|
Name |
Accession |
Description |
Interval |
E-value |
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
78-788 |
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: 1136.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 78 GNFRMDLGGGRKQGAALEEYGTDLTALAKQGKLDPVIGREEEIQRTIQILSRRTKNNPALVGPAGVGKTAIMEGLASRII 157
Cdd:COG0542 146 GGSRVTSQNPESKTPALDKYGRDLTELAREGKLDPVIGRDEEIRRVIQILSRRTKNNPVLIGEPGVGKTAIVEGLAQRIV 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 158 RGEVPESMKDKRVIVLDLGALISGAKFRGDFEERLKSVLSDLEGAEGKVILFVDEMHLLLGFGKAEGSIDASNLLKPALA 237
Cdd:COG0542 226 NGDVPESLKDKRVLSLDLGALVAGAKYRGEFEERLKAVLDEVKKSEGNIILFIDELHTLVGAGGAEGAMDAANLLKPALA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 238 RGKLHCCGATTLEEYRKYIEKDAALARRFQAVMVNEPSVADTISILRGLKERYEVHHGVRITDDALVTAATYSARYITDR 317
Cdd:COG0542 306 RGELRCIGATTLDEYRKYIEKDAALERRFQPVLVEEPSVEDTISILRGLKERYEAHHGVRITDEALVAAVRLSDRYITDR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 318 FLPDKAIDLVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKETDTTSVERREKLESKLTDLKEEQDKLSAAWEE 397
Cdd:COG0542 386 FLPDKAIDLIDEAAARVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEA 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 398 ERKLLDSIKKAKTELEQarielertqregnyaraselQYAIIPELERSVPKEEKTLEEKKPsMVHDSVTSDDIAVVVSRA 477
Cdd:COG0542 466 EKELIEEIQELKEELEQ--------------------RYGKIPELEKELAELEEELAELAP-LLREEVTEEDIAEVVSRW 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 478 TGIPTTNLMRGERDKLLNMEQTIGKKIIGQDEALKAIADAVRLSRAGLQNTNRPLASFLFLGPTGVGKTALTKALAEFLF 557
Cdd:COG0542 525 TGIPVGKLLEGEREKLLNLEEELHERVIGQDEAVEAVADAIRRSRAGLKDPNRPIGSFLFLGPTGVGKTELAKALAEFLF 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 558 DTDKAMIRFDMSEFQEKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFLTDSQ 637
Cdd:COG0542 605 GDEDALIRIDMSEYMEKHSVSRLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLLDEIEKAHPDVFNILLQVLDDGRLTDGQ 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 638 GRKVDFRSTLIVMTSNLGSDILVADPSTTVTPKS-RDAVMDVVQKYYPPEFLNRIDDQIVFNKLSEKNLEDIVNVRLDEV 716
Cdd:COG0542 685 GRTVDFRNTIIIMTSNIGSELILDLAEDEPDYEEmKEAVMEELKKHFRPEFLNRIDEIIVFHPLSKEELRKIVDLQLKRL 764
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112909 717 QQRLNDRRIILTVTEAARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQGEIKSDENVVIDVLDGELE 788
Cdd:COG0542 765 RKRLAERGITLELTDAAKDFLAEKGYDPEYGARPLKRAIQRELEDPLAEEILAGEIKEGDTITVDVDDGELV 836
|
|
| chaperone_ClpB |
TIGR03346 |
ATP-dependent chaperone ClpB; Members of this protein family are the bacterial ATP-dependent ... |
82-787 |
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: 1103.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 82 MDLGGGRK--------QGAALEEYGTDLTALAKQGKLDPVIGREEEIQRTIQILSRRTKNNPALVGPAGVGKTAIMEGLA 153
Cdd:TIGR03346 136 NAVRGGQKvtdanaedQYEALEKYARDLTERAREGKLDPVIGRDEEIRRTIQVLSRRTKNNPVLIGEPGVGKTAIVEGLA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 154 SRIIRGEVPESMKDKRVIVLDLGALISGAKFRGDFEERLKSVLSDLEGAEGKVILFVDEMHLLLGFGKAEGSIDASNLLK 233
Cdd:TIGR03346 216 QRIVNGDVPEGLKNKRLLALDMGALIAGAKYRGEFEERLKAVLNEVTKSEGQIILFIDELHTLVGAGKAEGAMDAGNMLK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 234 PALARGKLHCCGATTLEEYRKYIEKDAALARRFQAVMVNEPSVADTISILRGLKERYEVHHGVRITDDALVTAATYSARY 313
Cdd:TIGR03346 296 PALARGELHCIGATTLDEYRKYIEKDAALERRFQPVFVDEPSVEDTISILRGLKERYEVHHGVRITDPAIVAAATLSHRY 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 314 ITDRFLPDKAIDLVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKETDTTSVERREKLESKLTDLKEEQDKLSA 393
Cdd:TIGR03346 376 ITDRFLPDKAIDLIDEAAARIRMEIDSKPEELDELDRRIIQLEIEREALKKEKDEASKKRLEDLEKELADLEEEYAELEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 394 AWEEERKLLDSIKKAKTELEQARIELERTQREGNYARASELQYAIIPELERSVPKEEKTLEEKKPSMVHDSVTSDDIAVV 473
Cdd:TIGR03346 456 QWKAEKASIQGIQQIKEEIEQVRLELEQAEREGDLAKAAELQYGKLPELEKQLQAAEQKLGEEQNRLLREEVTAEEIAEV 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 474 VSRATGIPTTNLMRGERDKLLNMEQTIGKKIIGQDEALKAIADAVRLSRAGLQNTNRPLASFLFLGPTGVGKTALTKALA 553
Cdd:TIGR03346 536 VSRWTGIPVSKMLEGEREKLLHMEEELHERVVGQDEAVEAVSDAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELAKALA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 554 EFLFDTDKAMIRFDMSEFQEKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFL 633
Cdd:TIGR03346 616 EFLFDSEDAMVRIDMSEYMEKHSVARLIGAPPGYVGYEEGGQLTEAVRRRPYSVVLFDEVEKAHPDVFNVLLQVLDDGRL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 634 TDSQGRKVDFRSTLIVMTSNLGSDILVADPSTTVTPKSRDAVMDVVQKYYPPEFLNRIDDQIVFNKLSEKNLEDIVNVRL 713
Cdd:TIGR03346 696 TDGQGRTVDFRNTVIIMTSNLGSDFIQELAGGDDYEEMREAVMEVLRAHFRPEFLNRIDEIVVFHPLGREQIARIVEIQL 775
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112909 714 DEVQQRLNDRRIILTVTEAARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQGEIKSDENVVIDVLDGEL 787
Cdd:TIGR03346 776 GRLRKRLAERKITLELSDAALDFLAEAGYDPVYGARPLKRAIQREIENPLAKKILAGEVAPGDTIRVDVEGGRL 849
|
|
| PRK10865 |
PRK10865 |
ATP-dependent chaperone ClpB; |
86-787 |
0e+00 |
|
ATP-dependent chaperone ClpB;
Pssm-ID: 182791 [Multi-domain] Cd Length: 857 Bit Score: 871.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 86 GGRKQGAALEEYGTDLTALAKQGKLDPVIGREEEIQRTIQILSRRTKNNPALVGPAGVGKTAIMEGLASRIIRGEVPESM 165
Cdd:PRK10865 153 GAEDQRQALKKYTIDLTERAEQGKLDPVIGRDEEIRRTIQVLQRRTKNNPVLIGEPGVGKTAIVEGLAQRIINGEVPEGL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 166 KDKRVIVLDLGALISGAKFRGDFEERLKSVLSDLEGAEGKVILFVDEMHLLLGFGKAEGSIDASNLLKPALARGKLHCCG 245
Cdd:PRK10865 233 KGRRVLALDMGALVAGAKYRGEFEERLKGVLNDLAKQEGNVILFIDELHTMVGAGKADGAMDAGNMLKPALARGELHCVG 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 246 ATTLEEYRKYIEKDAALARRFQAVMVNEPSVADTISILRGLKERYEVHHGVRITDDALVTAATYSARYITDRFLPDKAID 325
Cdd:PRK10865 313 ATTLDEYRQYIEKDAALERRFQKVFVAEPSVEDTIAILRGLKERYELHHHVQITDPAIVAAATLSHRYIADRQLPDKAID 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 326 LVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKETDTTSVERREKLESKLTDLKEEQDKLSAAWEEERKLLDSI 405
Cdd:PRK10865 393 LIDEAASSIRMQIDSKPEELDRLDRRIIQLKLEQQALMKESDEASKKRLDMLNEELSDKERQYSELEEEWKAEKASLSGT 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 406 KKAKTELEQARIELERTQREGNYARASELQYAIIPELERSVPKEEKTLEEKKpSMVHDSVTSDDIAVVVSRATGIPTTNL 485
Cdd:PRK10865 473 QTIKAELEQAKIAIEQARRVGDLARMSELQYGKIPELEKQLAAATQLEGKTM-RLLRNKVTDAEIAEVLARWTGIPVSRM 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 486 MRGERDKLLNMEQTIGKKIIGQDEALKAIADAVRLSRAGLQNTNRPLASFLFLGPTGVGKTALTKALAEFLFDTDKAMIR 565
Cdd:PRK10865 552 LESEREKLLRMEQELHHRVIGQNEAVEAVSNAIRRSRAGLSDPNRPIGSFLFLGPTGVGKTELCKALANFMFDSDDAMVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 566 FDMSEFQEKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFLTDSQGRKVDFRS 645
Cdd:PRK10865 632 IDMSEFMEKHSVSRLVGAPPGYVGYEEGGYLTEAVRRRPYSVILLDEVEKAHPDVFNILLQVLDDGRLTDGQGRTVDFRN 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 646 TLIVMTSNLGSDILVADPSTTVTPKSRDAVMDVVQKYYPPEFLNRIDDQIVFNKLSEKNLEDIVNVRLDEVQQRLNDRRI 725
Cdd:PRK10865 712 TVVIMTSNLGSDLIQERFGELDYAHMKELVLGVVSHNFRPEFINRIDEVVVFHPLGEQHIASIAQIQLQRLYKRLEERGY 791
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112909 726 ILTVTEAARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQGEIKSDENVVIDVLDGEL 787
Cdd:PRK10865 792 EIHISDEALKLLSENGYDPVYGARPLKRAIQQQIENPLAQQILSGELVPGKVIRLEVNDDRI 853
|
|
| clpC |
CHL00095 |
Clp protease ATP binding subunit |
83-790 |
0e+00 |
|
Clp protease ATP binding subunit
Pssm-ID: 214361 [Multi-domain] Cd Length: 821 Bit Score: 773.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 83 DLGGGRKQGAALEEYGTDLTALAKQGKLDPVIGREEEIQRTIQILSRRTKNNPALVGPAGVGKTAIMEGLASRIIRGEVP 162
Cdd:CHL00095 151 GAEQSRSKTPTLEEFGTNLTKEAIDGNLDPVIGREKEIERVIQILGRRTKNNPILIGEPGVGKTAIAEGLAQRIVNRDVP 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 163 ESMKDKRVIVLDLGALISGAKFRGDFEERLKSVLSDLEGAeGKVILFVDEMHLLLGFGKAEGSIDASNLLKPALARGKLH 242
Cdd:CHL00095 231 DILEDKLVITLDIGLLLAGTKYRGEFEERLKRIFDEIQEN-NNIILVIDEVHTLIGAGAAEGAIDAANILKPALARGELQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 243 CCGATTLEEYRKYIEKDAALARRFQAVMVNEPSVADTISILRGLKERYEVHHGVRITDDALVTAATYSARYITDRFLPDK 322
Cdd:CHL00095 310 CIGATTLDEYRKHIEKDPALERRFQPVYVGEPSVEETIEILFGLRSRYEKHHNLSISDKALEAAAKLSDQYIADRFLPDK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 323 AIDLVDEACSSLRLQQESKPDELRRLDRQIMTIQieleslrketdttsverREKLESKLTDLKEEQDKLSAAWEEERKLL 402
Cdd:CHL00095 390 AIDLLDEAGSRVRLINSRLPPAARELDKELREIL-----------------KDKDEAIREQDFETAKQLRDREMEVRAQI 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 403 DSIKKAKTELEQARIELertqregnyaraselqyaiipelersvpkeektleekkpsmvhDSVTSDDIAVVVSRATGIPT 482
Cdd:CHL00095 453 AAIIQSKKTEEEKRLEV-------------------------------------------PVVTEEDIAEIVSAWTGIPV 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 483 TNLMRGERDKLLNMEQTIGKKIIGQDEALKAIADAVRLSRAGLQNTNRPLASFLFLGPTGVGKTALTKALAEFLFDTDKA 562
Cdd:CHL00095 490 NKLTKSESEKLLHMEETLHKRIIGQDEAVVAVSKAIRRARVGLKNPNRPIASFLFSGPTGVGKTELTKALASYFFGSEDA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 563 MIRFDMSEFQEKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFLTDSQGRKVD 642
Cdd:CHL00095 570 MIRLDMSEYMEKHTVSKLIGSPPGYVGYNEGGQLTEAVRKKPYTVVLFDEIEKAHPDIFNLLLQILDDGRLTDSKGRTID 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 643 FRSTLIVMTSNLGSDI-------LVADPSTTVTPKS-----RDAVMDVVQKYYPPEFLNRIDDQIVFNKLSEKNLEDIVN 710
Cdd:CHL00095 650 FKNTLIIMTSNLGSKVietnsggLGFELSENQLSEKqykrlSNLVNEELKQFFRPEFLNRLDEIIVFRQLTKNDVWEIAE 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 711 VRLDEVQQRLNDRRIILTVTEAARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQGEIKSDENVVIDVlDGELEFK 790
Cdd:CHL00095 730 IMLKNLFKRLNEQGIQLEVTERIKTLLIEEGYNPLYGARPLRRAIMRLLEDPLAEEVLSFKIKPGDIIIVDV-NDEKEVK 808
|
|
| ClpA |
TIGR02639 |
ATP-dependent Clp protease ATP-binding subunit clpA; [Protein fate, Degradation of proteins, ... |
82-782 |
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: 704.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 82 MDLGGGRKQGAALEEYGTDLTALAKQGKLDPVIGREEEIQRTIQILSRRTKNNPALVGPAGVGKTAIMEGLASRIIRGEV 161
Cdd:TIGR02639 152 EAGKEEEKGQDALEKYTVDLTEKAKNGKIDPLIGREDELERTIQVLCRRKKNNPLLVGEPGVGKTAIVEGLALRIAEGKV 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 162 PESMKDKRVIVLDLGALISGAKFRGDFEERLKSVLSDLEGAEGKvILFVDEMHLLLGFGK-AEGSIDASNLLKPALARGK 240
Cdd:TIGR02639 232 PERLKNAKIYSLDMGTLLAGTKYRGDFEERLKAVVSEIEKEPNA-ILFIDEIHTIVGAGAtSGGSMDASNLLKPALSSGK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 241 LHCCGATTLEEYRKYIEKDAALARRFQAVMVNEPSVADTISILRGLKERYEVHHGVRITDDALVTAATYSARYITDRFLP 320
Cdd:TIGR02639 311 IRCIGSTTYEEYKNHFEKDRALSRRFQKIDVGEPSIEETVKILKGLKEQYEEFHHVKYSDEALEAAVELSARYINDRFLP 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 321 DKAIDLVDEACSSLRLQQESKPDElrrldrqimtiqieleslrketdttsverrekleskltdlkeeqdklsaaweeerk 400
Cdd:TIGR02639 391 DKAIDVIDEAGAAFRLRPKAKKKA-------------------------------------------------------- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 401 lldsikkakteleqarielertqregnyaraselqyaiipelersvpkeektleekkpsmvhdSVTSDDIAVVVSRATGI 480
Cdd:TIGR02639 415 ---------------------------------------------------------------NVNVKDIENVVAKMAKI 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 481 PTTNLMRGERDKLLNMEQTIGKKIIGQDEALKAIADAVRLSRAGLQNTNRPLASFLFLGPTGVGKTALTKALAEFLfdtD 560
Cdd:TIGR02639 432 PVKTVSSDDREQLKNLEKNLKAKIFGQDEAIDQLVSAIKRSRAGLGDPNKPVGSFLFVGPTGVGKTELAKQLAEEL---G 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 561 KAMIRFDMSEFQEKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFLTDSQGRK 640
Cdd:TIGR02639 509 VHLLRFDMSEYMEKHTVSRLIGSPPGYVGFEQGGLLTDAVRKHPHCVLLLDEIEKAHPDIYNILLQVMDYATLTDNNGRK 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 641 VDFRSTLIVMTSNLGSDILVADPSTTVTPKSRDAVMDVVQKYYPPEFLNRIDDQIVFNKLSEKNLEDIVNVRLDEVQQRL 720
Cdd:TIGR02639 589 ADFRNVILIMTSNAGASEMSKPPIGFGGENRESKSLKAIKKLFSPEFRNRLDAIIHFNDLSEEMAEKIVKKFLDELQDQL 668
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112909 721 NDRRIILTVTEAARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQGEIKSDENVVIDV 782
Cdd:TIGR02639 669 NEKNIELELTDDAKKYLAEKGYDEEFGARPLARVIQEEIKKPLSDEILFGKLKKGGSVKISL 730
|
|
| VI_ClpV1 |
TIGR03345 |
type VI secretion ATPase, ClpV1 family; Members of this protein family are homologs of ClpB, ... |
85-769 |
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: 690.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 85 GGGRKQGAALEEYGTDLTALAKQGKLDPVIGREEEIQRTIQILSRRTKNNPALVGPAGVGKTAIMEGLASRIIRGEVPES 164
Cdd:TIGR03345 161 AAGAAGTSALDQYTTDLTAQAREGKIDPVLGRDDEIRQMIDILLRRRQNNPILTGEAGVGKTAVVEGLALRIAAGDVPPA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 165 MKDKRVIVLDLGALISGAKFRGDFEERLKSVLSDLEGAEGKVILFVDEMHLLLGFGKAEGSIDASNLLKPALARGKLHCC 244
Cdd:TIGR03345 241 LRNVRLLSLDLGLLQAGASVKGEFENRLKSVIDEVKASPQPIILFIDEAHTLIGAGGQAGQGDAANLLKPALARGELRTI 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 245 GATTLEEYRKYIEKDAALARRFQAVMVNEPSVADTISILRGLKERYEVHHGVRITDDALVTAATYSARYITDRFLPDKAI 324
Cdd:TIGR03345 321 AATTWAEYKKYFEKDPALTRRFQVVKVEEPDEETAIRMLRGLAPVLEKHHGVLILDEAVVAAVELSHRYIPGRQLPDKAV 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 325 DLVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKE--TDTTSVERREKLESKLTDLKEEQDKLSAAWEEERKLL 402
Cdd:TIGR03345 401 SLLDTACARVALSQNATPAALEDLRRRIAALELELDALEREaaLGADHDERLAELRAELAALEAELAALEARWQQEKELV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 403 DSIKKAKTELEQArielERTQREGNYARASELQyaiipELERSVpkeekTLEEKKPSMVHDSVTSDDIAVVVSRATGIPT 482
Cdd:TIGR03345 481 EAILALRAELEAD----ADAPADDDDALRAQLA-----ELEAAL-----ASAQGEEPLVFPEVDAQAVAEVVADWTGIPV 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 483 TNLMRGERDKLLNMEQTIGKKIIGQDEALKAIADAVRLSRAGLQNTNRPLASFLFLGPTGVGKTALTKALAEFLFDTDKA 562
Cdd:TIGR03345 547 GRMVRDEIEAVLSLPDRLAERVIGQDHALEAIAERIRTARAGLEDPRKPLGVFLLVGPSGVGKTETALALAELLYGGEQN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 563 MIRFDMSEFQEKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFLTDSQGRKVD 642
Cdd:TIGR03345 627 LITINMSEFQEAHTVSRLKGSPPGYVGYGEGGVLTEAVRRKPYSVVLLDEVEKAHPDVLELFYQVFDKGVMEDGEGREID 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 643 FRSTLIVMTSNLGSDILV---ADPSTTVTPKS-RDAVMDVVQKYYPPEFLNRIdDQIVFNKLSEKNLEDIVNVRLDEVQQ 718
Cdd:TIGR03345 707 FKNTVILLTSNAGSDLIMalcADPETAPDPEAlLEALRPELLKVFKPAFLGRM-TVIPYLPLDDDVLAAIVRLKLDRIAR 785
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 19112909 719 RLNDR-RIILTVTEAARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQ 769
Cdd:TIGR03345 786 RLKENhGAELVYSEALVEHIVARCTEVESGARNIDAILNQTLLPELSRQILE 837
|
|
| clpA |
PRK11034 |
ATP-dependent Clp protease ATP-binding subunit; Provisional |
94-790 |
4.99e-180 |
|
ATP-dependent Clp protease ATP-binding subunit; Provisional
Pssm-ID: 236828 [Multi-domain] Cd Length: 758 Bit Score: 535.19 E-value: 4.99e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 94 LEEYGTDLTALAKQGKLDPVIGREEEIQRTIQILSRRTKNNPALVGPAGVGKTAIMEGLASRIIRGEVPESMKDKRVIVL 173
Cdd:PRK11034 169 MENFTTNLNQLARVGGIDPLIGREKELERAIQVLCRRRKNNPLLVGESGVGKTAIAEGLAWRIVQGDVPEVMADCTIYSL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 174 DLGALISGAKFRGDFEERLKSVLSDLEgAEGKVILFVDEMHLLLGFGKAE-GSIDASNLLKPALARGKLHCCGATTLEEY 252
Cdd:PRK11034 249 DIGSLLAGTKYRGDFEKRFKALLKQLE-QDTNSILFIDEIHTIIGAGAASgGQVDAANLIKPLLSSGKIRVIGSTTYQEF 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 253 RKYIEKDAALARRFQAVMVNEPSVADTISILRGLKERYEVHHGVRITDDALVTAATYSARYITDRFLPDKAIDLVDEACS 332
Cdd:PRK11034 328 SNIFEKDRALARRFQKIDITEPSIEETVQIINGLKPKYEAHHDVRYTAKAVRAAVELAVKYINDRHLPDKAIDVIDEAGA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 333 SLRLqqeskpdelrrldrqimtiqieleslrketdtTSVERREKleskltdlkeeqdklsaaweeerklldsikkaktel 412
Cdd:PRK11034 408 RARL--------------------------------MPVSKRKK------------------------------------ 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 413 eqarielertqregnyaraselqyaiipelersvpkeektleekkpsmvhdSVTSDDIAVVVSRATGIPTTNLMRGERDK 492
Cdd:PRK11034 420 ---------------------------------------------------TVNVADIESVVARIARIPEKSVSQSDRDT 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 493 LLNMEQTIGKKIIGQDEALKAIADAVRLSRAGLQNTNRPLASFLFLGPTGVGKTALTKALAEFLfdtDKAMIRFDMSEFQ 572
Cdd:PRK11034 449 LKNLGDRLKMLVFGQDKAIEALTEAIKMSRAGLGHEHKPVGSFLFAGPTGVGKTEVTVQLSKAL---GIELLRFDMSEYM 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 573 EKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFLTDSQGRKVDFRSTLIVMTS 652
Cdd:PRK11034 526 ERHTVSRLIGAPPGYVGFDQGGLLTDAVIKHPHAVLLLDEIEKAHPDVFNLLLQVMDNGTLTDNNGRKADFRNVVLVMTT 605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 653 NLGSDILVADPSTTVTPKSRDAVMDVVQKYYPPEFLNRIDDQIVFNKLSEKNLEDIVNVRLDEVQQRLNDRRIILTVTEA 732
Cdd:PRK11034 606 NAGVRETERKSIGLIHQDNSTDAMEEIKKIFTPEFRNRLDNIIWFDHLSTDVIHQVVDKFIVELQAQLDQKGVSLEVSQE 685
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 19112909 733 ARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQGEIKSDENVVIDVLDGELEFK 790
Cdd:PRK11034 686 ARDWLAEKGYDRAMGARPMARVIQDNLKKPLANELLFGSLVDGGQVTVALDKEKNELT 743
|
|
| RecA-like_ClpB_Hsp104-like |
cd19499 |
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ... |
492-697 |
6.41e-96 |
|
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: 296.40 E-value: 6.41e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 492 KLLNMEQTIGKKIIGQDEALKAIADAVRLSRAGLQNTNRPLASFLFLGPTGVGKTALTKALAEFLFDTDKAMIRFDMSEF 571
Cdd:cd19499 1 KLLNLEERLHERVVGQDEAVKAVSDAIRRARAGLSDPNRPIGSFLFLGPTGVGKTELAKALAELLFGDEDNLIRIDMSEY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 572 QEKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFLTDSQGRKVDFRSTLIVMT 651
Cdd:cd19499 81 MEKHSVSRLIGAPPGYVGYTEGGQLTEAVRRKPYSVVLLDEIEKAHPDVQNLLLQVLDDGRLTDSHGRTVDFKNTIIIMT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19112909 652 SNlgsdilvadpsttvtpksrdavmdvvqkYYPPEFLNRIDDQIVF 697
Cdd:cd19499 161 SN----------------------------HFRPEFLNRIDEIVVF 178
|
|
| AAA_2 |
pfam07724 |
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ... |
530-693 |
2.10e-81 |
|
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: 257.89 E-value: 2.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 530 RPLASFLFLGPTGVGKTALTKALAEFLFDTDKAMIRFDMSEFQEKHTIARLIGSPPGYIGYEESGELTEAVRRKPYAVLL 609
Cdd:pfam07724 1 RPIGSFLFLGPTGVGKTELAKALAELLFGDERALIRIDMSEYMEEHSVSRLIGAPPGYVGYEEGGQLTEAVRRKPYSIVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 610 FDELEKAHHDITNLLLQVLDEGFLTDSQGRKVDFRSTLIVMTSNLGSDIL---VADPSTTVTPKSRDAVMDVVQKYYPPE 686
Cdd:pfam07724 81 IDEIEKAHPGVQNDLLQILEGGTLTDKQGRTVDFKNTLFIMTGNFGSEKIsdaSRLGDSPDYELLKEEVMDLLKKGFIPE 160
|
....*..
gi 19112909 687 FLNRIDD 693
Cdd:pfam07724 161 FLGRLPI 167
|
|
| AAA_lid_9 |
pfam17871 |
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ... |
275-378 |
5.10e-46 |
|
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: 159.57 E-value: 5.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 275 SVADTISILRGLKERYEVHHGVRITDDALVTAATYSARYITDRFLPDKAIDLVDEACSSLRLQQESKPDELRRLDRQIMT 354
Cdd:pfam17871 1 SVEEAIEILRGLKPKYEKHHGVRISDEALEAAVKLSKRYITDRFLPDKAIDLLDEACARVRLSQESKPEELEDLERELAK 80
|
90 100
....*....|....*....|....
gi 19112909 355 IQIELESLRKETDTTSVERREKLE 378
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, ... |
700-780 |
3.85e-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: 107.88 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 700 LSEKNLEDIVNVRLDEVQQRLNDRRIILTVTEAARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQGEIKSDENVV 779
Cdd:pfam10431 1 LSKEELRKIVDLQLKELQKRLAERGITLELTDAAKDWLAEKGYDPEYGARPLRRAIQREIEDPLAEEILSGELKEGDTVR 80
|
.
gi 19112909 780 I 780
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, ... |
700-789 |
1.21e-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: 106.76 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 700 LSEKNLEDIVNVRLDEVQQRLNDRRIILTVTEAARKWLAEKGYSPAYGARPLNRLIQKRILNTMAMKIIQGEIKSDENVV 779
Cdd:smart01086 1 LDKEDLVRIVDLPLNALQKRLAEKGITLEFTDEALDWLAEKGYDPKYGARPLRRIIQRELEDPLAELILSGELKDGDTVV 80
|
90
....*....|
gi 19112909 780 IDVLDGELEF 789
Cdd:smart01086 81 VDVDDGELVF 90
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
505-663 |
8.98e-17 |
|
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: 77.96 E-value: 8.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 505 IGQDEALKAIADAVRLsraglqntnRPLASFLFLGPTGVGKTALTKALAEFLFDTDKAMIRFDMSEFQEKHTIARLigsp 584
Cdd:cd00009 1 VGQEEAIEALREALEL---------PPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAEL---- 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112909 585 pgyIGYEESGELTEAVRRKPYAVLLFDELEKAHHDITNLLLQVLDEGFLTdsqgrKVDFRSTLIVMTSNLGSDILVADP 663
Cdd:cd00009 68 ---FGHFLVRLLFELAEKAKPGVLFIDEIDSLSRGAQNALLRVLETLNDL-----RIDRENVRVIGATNRPLLGDLDRA 138
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
114-267 |
1.26e-14 |
|
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: 71.79 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 114 IGREEEIQRTIQILSRRTKNNPALVGPAGVGKTAIMEGLASRIIRgevpesmKDKRVIVLDLGALISGAKFRGDFEERLK 193
Cdd:cd00009 1 VGQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFR-------PGAPFLYLNASDLLEGLVVAELFGHFLV 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112909 194 SVLSDLEGAEGKVILFVDEMHlLLGFGKAEGSIDASNLLKPALA-RGKLHCCGATTLEEYRKyieKDAALARRFQ 267
Cdd:cd00009 74 RLLFELAEKAKPGVLFIDEID-SLSRGAQNALLRVLETLNDLRIdRENVRVIGATNRPLLGD---LDRALYDRLD 144
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
536-659 |
1.32e-11 |
|
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: 63.16 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 536 LFLGPTGVGKTALTKALAEFLFDTDKAMIRFDMSEFQEKHTIARLIGSPPGYIGYEESGE----LTEAVRRKPYAVLLFD 611
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELrlrlALALARKLKPDVLILD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 19112909 612 ELEKAHHDITNLLLQVLDEGFLTDSQGRKVDFRstlIVMTSNLGSDIL 659
Cdd:smart00382 86 EITSLLDAEQEALLLLLEELRLLLLLKSEKNLT---VILTTNDEKDLG 130
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
534-653 |
3.74e-10 |
|
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: 58.46 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 534 SFLFLGPTGVGKTALTKALAEFLFDTDKAMIRF--DMSEfqekhtiARLIGS--PPGYIGYEESGELTEAVRRKpyAVLL 609
Cdd:pfam07728 1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLtrDTTE-------EDLFGRrnIDPGGASWVDGPLVRAAREG--EIAV 71
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 19112909 610 FDELEKAHHDITNLLLQVLDEG-FLTDSQGRKVDFR--STLIVMTSN 653
Cdd:pfam07728 72 LDEINRANPDVLNSLLSLLDERrLLLPDGGELVKAApdGFRLIATMN 118
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
510-661 |
3.11e-09 |
|
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: 56.52 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 510 ALKAIADAVRLSRAGLQNTNRPLA---SFLFLGPTGVGKTALTKALAEFLfdtDKAMIRFDMSEFQEKhtiarligsppg 586
Cdd:cd19481 1 LKASLREAVEAPRRGSRLRRYGLGlpkGILLYGPPGTGKTLLAKALAGEL---GLPLIVVKLSSLLSK------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 587 YIGYEES--GELTEAVRRKPYAVLLFDELEKA------------HHDITNLLLQVLDeGFLTDSQGrkvdfrstLIVMTS 652
Cdd:cd19481 66 YVGESEKnlRKIFERARRLAPCILFIDEIDAIgrkrdssgesgeLRRVLNQLLTELD-GVNSRSKV--------LVIAAT 136
|
....*....
gi 19112909 653 NLGSDILVA 661
Cdd:cd19481 137 NRPDLLDPA 145
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
137-267 |
1.31e-07 |
|
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: 51.05 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 137 LVGPAGVGKTAIMEGLASRIirgevpesmkDKRVIVLDLGALISgaKFRGDFEERLKSVLSDLEgAEGKVILFVDEMHLL 216
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKEL----------GAPFIEISGSELVS--KYVGESEKRLRELFEAAK-KLAPCVIFIDEIDAL 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 217 LG---FGKAEGSIDASNLLKPAL-----ARGKLHCCGATTleeyrkYIEK-DAALARRFQ 267
Cdd:pfam00004 70 AGsrgSGGDSESRRVVNQLLTELdgftsSNSKVIVIAATN------RPDKlDPALLGRFD 123
|
|
| RPT1 |
COG1222 |
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ... |
504-632 |
4.50e-06 |
|
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440835 [Multi-domain] Cd Length: 326 Bit Score: 49.62 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 504 IIGQDEALKAIADAV--------RLSRAGLqntnRPLASFLFLGPTGVGKTALTKALAEflfDTDKAMIRFDMSEFQEKh 575
Cdd:COG1222 80 IGGLDEQIEEIREAVelplknpeLFRKYGI----EPPKGVLLYGPPGTGKTLLAKAVAG---ELGAPFIRVRGSELVSK- 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112909 576 tiarligsppgYIGyeESG----ELTEAVRRKPYAVLLFDELE----KAHHDIT--------NLLLQVLDeGF 632
Cdd:COG1222 152 -----------YIG--EGArnvrEVFELAREKAPSIIFIDEIDaiaaRRTDDGTsgevqrtvNQLLAELD-GF 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
131-274 |
4.52e-06 |
|
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: 47.37 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 131 TKNNPALVGPAGVGKTAIMEGLASRIIRgevpesmKDKRVIVLDLGALISGAKFR------------GDFEERLKSVLSD 198
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGP-------PGGGVIYIDGEDILEEVLDQllliivggkkasGSGELRLRLALAL 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112909 199 LEgAEGKVILFVDEMHLLLG--FGKAEGSIDASNLLKPALARGKLHCCGATTLEEyrkyIEKDAALARRFQAVMVNEP 274
Cdd:smart00382 74 AR-KLKPDVLILDEITSLLDaeQEALLLLLEELRLLLLLKSEKNLTVILTTNDEK----DLGPALLRRRFDRRIVLLL 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
343-438 |
1.75e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 343 DELRRLDRQIMTIQIELESLRKETDTTS--------VERREKLESKLTDLKEEQDKLSAAWEEERKLLDSIKKAKTELEQ 414
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEkllqllplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE 174
|
90 100
....*....|....*....|....
gi 19112909 415 ARIELERTQREGNYARASELQYAI 438
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLA 198
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
110-270 |
7.61e-05 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 44.87 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 110 LDPVIGREEEIQRTIQILS--------RRTKNNPA----LVGPAGVGKTAIMEGLASRIirgevpesmkDKRVIVLDLGA 177
Cdd:COG1223 1 LDDVVGQEEAKKKLKLIIKelrrrenlRKFGLWPPrkilFYGPPGTGKTMLAEALAGEL----------KLPLLTVRLDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 178 LISgaKFRGDFEERLKSVLSdlEGAEGKVILFVDEMHLLlgfGKAEGSIDAS-------NLLKPALARGKLHCC--GATT 248
Cdd:COG1223 71 LIG--SYLGETARNLRKLFD--FARRAPCVIFFDEFDAI---AKDRGDQNDVgevkrvvNALLQELDGLPSGSVviAATN 143
|
170 180
....*....|....*....|..
gi 19112909 249 LEEyrkyiEKDAALARRFQAVM 270
Cdd:COG1223 144 HPE-----LLDSALWRRFDEVI 160
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
343-717 |
1.09e-04 |
|
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: 45.29 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 343 DELRRLDRQIMTIQIELESLRKETDTTSVERREKLESKLTDLKEEQDKLSAAWEEERKLLDSIKKAKTELEQARIELERT 422
Cdd:COG0464 1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 423 QREGNYARASELQYAIIPELERSVPKEEKTLEEKKPSMVHDSVTSDDIAVVVSRATGIPTTNLMRGERDKLLNMEQtigK 502
Cdd:COG0464 81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAIL---D 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 503 KIIGQDEALKAIADAVRL--------SRAGLQNTNRplasFLFLGPTGVGKTALTKALAEFLfdtDKAMIRFDMSEfqek 574
Cdd:COG0464 158 DLGGLEEVKEELRELVALplkrpelrEEYGLPPPRG----LLLYGPPGTGKTLLARALAGEL---GLPLIEVDLSD---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 575 htiarLIGsppGYIGyeESGELTEAV----RRKPYAVLLFDELEKAHHD-----------ITNLLLQVLDegfltdsqgr 639
Cdd:COG0464 227 -----LVS---KYVG--ETEKNLREVfdkaRGLAPCVLFIDEADALAGKrgevgdgvgrrVVNTLLTEME---------- 286
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112909 640 kvDFRSTLIVM-TSNLGSDIlvadpsttvtpksrdavmdvvqkyyPPEFLNRIDDQIVFNKLSEKNLEDIVNVRLDEVQ 717
Cdd:COG0464 287 --ELRSDVVVIaATNRPDLL-------------------------DPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRP 338
|
|
| COG1223 |
COG1223 |
Predicted ATPase, AAA+ superfamily [General function prediction only]; |
502-630 |
1.12e-04 |
|
Predicted ATPase, AAA+ superfamily [General function prediction only];
Pssm-ID: 440836 [Multi-domain] Cd Length: 246 Bit Score: 44.49 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 502 KKIIGQDEALKAIADAVR-------LSRAGLQNTNRplasFLFLGPTGVGKTALTKALAEflfDTDKAMIRFDMSEfqek 574
Cdd:COG1223 2 DDVVGQEEAKKKLKLIIKelrrrenLRKFGLWPPRK----ILFYGPPGTGKTMLAEALAG---ELKLPLLTVRLDS---- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112909 575 htiarLIGSppgYIGyeESG----ELTEAVRRKPyAVLLFDELEKAHHD------------ITNLLLQVLDE 630
Cdd:COG1223 71 -----LIGS---YLG--ETArnlrKLFDFARRAP-CVIFFDEFDAIAKDrgdqndvgevkrVVNALLQELDG 131
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
502-556 |
1.90e-04 |
|
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: 43.74 E-value: 1.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112909 502 KKIIGQDEALKAIADAV-----RLsRAGLQNTNRPL----ASFLFLGPTGVGKTALTKALAEFL 556
Cdd:cd19497 12 KYVIGQERAKKVLSVAVynhykRI-RNNLKQKDDDVelekSNILLIGPTGSGKTLLAQTLAKIL 74
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
504-556 |
3.10e-04 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 43.88 E-value: 3.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112909 504 IIGQDEALKAIADAV-----RLSRAG-------LQNTNrplasFLFLGPTGVGKTALTKALAEFL 556
Cdd:COG1219 74 VIGQERAKKVLSVAVynhykRLNSGSkddddveLEKSN-----ILLIGPTGSGKTLLAQTLARIL 133
|
|
| RecA-like_HslU |
cd19498 |
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ... |
502-573 |
3.80e-04 |
|
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: 42.37 E-value: 3.80e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112909 502 KKIIGQDEALKAIADAVRlSRAGLQNTNRPLA------SFLFLGPTGVGKTALTKALAEFlfdTDKAMIRFDMSEFQE 573
Cdd:cd19498 11 KYIIGQDEAKRAVAIALR-NRWRRMQLPEELRdevtpkNILMIGPTGVGKTEIARRLAKL---AGAPFIKVEATKFTE 84
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
310-414 |
6.48e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 310 SARYITDRFLPDKAIDLVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRketDTTSVERREKLESKLTDLKEEQD 389
Cdd:COG5022 895 SSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSI---EYVKLPELNKLHEVESKLKETSE 971
|
90 100
....*....|....*....|....*
gi 19112909 390 KLSAAWEEERKLLDSIKKAKTELEQ 414
Cdd:COG5022 972 EYEDLLKKSTILVREGNKANSELKN 996
|
|
| RecA-like_protease |
cd19481 |
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ... |
137-236 |
7.22e-04 |
|
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: 40.73 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 137 LVGPAGVGKTAIMEGLASRIirgevpesmkDKRVIVLDLGALISgaKFRGDFEERLKSVLSDLEgAEGKVILFVDEMHLL 216
Cdd:cd19481 31 LYGPPGTGKTLLAKALAGEL----------GLPLIVVKLSSLLS--KYVGESEKNLRKIFERAR-RLAPCILFIDEIDAI 97
|
90 100
....*....|....*....|
gi 19112909 217 LGFGKAEGSIDASNLLKPAL 236
Cdd:cd19481 98 GRKRDSSGESGELRRVLNQL 117
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
504-556 |
8.03e-04 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 42.45 E-value: 8.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112909 504 IIGQDEALKAIADAV-----RLSRAG-------LQNTNrplasFLFLGPTGVGKTALTKALAEFL 556
Cdd:PRK05342 73 VIGQERAKKVLSVAVynhykRLRHGDkkdddveLQKSN-----ILLIGPTGSGKTLLAQTLARIL 132
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
343-447 |
9.64e-04 |
|
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: 42.44 E-value: 9.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 343 DELRRLDRQIMTIQIELESLRKETDttsvERREKLESKLTDLKEEQDKLSAAWEEERKLLDSIKKAKTELEQARIELERT 422
Cdd:COG4942 146 PARREQAEELRADLAELAALRAELE----AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
90 100
....*....|....*....|....*
gi 19112909 423 QREGNyARASELQYAIIPELERSVP 447
Cdd:COG4942 222 AEELE-ALIARLEAEAAAAAERTPA 245
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
129-216 |
1.40e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 39.63 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 129 RRTKNNPALVGPAGVGKTAIMEGLA-------SRIIRGEVPESMKDKRVIVLDLGALISGAKFRGDFEERLKSVLSDLEG 201
Cdd:pfam13401 2 RFGAGILVLTGESGTGKTTLLRRLLeqlpevrDSVVFVDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLAALQQLLLA 81
|
90
....*....|....*
gi 19112909 202 AEGKVILFVDEMHLL 216
Cdd:pfam13401 82 LAVAVVLIIDEAQHL 96
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
536-653 |
1.42e-03 |
|
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: 39.50 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 536 LFLGPTGVGKTALTKALAEflfDTDKAMIRFDMSEFQEKHtiarlIGSPPGYIgyeesGELTEAVRRKPYAVLLFDELEK 615
Cdd:pfam00004 2 LLYGPPGTGKTTLAKAVAK---ELGAPFIEISGSELVSKY-----VGESEKRL-----RELFEAAKKLAPCVIFIDEIDA 68
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 19112909 616 -----------AHHDITNLLLQVLDegfltdsqGRKVDFRSTLIVMTSN 653
Cdd:pfam00004 69 lagsrgsggdsESRRVVNQLLTELD--------GFTSSNSKVIVIAATN 109
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
322-434 |
1.43e-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: 42.36 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 322 KAIDLVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRK-----ETDTTSV-----ERREKLESKLTDLKEEQDKL 391
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinelEEEKEDKaleikKQEWKLEQLAADLSKYEQEL 471
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 19112909 392 SAAWEEERKLLDSIKKAKTELEQARIELERTQREGNYARASEL 434
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
344-425 |
1.45e-03 |
|
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: 42.35 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 344 ELRRLDRQIMTIQIELESLRKETDTTSvERREKLESKLTDLKEEQDKLSAAWEEERKLLDSIKKAKTELEQARIELERTQ 423
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELE-AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
|
..
gi 19112909 424 RE 425
Cdd:TIGR02168 375 EE 376
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
324-436 |
1.99e-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: 41.98 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 324 IDLVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKETDTTSVERREkLESKLTDLKEEQDKLSAAWEEERKLLD 403
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE-LEAQLRELERKIEELEAQIEKKRKRLS 920
|
90 100 110
....*....|....*....|....*....|...
gi 19112909 404 SIKKAKTELEQARIELERTQREGNYARASELQY 436
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGEDEEIPEEELSL 953
|
|
| MoxR |
COG0714 |
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ... |
497-653 |
2.14e-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: 40.92 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 497 EQTIGKKIIGQDEALKAIADAVRLsraglqntNRPLasfLFLGPTGVGKTALTKALAEFLfdtDKAMIRFdmsEFQEKHT 576
Cdd:COG0714 7 RAEIGKVYVGQEELIELVLIALLA--------GGHL---LLEGVPGVGKTTLAKALARAL---GLPFIRI---QFTPDLL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 577 IARLIGSppgYIGYEESGELTeaVRRKPY--AVLLFDELEKAHHDITNLLLQVLDEGFLTdSQGRKVDFRSTLIVM-TSN 653
Cdd:COG0714 70 PSDILGT---YIYDQQTGEFE--FRPGPLfaNVLLADEINRAPPKTQSALLEAMEERQVT-IPGGTYKLPEPFLVIaTQN 143
|
|
| Sigma54_activat |
pfam00158 |
Sigma-54 interaction domain; |
504-659 |
2.42e-03 |
|
Sigma-54 interaction domain;
Pssm-ID: 425491 [Multi-domain] Cd Length: 168 Bit Score: 39.69 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 504 IIGQDEALKAIADAVRlsRAGLQNtnrplASFLFLGPTGVGKTALTKALAEFLFDTDKAMIRFDMSEFqekhtiarligs 583
Cdd:pfam00158 1 IIGESPAMQEVLEQAK--RVAPTD-----APVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAI------------ 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 584 PPGYI-----GYEEsGELTEAVRRKP----YA---VLLFDElekahhdITNL-------LLQVLDEGFLT---DSQGRKV 641
Cdd:pfam00158 62 PEELLeselfGHEK-GAFTGADSDRKglfeLAdggTLFLDE-------IGELplelqakLLRVLQEGEFErvgGTKPIKV 133
|
170
....*....|....*....
gi 19112909 642 DFRstLIVMTS-NLGSDIL 659
Cdd:pfam00158 134 DVR--IIAATNrDLEEAVA 150
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
112-216 |
2.64e-03 |
|
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: 39.41 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 112 PVIGREEEIQRTIQILSRRTKNNPALV---GPAGVGKTAIMEGLASRI-------IRGEVPESMK--------DKRVIVL 173
Cdd:pfam13191 1 RLVGREEELEQLLDALDRVRSGRPPSVlltGEAGTGKTTLLRELLRALerdggyfLRGKCDENLPyspllealTREGLLR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112909 174 DLGALISGAKF---------------------RGDFEERLKSVLSDLEGAEGKVILFVDEMHLL 216
Cdd:pfam13191 81 QLLDELESSLLeawraallealapvpelpgdlAERLLDLLLRLLDLLARGERPLVLVLDDLQWA 144
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
356-444 |
2.69e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 356 QIELESLR--KETDTTSVERREKLESKLTDLKEEQDKLSAAWEEERKLldsikKAKTELEQARIELERTQREGNYARASE 433
Cdd:pfam17380 295 KMEQERLRqeKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERM-----AMERERELERIRQEERKRELERIRQEE 369
|
90
....*....|...
gi 19112909 434 LQYAI--IPELER 444
Cdd:pfam17380 370 IAMEIsrMRELER 382
|
|
| DNA_pol3_delta2 |
pfam13177 |
DNA polymerase III, delta subunit; DNA polymerase III, delta subunit (EC 2.7.7.7) is required ... |
506-630 |
2.75e-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: 39.12 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 506 GQDEALKaiadavRLSRAgLQNtNRPLASFLFLGPTGVGKTALTKALAEFLFDTD----------KAMIRFDmsefQEKH 575
Cdd:pfam13177 1 GQPEAIQ------LLQNS-LEN-GRLSHAYLFSGPEGVGKLELALAFAKALFCEEpgddlpcgqcRSCRRIE----SGNH 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112909 576 TIARLIGSPPGYIGYEESGELTEAVRRKPY----AVLLFDELEKAHHDITNLLLQVLDE 630
Cdd:pfam13177 69 PDLVIIEPEGQSIKIDQIRELQKEFSKSPYegkkKVYIIEDAEKMTASAANSLLKFLEE 127
|
|
| SpoVK |
COG0464 |
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ... |
137-218 |
3.04e-03 |
|
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: 40.66 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 137 LVGPAGVGKTAIMEGLASRIirgevpesmkDKRVIVLDLGALISgaKFRGDFEERLKSVLSDLEGAEGkVILFVDEMHLL 216
Cdd:COG0464 196 LYGPPGTGKTLLARALAGEL----------GLPLIEVDLSDLVS--KYVGETEKNLREVFDKARGLAP-CVLFIDEADAL 262
|
..
gi 19112909 217 LG 218
Cdd:COG0464 263 AG 264
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
533-629 |
3.05e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.48 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 533 ASFLFL-GPTGVGKTALTKALAEFLFDTDKAMIRFDMSEFQEK----HTIARLIGSPPgyIGYEESGELTEAV-----RR 602
Cdd:pfam13401 5 AGILVLtGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPkdllRALLRALGLPL--SGRLSKEELLAALqqlllAL 82
|
90 100
....*....|....*....|....*..
gi 19112909 603 KPYAVLLFDELEKAHHDITNLLLQVLD 629
Cdd:pfam13401 83 AVAVVLIIDEAQHLSLEALEELRDLLN 109
|
|
| DnaX |
COG2812 |
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair]; |
504-557 |
3.45e-03 |
|
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
Pssm-ID: 442061 [Multi-domain] Cd Length: 340 Bit Score: 40.56 E-value: 3.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 19112909 504 IIGQDEALKAIADAVRLSRaglqntnrpLA-SFLFLGPTGVGKTALTKALAEFLF 557
Cdd:COG2812 12 VVGQEHVVRTLKNALASGR---------LAhAYLFTGPRGVGKTTLARILAKALN 57
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
323-425 |
3.77e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 323 AIDLVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKETDttsvERREKLESKLTDLKEEQDKLSAAWEEERKLL 402
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELE----QARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100
....*....|....*....|...
gi 19112909 403 DSIKKAKTELEQARIELERTQRE 425
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKE 123
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
333-414 |
5.36e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 333 SLRLQQESKPDELRRLDRQIMTIQIELESLRK--ETDTTSVERREKLESKltdLKEEQDKLSAAWEEERKLLDSIKKAKT 410
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKklEEDAGTLEALEEGKKR---LQRELEALTQQLEEKAAAYDKLEKTKN 576
|
....
gi 19112909 411 ELEQ 414
Cdd:pfam01576 577 RLQQ 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
322-431 |
5.80e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 322 KAIDLVDEACSSLRLQQESKPD--ELRRLDRQIMTIQIELESLR------KETDTTSVERREKLESKLTDLKEEQDKLSA 393
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEELEerleelRELEEELEELEAELAELQEELEELLEQLSL 188
|
90 100 110
....*....|....*....|....*....|....*....
gi 19112909 394 AWEEE-RKLLDSIKKAKTELEQARIELERTQREGNYARA 431
Cdd:COG4717 189 ATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
330-444 |
5.99e-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: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 330 ACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKEtdttsVERREKLESKLTD-LKEEQDKLSAAWEEERKLLDSIKKA 408
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSE-----LRRIENRLDELSQeLSDASRKIGEIEKEIEQLEQEEEKL 735
|
90 100 110
....*....|....*....|....*....|....*..
gi 19112909 409 KTELEQARIELERTQREGNYARASELQY-AIIPELER 444
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELeARIEELEE 772
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
337-421 |
6.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 337 QQESKPDELRRLDRQIMTIQIELESLRKETDTTSvERREKLESKLTDLKEEQDKLsaawEEErklldsIKKAKTELEQAR 416
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELN-EEYNELQAELEALQAEIDKL----QAE------IAEAEAEIEERR 85
|
....*
gi 19112909 417 IELER 421
Cdd:COG3883 86 EELGE 90
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
329-421 |
6.75e-03 |
|
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: 40.04 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 329 EACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKETDTtSVERREKLESKLTDLKEEQDKLSAAWEEERKLLDSIKKA 408
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE-LEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
90
....*....|...
gi 19112909 409 KTELEQARIELER 421
Cdd:TIGR02168 903 LRELESKRSELRR 915
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
324-425 |
7.11e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 7.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 324 IDLVDEACSSLRLQQESKPDELRRLDRQIMTIQIELESLRKETDTTSVERREKLEsKLTDLKEEQDKLSAAWEEERKLLD 403
Cdd:COG1340 17 IEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-KVKELKEERDELNEKLNELREELD 95
|
90 100
....*....|....*....|..
gi 19112909 404 SIKKAKTELEQARIELERTQRE 425
Cdd:COG1340 96 ELRKELAELNKAGGSIDKLRKE 117
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
137-418 |
7.39e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 137 LVGPAGVGKTAIMEGL-------ASRIIRGEVPESMKDkRVIVLDLGALISgaKFRGDFEERLKSVLSDLEGAEGKVILF 209
Cdd:pfam12128 22 ICGTNAAGKTTLLRLLplfygeyPSRIVPGTDRDSFED-YYLPRDSSYIVY--EYQRPDGQLCMAVLHSNGDGKGVQYRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 210 VDEMHLLLGFGKAEGSI----DASNLLKpALARGKLHCCGATTLEEYRKYIEKDA-----------ALARRFqAVMVNEP 274
Cdd:pfam12128 99 IAGGYRLDDFIKANNDFvkceTVAELGR-FMKNAGIQRTNLLNTREYRSIIQNDRtllgrervelrSLARQF-ALCDSES 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 275 SVADTISILRGLKERYEVHHGVR------ITDDALVTAATYSARYITDRFLPDK--AIDLVDEACSSLRLQQESKPDE-- 344
Cdd:pfam12128 177 PLRHIDKIAKAMHSKEGKFRDVKsmivaiLEDDGVVPPKSRLNRQQVEHWIRDIqaIAGIMKIRPEFTKLQQEFNTLEsa 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 345 ---LRRLDRQIMTIQIELESLRKETDTTSVERREKLESKLTDLKEEQDKLS-------AAWEEERKLLDSIKKAKTELEQ 414
Cdd:pfam12128 257 elrLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNgelsaadAAVAKDRSELEALEDQHGAFLD 336
|
....
gi 19112909 415 ARIE 418
Cdd:pfam12128 337 ADIE 340
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
344-425 |
7.71e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 344 ELRRLDRQIMTIQIELESLRKETDTTSVERREKLESKLTDLKEEQDK---LSAAWEEERKLLDSIKKAKTELEQARIELE 420
Cdd:PRK03918 557 KLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELA 636
|
....*
gi 19112909 421 RTQRE 425
Cdd:PRK03918 637 ETEKR 641
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
357-435 |
7.80e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 357 IELESLRKETDTTsverREKLESKLTDLKEEQDKLSAawEEERKLLDSIKKAKTELEQARIELERTQREGNYA-RASELQ 435
Cdd:PRK00409 537 EEAEALLKEAEKL----KEELEEKKEKLQEEEDKLLE--EAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASvKAHELI 610
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
344-425 |
8.75e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112909 344 ELRRLDRQIMTIQIELESLRKETDTTSvERREKLESKLTDLKEEQDKLSAAWEEERKLLDSIKKAKTELEQARIELERTQ 423
Cdd:COG2433 414 EIRRLEEQVERLEAEVEELEAELEEKD-ERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELK 492
|
..
gi 19112909 424 RE 425
Cdd:COG2433 493 RK 494
|
|
| |
