN 118
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
32-404 |
1.24e-10 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 64.16 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 32 VHLLTALLNQQGGSIAPILTASGVNVALLRNELKTELNKLPQVIGNGGDVQLSRQLINLLNLCDKFAQQNQDKFISSELF 111
Cdd:COG0464 11 LALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 112 LLAALEERGTISDILKKCGAKKEQISQAIQHIRGGQNVNDQNAEESRQALEKYTIDLTARAESGKLDPVIGRDE---EIR 188
Cdd:COG0464 91 LLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEvkeELR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 189 RAIQVLQRRTK-------NNP---VLIGEPGVGKTAIVEGLAQRIvngevpeglkNKRVLSLDMGALIagAKYRGEFEER 258
Cdd:COG0464 171 ELVALPLKRPElreeyglPPPrglLLYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLV--SKYVGETEKN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 259 LKAVLNELsKEEGRVILFIDEIHTmvGAGKTDGAMDA------GNLLKpSLA--RGELHCVGATtldeYRqyIEK-DAAL 329
Cdd:COG0464 239 LREVFDKA-RGLAPCVLFIDEADA--LAGKRGEVGDGvgrrvvNTLLT-EMEelRSDVVVIAAT----NR--PDLlDPAL 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491878479 330 ERRFQ-KVFVDEPSVEDTIAILRGLKERYEIHHHVDITDpaiVAAAT--LSHRYIsdRQLPDKAIDL-IDEAASSIRME 404
Cdd:COG0464 309 LRRFDeIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEE---LAEATegLSGADI--RNVVRRAALQaLRLGREPVTTE 382
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
17-69 |
6.54e-10 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 55.22 E-value: 6.54e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 491878479 17 AQSLAIGKDNQFIEPVHLLTALLNQQGGSIAPILTASGVNVALLRNELKTELN 69
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEDDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
575-725 |
8.25e-10 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 58.45 E-value: 8.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 575 EAVDAVANAIRRSRAGLsdpNRPIGsFLFLGPTGVGKTELCKTLAKFLfDSEdaMVRIDMSEFMEKHSvsrlvgappgYV 654
Cdd:cd19481 7 EAVEAPRRGSRLRRYGL---GLPKG-ILLYGPPGTGKTLLAKALAGEL-GLP--LIVVKLSSLLSKYV----------GE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 655 GYEEGGYLTEAVRRRPYSVILLDEVEKA------------HADVFNILLQVLDDGRLTDgqgrtvdfrNTVVIMTSNLGS 722
Cdd:cd19481 70 SEKNLRKIFERARRLAPCILFIDEIDAIgrkrdssgesgeLRRVLNQLLTELDGVNSRS---------KVLVIAATNRPD 140
|
...
gi 491878479 723 DLI 725
Cdd:cd19481 141 LLD 143
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
602-719 |
2.37e-08 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 53.37 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 602 LFLGPTGVGKTELCKTLAKFLFDSedaMVRIDMSEFMEKHsvsrlVGAPPGYVgyeeGGYLTEAVRRRPySVILLDEVEK 681
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAKELGAP---FIEISGSELVSKY-----VGESEKRL----RELFEAAKKLAP-CVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 491878479 682 -----------AHADVFNILLQVLDdgrltdgqGRTVDFRNTVVIMTSN 719
Cdd:pfam00004 69 lagsrgsggdsESRRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
564-681 |
3.75e-08 |
|
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410906 [Multi-domain] Cd Length: 183 Bit Score: 53.92 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 564 EELHKRVIGQNEAVDAVA----NAIRRSR--AGLSDPNRPiGSFLFLGPTGVGKTELCKTLAKFlfdSEDAMVRIDMSEF 637
Cdd:cd19498 7 SELDKYIIGQDEAKRAVAialrNRWRRMQlpEELRDEVTP-KNILMIGPTGVGKTEIARRLAKL---AGAPFIKVEATKF 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 491878479 638 MEKhsvsrlvgappGYVGYEeggyLTEAVRRRPYSVILLDEVEK 681
Cdd:cd19498 83 TEV-----------GYVGRD----VESIIRDLVEGIVFIDEIDK 111
|
|
| Clp_N |
pfam02861 |
Clp amino terminal domain, pathogenicity island component; This short domain is found in one ... |
94-145 |
5.20e-08 |
|
Clp amino terminal domain, pathogenicity island component; This short domain is found in one or two copies at the amino terminus of ClpA and ClpB proteins from bacteria and eukaryotes. The function of these domains is uncertain but they may form a protein binding site. In many bacterial species, including E.coli, this region represents the N-terminus of one of the key components of the pathogenicity island complex that injects toxin from one bacterium into another.
Pssm-ID: 460724 [Multi-domain] Cd Length: 53 Bit Score: 49.83 E-value: 5.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 491878479 94 CDKFAQQNQDKFISSELFLLAALEE-RGTISDILKKCGAKKEQISQAIQHIRG 145
Cdd:pfam02861 1 AQELARALGHQYIGTEHLLLALLEEdDGLAARLLKKAGVDLDALREAIEKLLG 53
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
410-786 |
2.01e-07 |
|
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 440232 [Multi-domain] Cd Length: 397 Bit Score: 54.15 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 410 EPLDRLERRIIQLKLEQQALQKEEDEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLSGSQHIKQELDTAKTELEQA 489
Cdd:COG0464 15 LLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 490 RRAGDLAKMSELQYGRIPALEKQLEQAETSEGKEMTLLRYRVTDEEIA---EVLSKATGIPVSKM--MEGEKEKLLRMEE 564
Cdd:COG0464 95 GELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGgleEELLELREAILDDLggLEEVKEELRELVA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 565 ELHKRvigqneavdavanAIRRSRAGLsdpnRPIGSFLFLGPTGVGKTELCKTLAKFLfdsEDAMVRIDMSEFMEKhsvs 644
Cdd:COG0464 175 LPLKR-------------PELREEYGL----PPPRGLLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSDLVSK---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 645 rlvgappgYVGyEEGGYLTEAV---RRRPYSVILLDEVEKAHAD-----------VFNILLQVLDDGRltdgqgrtvdfR 710
Cdd:COG0464 231 --------YVG-ETEKNLREVFdkaRGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEMEELR-----------S 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 711 NTVVIMTSNLGSDLiqgnkDesysemkalvmsvvsqhfrPEFINRIDETVVFHPLGKENIRAI-----------ASIQLE 779
Cdd:COG0464 291 DVVVIAATNRPDLL-----D-------------------PALLRRFDEIIFFPLPDAEERLEIfrihlrkrpldEDVDLE 346
|
....*..
gi 491878479 780 RLAKRME 786
Cdd:COG0464 347 ELAEATE 353
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
198-338 |
4.97e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 198 TKNNPVLIGEPGVGKTAIVEGLAQRIvngevpeGLKNKRVLSLDMGALIAGA------------KYRGEFEERLKaVLNE 265
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAREL-------GPPGGGVIYIDGEDILEEVldqllliivggkKASGSGELRLR-LALA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491878479 266 LSKEEGRVILFIDEIHTMVGAGKTDGAMDA--GNLLKPSLARGELHCVGATTLDEyrqyIEKDAALERRFQKVFV 338
Cdd:smart00382 73 LARKLKPDVLILDEITSLLDAEQEALLLLLeeLRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIV 143
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
347-547 |
3.44e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 347 IAILRGLKERYEIHHHVDITDPAIVAAATLSHRYISDRqlpdkAIDLIDEAASSIRMEIDSKPEPLDRLERRIIQLKLEQ 426
Cdd:COG4913 251 IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-----RLELLEAELEELRAELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 427 QALQKEEDEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLsgsQHIKQELDTAKTELEQARRAGDLAKmselqyGRI 506
Cdd:COG4913 326 DELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL---AALGLPLPASAEEFAALRAEAAALL------EAL 396
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491878479 507 PALEKQLEQAETSEGKEMTLLR--YRVTDEEIAEVLSKATGIP 547
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRreLRELEAEIASLERRKSNIP 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-593 |
3.60e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 388 DKAIDLIDEAASSIRMEIDSKPEPLDRLERRIIQLKLEQQALQKEEDEAsRKRLEMLEKELAEKEREYAELEEVWKSEKA 467
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 468 TLSGSQHIKQELDTAKTELEQARRAGDLAKMSELQyGRIPALEKQLEQAETSEGKEMTLLRYRVTDEEIAEVLSKATGIP 547
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALR-AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491878479 548 VSKmmEGEKEKLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGLSD 593
Cdd:COG1196 438 EEE--EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
412-591 |
4.38e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 412 LDRLERRIIQLKLEQQALQKEEDEAS------RKRLEMLEKELAEKEREYAELEEVWKSEKATLSGSQHIKQELDTAKTE 485
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEaqleelESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 486 LEQA--RRAGDLAKMSE---LQYGRIPALEKQLEQAETSEGKEMTLLRYRVTDEEIAEVLSKATGIPVSKMM----EGEK 556
Cdd:TIGR02168 377 LEEQleTLRSKVAQLELqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelQEEL 456
|
170 180 190
....*....|....*....|....*....|....*
gi 491878479 557 EKLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGL 591
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
564-622 |
5.17e-06 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 48.75 E-value: 5.17e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491878479 564 EELHKRVIGQNEA--VDAVA--NAIRRSRAGLSDPNRPI----GSFLFLGPTGVGKTELCKTLAKFL 622
Cdd:cd19497 8 EHLDKYVIGQERAkkVLSVAvyNHYKRIRNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| hslU |
PRK05201 |
ATP-dependent protease ATPase subunit HslU; |
564-620 |
1.19e-05 |
|
ATP-dependent protease ATPase subunit HslU;
Pssm-ID: 235364 [Multi-domain] Cd Length: 443 Bit Score: 48.54 E-value: 1.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491878479 564 EELHKRVIGQNEAVDAVANAI----RRSRagLSDPNR----P--IgsfLFLGPTGVGKTELCKTLAK 620
Cdd:PRK05201 11 SELDKYIIGQDDAKRAVAIALrnrwRRMQ--LPEELRdevtPknI---LMIGPTGVGKTEIARRLAK 72
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
185-283 |
1.30e-05 |
|
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410889 [Multi-domain] Cd Length: 158 Bit Score: 46.12 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 185 EEIRRAIQVLQRRTKNNPV---------LIGEPGVGKTAIVEGLAQRIVNGevpeglknkrVLSLDMGALIagAKYRGEF 255
Cdd:cd19481 3 ASLREAVEAPRRGSRLRRYglglpkgilLYGPPGTGKTLLAKALAGELGLP----------LIVVKLSSLL--SKYVGES 70
|
90 100
....*....|....*....|....*...
gi 491878479 256 EERLKAVLNELsKEEGRVILFIDEIHTM 283
Cdd:cd19481 71 EKNLRKIFERA-RRLAPCILFIDEIDAI 97
|
|
| HslU |
COG1220 |
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, ... |
564-620 |
1.55e-05 |
|
ATP-dependent protease HslVU (ClpYQ), ATPase subunit HslU [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440833 [Multi-domain] Cd Length: 454 Bit Score: 48.50 E-value: 1.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491878479 564 EELHKRVIGQNEAVDAVA----NAIRRSRagLSDPNRP------IgsfLFLGPTGVGKTELCKTLAK 620
Cdd:COG1220 11 AELDKYIIGQDEAKRAVAialrNRWRRQQ--LPEELRDeitpknI---LMIGPTGVGKTEIARRLAK 72
|
|
| PRK13341 |
PRK13341 |
AAA family ATPase; |
147-315 |
2.01e-05 |
|
AAA family ATPase;
Pssm-ID: 237354 [Multi-domain] Cd Length: 725 Bit Score: 48.13 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 147 QNVNDQNAEESRQALEKytidLTARAESGKLDPVIGRDEEI------RRAIQVLQRrtkNNPVLIGEPGVGKTAivegLA 220
Cdd:PRK13341 1 QDLFAFHGEQMSQSEAP----LADRLRPRTLEEFVGQDHILgegrllRRAIKADRV---GSLILYGPPGVGKTT----LA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 221 QRIVNGevpeglKNKRVLSLDmgALIAGAKyrgEFEERLKAVLNELSKEEGRVILFIDEIHTMVGAGKtdgamDAgnlLK 300
Cdd:PRK13341 70 RIIANH------TRAHFSSLN--AVLAGVK---DLRAEVDRAKERLERHGKRTILFIDEVHRFNKAQQ-----DA---LL 130
|
170
....*....|....*
gi 491878479 301 PSLARGELHCVGATT 315
Cdd:PRK13341 131 PWVENGTITLIGATT 145
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
600-698 |
2.18e-05 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 44.64 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 600 SFLFL-GPTGVGKTELCKTLAKFLFDSEDAMVRIDMSEFMEK----HSVSRLVGAPPGYVGYEEG--GYLTEAVRRRP-Y 671
Cdd:pfam13401 6 GILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPLSGRLSKEEllAALQQLLLALAvA 85
|
90 100
....*....|....*....|....*..
gi 491878479 672 SVILLDEVEKAHADVFNILLQVLDDGR 698
Cdd:pfam13401 86 VVLIIDEAQHLSLEALEELRDLLNLSS 112
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
177-381 |
3.34e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 46.42 E-value: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 177 LDPVIGrDEEIRRAIQVL---QRRTKN----------NPVLIGEPGVGKTAIVEGLAQRIvngevpeglkNKRVLSLDMG 243
Cdd:COG1223 1 LDDVVG-QEEAKKKLKLIikeLRRRENlrkfglwpprKILFYGPPGTGKTMLAEALAGEL----------KLPLLTVRLD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 244 ALIAgaKYRGEFEERLKAVLNELskEEGRVILFIDEIHTmVGAGKTDgamdagnllkPSLaRGELH-CVGA--TTLDEYR 320
Cdd:COG1223 70 SLIG--SYLGETARNLRKLFDFA--RRAPCVIFFDEFDA-IAKDRGD----------QND-VGEVKrVVNAllQELDGLP 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491878479 321 QYI----------EKDAALERRFQ-KVFVDEPSVEDTIAILRGLKERYEIhhHVDITDPAIVAAAT-LSHRYI 381
Cdd:COG1223 134 SGSvviaatnhpeLLDSALWRRFDeVIEFPLPDKEERKEILELNLKKFPL--PFELDLKKLAKKLEgLSGADI 204
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
394-591 |
3.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 394 IDEAASSIRMEIDSKPEPLDRLErriiQLKLEQQALQKEEDEasRKRLEMLEKELAEKEREyaeLEEVWKSEKATLSGSQ 473
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAE----EAKIKAEELKKAEEE--KKKVEQLKKKEAEEKKK---AEELKKAEEENKIKAA 1664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 474 HIKQELDTAKTELEQARRAGDLAKMSELQYGRIPALEKQLEQAETSEGKEMTLLRYRVTDEEIAEVlsKATGIPVSKMME 553
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI--KAEEAKKEAEED 1742
|
170 180 190
....*....|....*....|....*....|....*...
gi 491878479 554 GEKEKLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGL 591
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| RecA-like_CDC48_NLV2_r1-like |
cd19503 |
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ... |
204-280 |
7.19e-05 |
|
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410911 [Multi-domain] Cd Length: 165 Bit Score: 44.20 E-value: 7.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491878479 204 LIGEPGVGKTAIVEGLAQRIvngevpeglkNKRVLSLDmGALIAGaKYRGEFEERLKAVLNElSKEEGRVILFIDEI 280
Cdd:cd19503 39 LHGPPGTGKTLLARAVANEA----------GANFLSIS-GPSIVS-KYLGESEKNLREIFEE-ARSHAPSIIFIDEI 102
|
|
| PRK14956 |
PRK14956 |
DNA polymerase III subunits gamma and tau; Provisional |
552-696 |
7.84e-05 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184920 [Multi-domain] Cd Length: 484 Bit Score: 46.09 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 552 MEGEKEKLLR-MEEELHKRVIGQNEAVDAVANAIRRSRAGlsdpnrpiGSFLFLGPTGVGKTELCKTLAKFL-----FDS 625
Cdd:PRK14956 1 MSGTHEVLSRkYRPQFFRDVIHQDLAIGALQNALKSGKIG--------HAYIFFGPRGVGKTTIARILAKRLncenpIGN 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491878479 626 EDAMVRIDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRP----YSVILLDEVEKAHADVFNILLQVLDD 696
Cdd:PRK14956 73 EPCNECTSCLEITKGISSDVLEIDAASNRGIENIRELRDNVKFAPmggkYKVYIIDEVHMLTDQSFNALLKTLEE 147
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
412-518 |
8.61e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 412 LDRLERRIIQLKLEQQALQKEEDEASRKR---------------LEMLEKELAEKEREYAELEevwksekATLSGSQHIK 476
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidVASAEREIAELEAELERLD-------ASSDDLAALE 691
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 491878479 477 QELDTAKTELEQARRAGDLAKmselqyGRIPALEKQLEQAET 518
Cdd:COG4913 692 EQLEELEAELEELEEELDELK------GEIGRLEKELEQAEE 727
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
179-281 |
8.90e-05 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 44.03 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 179 PVIGRDEEIRRAIQVLQRRTKNNP---VLIGEPGVGKTAIVEGLAQRIV--NGEVPEG---------------LKNKRVL 238
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPpsvLLTGEAGTGKTTLLRELLRALErdGGYFLRGkcdenlpyspllealTREGLLR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491878479 239 SLDM---------------GALIAGAKYRGEFEERLKAVLNE----LSKEEGRVILFIDEIH 281
Cdd:pfam13191 81 QLLDelesslleawraallEALAPVPELPGDLAERLLDLLLRlldlLARGERPLVLVLDDLQ 142
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
372-578 |
1.24e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 372 AAATLSHRYISDRQLPDKAIDLideaaSSIRMEIDSKPEPLDRLERRIIQLKLEQQALQKEEDEASR-------KRLEML 444
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLEL-----QEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRavkdikqERDQLL 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 445 EK------ELAEKEREYAELEEVW--KSEKATLSgSQHIKQELDTAKTELEQARR---------------AGDLAKMSEL 501
Cdd:pfam15921 660 NEvktsrnELNSLSEDYEVLKRNFrnKSEEMETT-TNKLKMQLKSAQSELEQTRNtlksmegsdghamkvAMGMQKQITA 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 502 QYGRIPALEKQ---LEQAETSEGKEMTLLRyrvtdEEIAEVLSKATGIPVSK-MMEGEKEKLLRMEEELHKRVIGQNEAV 577
Cdd:pfam15921 739 KRGQIDALQSKiqfLEEAMTNANKEKHFLK-----EEKNKLSQELSTVATEKnKMAGELEVLRSQERRLKEKVANMEVAL 813
|
.
gi 491878479 578 D 578
Cdd:pfam15921 814 D 814
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
432-620 |
1.43e-04 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 45.27 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 432 EEDEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLSGSQHIKQELDTAKTELEQARRAGdlakmSELQYGRIPALEK 511
Cdd:PRK05703 52 DEDETPKKNPVLREEKRKPAKSILSLQALLEKRPSRTNSQDALLQAENALPEWKKELEKPSE-----PKEEEPKAAAESK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 512 QLEQAETSEGKEMTLLRYRVTdEEIAEVLSKATGIPVSKMMEgekEKLLRME--EELHKRVIGQ-NEAVDAVANAIRRS- 587
Cdd:PRK05703 127 VVQKELDELRDELKELKNLLE-DQLSGLRQVERIPPEFAELY---KRLKRSGlsPEIAEKLLKLlLEHMPPRERTAWRYl 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491878479 588 --------RAGLSDPNRPIGSFLFLGPTGVGKTelcKTLAK 620
Cdd:PRK05703 203 lellanmiPVRVEDILKQGGVVALVGPTGVGKT---TTLAK 240
|
|
| PRK13342 |
PRK13342 |
recombination factor protein RarA; Reviewed |
180-281 |
2.01e-04 |
|
recombination factor protein RarA; Reviewed
Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 44.69 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 180 VIGRDEEIRRAIQvlqrrTKNNPVLI--GEPGVGKTAIVEGLAQRIvngevpeglkNKRVLSLDmgALIAGAKyrgefee 257
Cdd:PRK13342 20 LLGPGKPLRRMIE-----AGRLSSMIlwGPPGTGKTTLARIIAGAT----------DAPFEALS--AVTSGVK------- 75
|
90 100
....*....|....*....|....*..
gi 491878479 258 RLKAVLNE---LSKEEGRVILFIDEIH 281
Cdd:PRK13342 76 DLREVIEEarqRRSAGRRTILFIDEIH 102
|
|
| RecA-like_KTNA1 |
cd19522 |
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ... |
196-335 |
2.41e-04 |
|
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410930 [Multi-domain] Cd Length: 170 Bit Score: 42.66 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 196 RRTKNNPVLIGEPGVGKTAIVEGLAQrivngEVPEGLKNKRVLSLdmgaliaGAKYRGEfEERLKAVLNELSKEEGRVIL 275
Cdd:cd19522 30 RRPWKGVLMVGPPGTGKTLLAKAVAT-----ECGTTFFNVSSSTL-------TSKYRGE-SEKLVRLLFEMARFYAPTTI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 276 FIDEIHTMVGAGKTDGAMDAGNLLKPSLARGELHCVGATTLDEYRQYI----------EKDAALERRFQK 335
Cdd:cd19522 97 FIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPSKMVmvlaatnfpwDIDEALRRRLEK 166
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
561-719 |
2.42e-04 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 44.00 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 561 RMEEELHKRVIGQNEAVDAVANAIrrsragLSdpNRPIgsfLFLGPTGVGKTELCKTLAKfLFDSEdaMVRI----DMse 636
Cdd:COG0714 5 RLRAEIGKVYVGQEELIELVLIAL------LA--GGHL---LLEGVPGVGKTTLAKALAR-ALGLP--FIRIqftpDL-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 637 fMEkhsvSRLVGAppgYVgYEEgGYLTEAVRRRPY--SVILLDEVEKAHADVFNILLQVLDDGRLTDGqGRTVDFRNT-V 713
Cdd:COG0714 69 -LP----SDILGT---YI-YDQ-QTGEFEFRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVTIP-GGTYKLPEPfL 137
|
....*.
gi 491878479 714 VIMTSN 719
Cdd:COG0714 138 VIATQN 143
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
203-333 |
2.80e-04 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 41.89 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 203 VLIGEPGVGKTAIVEGLAQRIVNGEVPEglknkRVLSLDMGA--LIAGAKYRGEFEERLKAVLNElSKEEGRVIlFIDEI 280
Cdd:pfam07728 3 LLVGPPGTGKTELAERLAAALSNRPVFY-----VQLTRDTTEedLFGRRNIDPGGASWVDGPLVR-AAREGEIA-VLDEI 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491878479 281 HTMVGA--GKTDGAMDAGNLLKPSLaRGELHC------VGATTLDEYRQYIEKDAALERRF 333
Cdd:pfam07728 76 NRANPDvlNSLLSLLDERRLLLPDG-GELVKAapdgfrLIATMNPLDRGLNELSPALRSRF 135
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
388-593 |
2.81e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 388 DKAIDLIDEAASSIRMEIDSKPEPLDRLERRIIQLkLEQQALQKEEDEASRKRLEMLEKELAEKEREYAELEEVWKSEka 467
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-- 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 468 tlsgsqhiKQELDTAKTELEQARRAGDlAKMSELQYGRIPALEKQLEQAETSEGKEMTLLRYRVTDEEIAEVLSKATGip 547
Cdd:TIGR02168 788 --------EAQIEQLKEELKALREALD-ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-- 856
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491878479 548 vskmMEGEKEKLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGLSD 593
Cdd:TIGR02168 857 ----LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
98-404 |
3.18e-04 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 43.84 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 98 AQQNQDKFISSELFLLAALEERG-TISDILKKCGAKKEQISQAIQHIRggqnvNDQNAEESRQALEKYTIDLTARAESgK 176
Cdd:COG1222 3 DLLTIDENIKALLALIDALQERLgVELALLLQPVKALELLEEAPALLL-----NDANLTQKRLGTPRGTAVPAESPDV-T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 177 LDPVIGRDEEIRRAIQVLQRRTKNN---------PV----LIGEPGVGKTaivegLAQRIVNGEVpeglkNKRVLSLDMG 243
Cdd:COG1222 77 FDDIGGLDEQIEEIREAVELPLKNPelfrkygiePPkgvlLYGPPGTGKT-----LLAKAVAGEL-----GAPFIRVRGS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 244 ALIAgaKYRGEFEERLKAVLnELSKEEGRVILFIDEIHTMvgAGKTDGAMDAG------NLLKPSL----ARGELHCVGA 313
Cdd:COG1222 147 ELVS--KYIGEGARNVREVF-ELAREKAPSIIFIDEIDAI--AARRTDDGTSGevqrtvNQLLAELdgfeSRGDVLIIAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 314 TtldeyrQYIEK-DAALER--RF-QKVFVDEPSVEDTIAILRGLKERYEIHHHVDITDpaiVAAAT--LSHRYIsdRQLP 387
Cdd:COG1222 222 T------NRPDLlDPALLRpgRFdRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDK---LAKLTegFSGADL--KAIV 290
|
330
....*....|....*...
gi 491878479 388 DKAIDL-IDEAASSIRME 404
Cdd:COG1222 291 TEAGMFaIREGRDTVTME 308
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
533-622 |
4.42e-04 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 43.61 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 533 DEEIAEVLSKATGIPvskmmegeKEKLLRmeEELHKRVIGQNEA--VDAVA--NAIRRSRAGLSDPNRP------IgsfL 602
Cdd:PRK05342 46 REELKEEAVELKELP--------TPKEIK--AHLDQYVIGQERAkkVLSVAvyNHYKRLRHGDKKDDDVelqksnI---L 112
|
90 100
....*....|....*....|
gi 491878479 603 FLGPTGVGKTELCKTLAKFL 622
Cdd:PRK05342 113 LIGPTGSGKTLLAQTLARIL 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
389-577 |
6.70e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 389 KAIDLIDEAASSIRMEIDSKPE----PLDRLERRIIQLKLEQQALQKEEDEASRKRLEMLEKELAEK---EREYAELEEV 461
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEeekkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKkkaEEAKKAEEDE 1687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 462 WKSEKATLSGSQHIKQELDTAKTELEQARRAGDLAKMSELQYGRIPALEKQ-------LEQAETSEGKEMTLLRYRVTDE 534
Cdd:PTZ00121 1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEaeedkkkAEEAKKDEEEKKKIAHLKKEEE 1767
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 491878479 535 EIAEVLSKATGIPVSKMMEGEKEKLlRMEEELHKRVIGQNEAV 577
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKR-RMEVDKKIKDIFDNFAN 1809
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
327-518 |
7.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 327 AALERRFQKVfvdEPSVEDTIAILRGLKERYEIHHHVDITDPAIVAAATLSHRYisdRQLpDKAIDLIDEAASSirmeid 406
Cdd:COG4913 620 AELEEELAEA---EERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI---AEL-EAELERLDASSDD------ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 407 skpepLDRLERRIIQLKLEQQALQKEEDEASRKRlEMLEKELAEKEREYAELEEVWksEKATLSGSQHIKQELDTAKTEL 486
Cdd:COG4913 687 -----LAALEEQLEELEAELEELEEELDELKGEI-GRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEERFAAA 758
|
170 180 190
....*....|....*....|....*....|..
gi 491878479 487 EQARRAGDLAKmsELQyGRIPALEKQLEQAET 518
Cdd:COG4913 759 LGDAVERELRE--NLE-ERIDALRARLNRAEE 787
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
570-623 |
8.43e-04 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 42.49 E-value: 8.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 491878479 570 VIGQNEAVDAVANAIRRSRaglsdpnrpIG-SFLFLGPTGVGKTELCKTLAKFLF 623
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILAKALN 57
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
533-622 |
1.41e-03 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 41.96 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 533 DEEIAEVLSKATGIPVSKMMEgekekllrMEEELHKRVIGQNEA--VDAVA--NAIRRSRAGLSDPNRP------IgsfL 602
Cdd:COG1219 45 EEELKEEEAEEELKKLPKPKE--------IKAFLDEYVIGQERAkkVLSVAvyNHYKRLNSGSKDDDDVeleksnI---L 113
|
90 100
....*....|....*....|
gi 491878479 603 FLGPTGVGKTELCKTLAKFL 622
Cdd:COG1219 114 LIGPTGSGKTLLAQTLARIL 133
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
375-543 |
1.54e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 375 TLSHRYISDRQLPDKAIDLIDEAASSIRMEIDSKPEP-------LDRLERRIIQLKLEQ-------QALQKEEDEAsRKR 440
Cdd:PRK04778 341 TLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAyselqeeLEEILKQLEEIEKEQeklsemlQGLRKDELEA-REK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 441 LEMLEKELAEKEReyaeleevwKSEKATLSG-SQHIKQELDTAKTELEQArragdlakMSELQYGRI--PALEKQLEQAE 517
Cdd:PRK04778 420 LERYRNKLHEIKR---------YLEKSNLPGlPEDYLEMFFEVSDEIEAL--------AEELEEKPInmEAVNRLLEEAT 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491878479 518 T--SEGKEMT------------LL----RYRVTDEEIAEVLSKA 543
Cdd:PRK04778 483 EdvETLEEETeelvenatlteqLIqyanRYRSDNEEVAEALNEA 526
|
|
| PRK14970 |
PRK14970 |
DNA polymerase III subunits gamma and tau; Provisional |
568-696 |
1.55e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184934 [Multi-domain] Cd Length: 367 Bit Score: 41.78 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 568 KRVIGQNEAVDAVANAIRRsraglsdpNRPIGSFLFLGPTGVGKTELCKTLAKFLFDSEdamvrIDMSEFMEKHSVSRLV 647
Cdd:PRK14970 17 DDVVGQSHITNTLLNAIEN--------NHLAQALLFCGPRGVGKTTCARILARKINQPG-----YDDPNEDFSFNIFELD 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 491878479 648 GAPPGYVgyEEGGYLTEAVRRRP----YSVILLDEVEKAHADVFNILLQVLDD 696
Cdd:PRK14970 84 AASNNSV--DDIRNLIDQVRIPPqtgkYKIYIIDEVHMLSSAAFNAFLKTLEE 134
|
|
| RecA-like_Ycf46-like |
cd19507 |
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ... |
204-296 |
1.67e-03 |
|
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410915 [Multi-domain] Cd Length: 161 Bit Score: 40.04 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 204 LIGEPGVGKTAIVEGLAqrivngevpeGLKNKRVLSLDMGALIAGakYRGEFEERLKAVLnELSKEEGRVILFIDEIHTm 283
Cdd:cd19507 36 LVGIQGTGKSLTAKAIA----------GVWQLPLLRLDMGRLFGG--LVGESESRLRQMI-QTAEAIAPCVLWIDEIEK- 101
|
90
....*....|...
gi 491878479 284 vGAGKTDGAMDAG 296
Cdd:cd19507 102 -GFSNADSKGDSG 113
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
396-570 |
1.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 396 EAASSIRMEIDSKPEPLDRLERRIIQLKLEQQALQKEEDEASR--KRLEMLEKELAEKEREYAELEEVWKSEKATLSGSQ 473
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 474 HIKQELDTAKTELEQARRAGDLAKMSELQYGRIPALEKQLEQAETSEGKEMTLLRYRVtdEEIAEVLSKATGipvskmME 553
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI--NGIEERIKELEE------KE 337
|
170
....*....|....*..
gi 491878479 554 GEKEKLLRMEEELHKRV 570
Cdd:PRK03918 338 ERLEELKKKLKELEKRL 354
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
410-586 |
2.27e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 410 EPLDRLERRIIQLKLE----QQALQKEEDEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLSGSQHIKQELDTAKTE 485
Cdd:COG1196 220 EELKELEAELLLLKLReleaELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 486 LEQARRAGDLAKMSELQygRIPALEKQLEQ-AETSEGKEMTLLRYRVTDEEIAEVLSKATgipvsKMMEGEKEKLLRMEE 564
Cdd:COG1196 300 LEQDIARLEERRRELEE--RLEELEEELAElEEELEELEEELEELEEELEEAEEELEEAE-----AELAEAEEALLEAEA 372
|
170 180
....*....|....*....|..
gi 491878479 565 ELHKRVIGQNEAVDAVANAIRR 586
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRA 394
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
412-593 |
2.51e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 412 LDRLERRIIQL-----KLEQQA--------LQKEEDEASRK----RLEMLEKELAEKEREYAELEEVWKSEKATLsgsQH 474
Cdd:COG1196 188 LERLEDILGELerqlePLERQAekaeryreLKEELKELEAEllllKLRELEAELEELEAELEELEAELEELEAEL---AE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 475 IKQELDTAKTELEQARRAGDLAKMSELQYG-RIPALEKQLE-QAETSEGKEMTLLRYRVTDEEIAEVLSKAtgipvskmm 552
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEEYELLaELARLEQDIArLEERRRELEERLEELEEELAELEEELEEL--------- 335
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491878479 553 EGEKEKLLRMEEELHKRVIGQNEAVDAVANAIRRSRAGLSD 593
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
195-283 |
2.62e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.86 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 195 QRRTKNNPVLIGEPGVGKTAIVEGLAQRIVNG-------EVPEGLKNKRVLSLDMGALIAGAKYRGEFEERLKAVLNELS 267
Cdd:pfam13401 1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPEVrdsvvfvDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQLLL 80
|
90
....*....|....*.
gi 491878479 268 KEEGRVILFIDEIHTM 283
Cdd:pfam13401 81 ALAVAVVLIIDEAQHL 96
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
412-492 |
2.95e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 412 LDRLERRIIQLKLEQQALQKEEDEAsRKRLEMLEKELAEKEREYAELEEVWKSEKATLSGsqhIKQELDTAKTELEQARR 491
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILEL-MERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAERE 166
|
.
gi 491878479 492 A 492
Cdd:COG1579 167 E 167
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
417-568 |
3.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 417 RRIIQLKLEQQALQKEEDEASRKRLEMLEKELAEKEREYAELEEVWKSEKatlsgsqhiKQELDTAKtELEQARRAGDLA 496
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE---------AKKADEAK-KAEEKKKADELK 1552
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491878479 497 KMSELqygRIPALEKQLEQAETSEGKEMTLLRyrvtDEEIAEVLSKATGIPVSKMMEGEK----EKLLRMEEELHK 568
Cdd:PTZ00121 1553 KAEEL---KKAEEKKKAEEAKKAEEDKNMALR----KAEEAKKAEEARIEEVMKLYEEEKkmkaEEAKKAEEAKIK 1621
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
185-283 |
3.21e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.16 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 185 EEIRRAIQVLQRRTKNNP---VLIGEPGVGKTAIVEGLAQR---------IVNGEV-PEGLknKRVLSLDMGaLIAGAKY 251
Cdd:COG3267 26 PSHREALARLEYALAQGGgfvVLTGEVGTGKTTLLRRLLERlpddvkvayIPNPQLsPAEL--LRAIADELG-LEPKGAS 102
|
90 100 110
....*....|....*....|....*....|..
gi 491878479 252 RGEFEERLKAVLNELSKEEGRVILFIDEIHTM 283
Cdd:COG3267 103 KADLLRQLQEFLLELAAAGRRVVLIIDEAQNL 134
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
557-620 |
4.41e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 40.23 E-value: 4.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491878479 557 EKLLRME------EELHKRV---IGQNEAVDAVANAIRRSragLSDPNRPIGS----FLFLGPTGVGKTelcKTLAK 620
Cdd:COG1419 113 ERLLEAGvspelaRELLEKLpedLSAEEAWRALLEALARR---LPVAEDPLLDeggvIALVGPTGVGKT---TTIAK 183
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
180-280 |
4.53e-03 |
|
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 440478 [Multi-domain] Cd Length: 292 Bit Score: 40.15 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 180 VIGRDEEIRRA-IQVLQRRtknnPVLI-GEPGVGKTAIVEGLAQRIvngevpeGLKNKRV------LSLDM-GALIAGAK 250
Cdd:COG0714 14 YVGQEELIELVlIALLAGG----HLLLeGVPGVGKTTLAKALARAL-------GLPFIRIqftpdlLPSDIlGTYIYDQQ 82
|
90 100 110
....*....|....*....|....*....|
gi 491878479 251 YrGEFEERLKAVLnelskeegRVILFIDEI 280
Cdd:COG0714 83 T-GEFEFRPGPLF--------ANVLLADEI 103
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
572-694 |
4.60e-03 |
|
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required for, along with delta' subunit, the assembly of the processivity factor beta(2) onto primed DNA in the DNA polymerase III holoenzyme-catalyzed reaction. The delta subunit is also known as HolA.
Pssm-ID: 433013 [Multi-domain] Cd Length: 161 Bit Score: 38.73 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 572 GQNEAVDAVANAIRRsraglsdpNRPIGSFLFLGPTGVGKTELCKTLAKFLFDSEDamvriDMSEFMEKHSVSRLV--GA 649
Cdd:pfam13177 1 GQPEAIQLLQNSLEN--------GRLSHAYLFSGPEGVGKLELALAFAKALFCEEP-----GDDLPCGQCRSCRRIesGN 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 491878479 650 PPGYVGYEEGG---------YLTEAVRRRPY----SVILLDEVEKAHADVFNILLQVL 694
Cdd:pfam13177 68 HPDLVIIEPEGqsikidqirELQKEFSKSPYegkkKVYIIEDAEKMTASAANSLLKFL 125
|
|
| RecA-like_VPS4 |
cd19521 |
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ... |
203-335 |
5.18e-03 |
|
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410929 [Multi-domain] Cd Length: 170 Bit Score: 38.69 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 203 VLIGEPGVGKTAIVEGLAQRIvngevpeglkNKRVLSLDMGALIAgaKYRGEfEERLKAVLNELSKEEGRVILFIDEIHT 282
Cdd:cd19521 44 LLYGPPGTGKSYLAKAVATEA----------NSTFFSVSSSDLVS--KWMGE-SEKLVKQLFAMARENKPSIIFIDEVDS 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491878479 283 MVGAgKTDGAMDAGNLLKPSL----------ARGELhCVGATTLDeyrqyIEKDAALERRFQK 335
Cdd:cd19521 111 LCGT-RGEGESEASRRIKTELlvqmngvgndSQGVL-VLGATNIP-----WQLDSAIRRRFEK 166
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
106-223 |
6.36e-03 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 39.75 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 106 ISSELFLLAALEERGTISD-ILKKCGAKKEQISQAIQHIRGGQNV----NDQNAEESRQALEKYTIDLTARAESGK--LD 178
Cdd:COG3829 59 LIPNSPLLEVLKTGKPVTGvIQKTGGKGKTVIVTAIPIFEDGEVIgaveTFRDITELKRLERKLREEELERGLSAKytFD 138
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 491878479 179 PVIGRDEEIRRAIQVLQR--RTkNNPVLI-GEPGVGKtaivEGLAQRI 223
Cdd:COG3829 139 DIIGKSPAMKELLELAKRvaKS-DSTVLIlGESGTGK----ELFARAI 181
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-570 |
6.48e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 399 SSIRMEIDSKPEPLDRLERRIIQLKLEQQALQKEEdEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLSGSQHIKQE 478
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE-EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 479 LDTAKTELEqARRAGDLAKMSELQYGRIPA----LEKQLEQAETSEGKEMTLLRYrvTDEEIAEVLSKATGIPVSKMM-- 552
Cdd:TIGR02169 777 LEEALNDLE-ARLSHSRIPEIQAELSKLEEevsrIEARLREIEQKLNRLTLEKEY--LEKEIQELQEQRIDLKEQIKSie 853
|
170 180
....*....|....*....|....
gi 491878479 553 ------EGEKEKLLRMEEELHKRV 570
Cdd:TIGR02169 854 keienlNGKKEELEEELEELEAAL 877
|
|
| FlhF |
TIGR03499 |
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility] |
405-620 |
6.60e-03 |
|
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274609 [Multi-domain] Cd Length: 282 Bit Score: 39.24 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 405 IDSKPEPLDRLERrIIQLKLEQQALQKEEDEASRKRLEMLEKELAEKEREYAELEEVWKSEKATLSGsqhIKQELDTAKT 484
Cdd:TIGR03499 50 IDEEEAAAASAEE-EASKALEQADPKPLSATAEPLELPAPQEEPAAPAAQAAEPLLPEEELRKELEA---LRELLERLLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 485 ELEQARRAGDLAKmselqygripaLEKQLEQAETSEGKEMTLLRY---RVTDEEIAEVLSKAtgipVSKMMEGEKEKLLR 561
Cdd:TIGR03499 126 GLAWLQRPPERAK-----------LYERLLEAGVSEELARELLEKlpeDADAEDAWRWLREA----LEGMLPVKPEEDPI 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491878479 562 MEEelhKRVIgqneavdavanairrsraglsdpnrpigsfLFLGPTGVGKTelcKTLAK 620
Cdd:TIGR03499 191 LEQ---GGVI------------------------------ALVGPTGVGKT---TTLAK 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
389-520 |
6.85e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 389 KAIDLIDEAASSIRMEIDSKPEPLDRLERRIIQLKLEQQALQKEEDEAsRKRLEMLEKELAEKEREYAELEEVWKSEKAT 468
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-EAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491878479 469 L--SGSQHIKQELDTAKTELEQARRAGDLAKMSELQYGRIPALEKQLEQAETSE 520
Cdd:COG4942 113 LyrLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
|
| RarA |
COG2256 |
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ... |
180-377 |
7.55e-03 |
|
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];
Pssm-ID: 441857 [Multi-domain] Cd Length: 439 Bit Score: 39.65 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 180 VIGRDEEIRRAIQvlqrrTKNNPVLI--GEPGVGKTAIVEGLAQRIvngevpeglkNKRVLSLDmgALIAGAKyrgefee 257
Cdd:COG2256 33 LLGPGKPLRRAIE-----AGRLSSMIlwGPPGTGKTTLARLIANAT----------DAEFVALS--AVTSGVK------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 258 RLKAVLNE---LSKEEGRVILFIDEIHTMvgaGKT--DGamdagnLLkPSLARGELHCVGATTldEyRQYIEKDAALERR 332
Cdd:COG2256 89 DIREVIEEareRRAYGRRTILFVDEIHRF---NKAqqDA------LL-PHVEDGTITLIGATT--E-NPSFEVNSALLSR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491878479 333 FQkVFVDEP-SVEDTIAIL-RGL--KERYEIHHHVDITDPAIVAAATLS 377
Cdd:COG2256 156 CR-VFVLKPlSEEDLEQLLeRALadDERGLGGYKLELDDEALEALARLA 203
|
|
| PRK10787 |
PRK10787 |
DNA-binding ATP-dependent protease La; Provisional |
388-695 |
7.85e-03 |
|
DNA-binding ATP-dependent protease La; Provisional
Pssm-ID: 182730 [Multi-domain] Cd Length: 784 Bit Score: 39.92 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 388 DKAIDLIDEAASSIRMEIDSKPEPLD------RLERRIIQLKLEQQALQKEEDEASRkrlemLEKELAEKEREYAeLEEV 461
Cdd:PRK10787 160 DDPARLADTIAAHMPLKLADKQSVLEmsdvneRLEYLMAMMESEIDLLQVEKRIRNR-----VKKQMEKSQREYY-LNEQ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 462 WKSEKATLSgsqhikqELDTAKTELEQARRAGDLAKMselqygriPALEKQLEQAETSEGKEMTLLRYRVTdeEIAEVLS 541
Cdd:PRK10787 234 MKAIQKELG-------EMDDAPDENEALKRKIDAAKM--------PKEAKEKAEAELQKLKMMSPMSAEAT--VVRGYID 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 542 KATGIPVSKMMEGEKEkLLRMEEELHKRVIGqneaVDAVANAIRRSRAGLSDPNRPIGSFLFL-GPTGVGKTELCKTLAK 620
Cdd:PRK10787 297 WMVQVPWNARSKVKKD-LRQAQEILDTDHYG----LERVKDRILEYLAVQSRVNKIKGPILCLvGPPGVGKTSLGQSIAK 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 621 flfDSEDAMVRIDMSEFMEKhsvSRLVGAPPGYVGYEEGGYLTEAVR---RRPysVILLDEVEKAHADV----FNILLQV 693
Cdd:PRK10787 372 ---ATGRKYVRMALGGVRDE---AEIRGHRRTYIGSMPGKLIQKMAKvgvKNP--LFLLDEIDKMSSDMrgdpASALLEV 443
|
..
gi 491878479 694 LD 695
Cdd:PRK10787 444 LD 445
|
|
| AcoR |
COG3284 |
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription]; |
177-283 |
7.94e-03 |
|
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
Pssm-ID: 442514 [Multi-domain] Cd Length: 625 Bit Score: 39.88 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 177 LDPVIGRDEEIRRAIQVLQR-RTKNNPVLI-GEPGVGKTAIVEGLAQR---------IVN-GEVPEGLKNKRVLSLDMGA 244
Cdd:COG3284 320 LAALAGGDPAMRRALRRARRlADRDIPVLIlGETGTGKELFARAIHAAspradgpfvAVNcAAIPEELIESELFGYEPGA 399
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 491878479 245 LiAGAK---YRGEFEErlkavlnelskEEGRViLFIDEIHTM 283
Cdd:COG3284 400 F-TGARrkgRPGKIEQ-----------ADGGT-LFLDEIGDM 428
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-501 |
8.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491878479 379 RYISDRQLPdKAIDLIDEAASSIRMEIDSKPEPLDRLERRIIQLKLEQQALQK----EEDEASRKRLEMLEKELAEKERE 454
Cdd:PRK03918 603 EYLELKDAE-KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseEEYEELREEYLELSRELAGLRAE 681
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 491878479 455 YAELEEVWKSEKATLSGSQHIKQELDTAKTELEQARRAgdLAKMSEL 501
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA--LERVEEL 726
|
|
| PRK14950 |
PRK14950 |
DNA polymerase III subunits gamma and tau; Provisional |
570-620 |
9.16e-03 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 237864 [Multi-domain] Cd Length: 585 Bit Score: 39.41 E-value: 9.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 491878479 570 VIGQNEAVDAVANAIRRSRAGlsdpnrpiGSFLFLGPTGVGKTELCKTLAK 620
Cdd:PRK14950 18 LVGQEHVVQTLRNAIAEGRVA--------HAYLFTGPRGVGKTSTARILAK 60
|
|
| |
