|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1000 |
5.20e-120 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 395.49 E-value: 5.20e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTS-NLRVKTLRDLIHgaPVGKPAANRAFVS 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAkSLRSERLSDLIH--SKSGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 82 MVYSEEGA-------EDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTAL 154
Cdd:pfam02463 79 ITFDNEDHelpidkeEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 155 FEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEA 314
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 315 AKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELE 394
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 395 KFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEIN 474
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 475 KELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIAVTKVLGKNMDAIIVDSEKTGR 554
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 555 DCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEpphikkalqyacgnalvcdnvedarriafgghq 634
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL--------------------------------- 605
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 635 rhktvaldgtlfqksgvisggASDLKAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKY 714
Cdd:pfam02463 606 ---------------------AQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEV 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 715 SQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEE 794
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 795 EKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLK 874
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLI 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 875 NQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEE 954
Cdd:pfam02463 825 EQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*.
gi 1907203694 955 GSSQGEESVSGSQRTSSIYAREALIEIDYGDLCEDLKFPVTVVKDA 1000
Cdd:pfam02463 905 ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
4-148 |
7.87e-86 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 276.38 E-value: 7.87e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPVGKPAANRAFVSMV 83
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907203694 84 YSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNP 148
Cdd:cd03275 81 YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-920 |
1.33e-68 |
|
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: 249.98 E-value: 1.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSN-LRVKTLRDLIHGAPVGKPaANRAFVS 81
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNGQS-GNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 82 MVYSEEGA----EDRTFARVIV---GGSSEYKINNKVVQLHEYSEELEKLGILIKARNFlVFQGAVESIAMKNPKERTAL 154
Cdd:TIGR02169 80 VTFKNDDGkfpdELEVVRRLKVtddGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 155 FEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMR--------EQQQIEKEIKEKDSELNQKRPQyIKAKEnts 306
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKIGELEAEIASLERS-IAEKE--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 307 hkiKKLEAAKKSLQNAQKHYKKRKGDMDELEKEmLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHR-LKEEASKR 385
Cdd:TIGR02169 315 ---RELEDAEERLAKLEAEIDKLLAEIEELERE-IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAeTRDELKDY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 386 AATLAQ---ELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:TIGR02169 391 REKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 463 VEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQpTQKKYQIAVTKVLGKNM 542
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS-VGERYATAIEVAAGNRL 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 543 DAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGA-KLVIDVIRYEpPHIKKALQYACGNALVCDN 621
Cdd:TIGR02169 550 NNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGViGFAVDLVEFD-PKYEPAFKYVFGDTLVVED 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 622 VEDARRIAfgghQRHKTVALDGTLFQKSGVISGGASDLKAKA--RRWDEKAVDKLKEKKERLTEEL----KEQMKAKRKE 695
Cdd:TIGR02169 629 IEAARRLM----GKYRMVTLEGELFEKSGAMTGGSRAPRGGIlfSRSEPAELQRLRERLEGLKRELsslqSELRRIENRL 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 696 AELRQVQSQAHGLQMRLKYSQSDLEQ--TKTRHLALNLQEK-SKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQV 772
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQeeEKLKERLEELEEDlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 773 EDEVFEEFCREIGvRNIREFEEEkVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKvhmWEQTVKKDENEIEKL 852
Cdd:TIGR02169 785 EARLSHSRIPEIQ-AELSKLEEE-VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID---LKEQIKSIEKEIENL 859
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907203694 853 KKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLE 920
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3-932 |
2.88e-61 |
|
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: 228.02 E-value: 2.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 3 FLKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGE-KTSNLRVKTLRDLIHGAPVGKPAANRAFVS 81
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEqSAKALRGGKMEDVIFNGSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 82 MVYSEEgaeDRTFA-----------RVIVGGSSEYKINNKVVQLHEYSEELekLGILIKARNF-LVFQGAVESIAMKNPK 149
Cdd:TIGR02168 81 LVFDNS---DGLLPgadyseisitrRLYRDGESEYFINGQPCRLKDIQDLF--LDTGLGKRSYsIIEQGKISEIIEAKPE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 150 ERTALFEE---ISRsgelaqeYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEA----KQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:TIGR02168 156 ERRAIFEEaagISK-------YKERRKETERKLERTRENLDRLEDILNELERQlkslERQAEKAERYKELKAELRELELA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAK 302
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 303 ENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKarqefeermeeesqsqgrDLTLEENQVKKYHRLKEEA 382
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE------------------ELESLEAELEELEAELEEL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 383 SKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSK-----QSLEEQKKLEG 457
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkelqAELEELEEELE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 458 ELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQES--------SRQQRKAEIMESIK-----RLYPGSVYGRLIDLCQ 524
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLqarldsleRLQENLEGFSEGVKallknQSGLSGILGVLSELIS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 525 pTQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLE----VKPTDEKLRELKGAKLVIDVIRY 600
Cdd:TIGR02168 531 -VDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgteiQGNDREILKNIEGFLGVAKDLVK 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 601 EPPHIKKALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAK--ARRwdeKAVDKLKEKK 678
Cdd:TIGR02168 610 FDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSilERR---REIEELEEKI 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 679 ERLTEELKE-QMKAKRKEAELRQVQSQAHGLQMRLKYSQsdleqtktrhlalnlQEKSKLESELANFGPRINDIKRIIQS 757
Cdd:TIGR02168 687 EELEEKIAElEKALAELRKELEELEEELEQLRKELEELS---------------RQISALRKDLARLEAEVEQLEERIAQ 751
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 758 REREMKDLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNE---IAKKRL-EFENQKTRLGIQLDFEKNQLKEDQD 833
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkALREALdELRAELTLLNEEAANLRERLESLER 831
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 834 KVHMWEQTVKKDENEIEKLKK-----------------EEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRK 896
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEdieslaaeieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
970 980 990
....*....|....*....|....*....|....*.
gi 1907203694 897 KLggaNKEMTHLQKEVTAIETKLEQKRSDRHNLLQA 932
Cdd:TIGR02168 912 EL---RRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-771 |
2.76e-57 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 214.42 E-value: 2.76e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 3 FLKLIEIENFKSYKGRQIIgPFQR-FTAIIGPNGSGKSNLMDAISFVLGE-KTSNLRVKTLRDLIHGAPVGKPAANRAFV 80
Cdd:COG1196 2 RLKRLELAGFKSFADPTTI-PFEPgITAIVGPNGSGKSNIVDAIRWVLGEqSAKSLRGGKMEDVIFAGSSSRKPLGRAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 81 SMVYS-EEGAEDRTFARVIV------GGSSEYKINNKVVQLHEYSEELEKLGIliKARNF-LVFQGAVESIAMKNPKERT 152
Cdd:COG1196 81 SLTFDnSDGTLPIDYDEVTItrrlyrSGESEYYINGKPCRLKDIQDLFLDTGL--GPESYsIIGQGMIDRIIEAKPEERR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 153 ALFEE---ISRsgelaqeYDKRKKEmvkAE---EDTQFNYHRKKNIAAE----RKEAKQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:COG1196 159 AIIEEaagISK-------YKERKEE---AErklEATEENLERLEDILGElerqLEPLERQAEKAERYRELKEELKELEAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAK 302
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 303 ENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEA 382
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 383 SKRAATLAQELEKFNRDQKADQDRLDLEERkkveteakikqKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLER-----------LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 463 VEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVY-----------GRLIDLCQPTQKKYQ 531
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaalllaglrglAGAVAVLIGVEAAYE 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 532 IAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRE----LKGAKLVIDVIRYEPPHIKK 607
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgaiGAAVDLVASDLREADARYYV 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 608 ALQYACGNALVCDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRwdeKAVDKLKEKKERLTEELKE 687
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL---EAEAELEELAERLAEEELE 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 688 QMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKE 767
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....
gi 1907203694 768 KMNQ 771
Cdd:COG1196 775 EIEA 778
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
513-628 |
2.78e-32 |
|
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 214944 [Multi-domain] Cd Length: 120 Bit Score: 121.57 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 513 GSVYGRLIDLCQPtQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVK-PTDEKLRELK-- 589
Cdd:smart00968 1 PGVLGRVADLISV-DPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRsPAGSKLREALlp 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907203694 590 ---GAKLVIDVIRYePPHIKKALQYACGNALVCDNVEDARRI 628
Cdd:smart00968 80 epgFVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
515-629 |
7.86e-28 |
|
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC (Structural Maintenance of Chromosomes) family of proteins. The hinge region is responsible for formation of the DNA interacting dimer. It is also possible that the precise structure of it is an essential determinant of the specificity of the DNA-protein interaction.
Pssm-ID: 461926 [Multi-domain] Cd Length: 116 Bit Score: 108.89 E-value: 7.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 515 VYGRLIDLCQPtQKKYQIAVTKVLGKNMDAIIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLV 594
Cdd:pfam06470 4 VLGRLADLIEV-DEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGGAGPL 82
|
90 100 110
....*....|....*....|....*....|....*
gi 1907203694 595 IDVIRYEPPhIKKALQYACGNALVCDNVEDARRIA 629
Cdd:pfam06470 83 LDLVEYDDE-YRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
3-145 |
4.12e-25 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 104.30 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 3 FLKLIEIENFKSYKGRQIIGPF-QRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAPvGKPAANRAFVS 81
Cdd:cd03274 2 IITKLVLENFKSYAGEQVIGPFhKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSA-GHPNLDSCSVE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907203694 82 MvyseegaedrTFARVIVggsseykinnkvvqlheySEELEKLGILIKARNFLVFQGAVESIAM 145
Cdd:cd03274 81 V----------HFQEIID------------------KPLLKSKGIDLDHNRFLILQGEVEQIAQ 116
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-100 |
3.75e-24 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 101.00 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 4 LKLIEIENFKSYKGRQIIgPFQR-FTAIIGPNGSGKSNLMDAISFVLGEKTS-NLRVKTLRDLIHGAPVGKPAANRAFVS 81
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPgLTAIVGPNGSGKSNIIDAIRWVLGEQSAkSLRGEKMSDVIFAGSETRKPANFAEVT 79
|
90
....*....|....*....
gi 1907203694 82 MVYSEegaEDRTFArvIVG 100
Cdd:cd03278 80 LTFDN---SDGRYS--IIS 93
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
3-140 |
1.23e-23 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 101.22 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 3 FLKLIEIENFKSYKGRQIIGPFQR-FTAIIGPNGSGKSNLMDAISFVLG-EKTSNLRVKTLRDLIHGApvGKPAANRAFV 80
Cdd:cd03273 2 HIKEIILDGFKSYATRTVISGFDPqFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIYKR--GQAGITKASV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907203694 81 SMVY-------SEEGAEDR---TFAR-VIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAV 140
Cdd:cd03273 80 TIVFdnsdksqSPIGFENYpeiTVTRqIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRI 150
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
4-84 |
2.86e-23 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 97.76 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGApvGKPAANRAFVSMV 83
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGG--VKAGINSASVEIT 78
|
.
gi 1907203694 84 Y 84
Cdd:cd03239 79 F 79
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
4-145 |
3.54e-16 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 79.23 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 4 LKLIEIENFKSYKGRQIIGPFQ-RFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIH-GApvgKPAANRAFVS 81
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSpKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHeGS---GPSVMSAYVE 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 82 MVY--SEE----GAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAM 145
Cdd:cd03272 78 IIFdnSDNrfpiDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTN 147
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
7-84 |
6.74e-13 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 67.38 E-value: 6.74e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907203694 7 IEIENFKSYKGRQIIGPF-QRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTlrdlihgapVGKPAANRAFVSMVY 84
Cdd:cd03227 2 IVLGRFPSYFVPNDVTFGeGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS---------GVKAGCIVAAVSAEL 71
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-127 |
8.78e-12 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 65.42 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNlRVKTLRDLIHgapvgkPAANRAFVSMV 83
Cdd:COG0419 2 LLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLIN------VGSEEASVELE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907203694 84 YSEEGAEDR------TFARVIVGGSSE-YKINNKVVQLHEYSEELEKLGIL 127
Cdd:COG0419 75 FEHGGKRYRierrqgEFAEFLEAKPSErKEALKRLLGLEIYEELKERLKEL 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-509 |
5.16e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 156 EEISRSGELAQ-EYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE 234
Cdd:PTZ00121 1339 EEAKKAAEAAKaEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE---------NT 305
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakkkaeeakKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 306 SHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKR 385
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 386 AATLAQELEKFNRDQKADQDRLDLEERK------KVETEAKIK-QKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE 458
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeeaKKAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1907203694 459 LTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-48 |
9.36e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 64.95 E-value: 9.36e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1907203694 4 LKLIEIENFKSYkgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFV 48
Cdd:COG4637 2 ITRIRIKNFKSL--RDLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-509 |
9.98e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 118 SEELEKLGILIKARNFLVFQGAVESIAMKNPKERTAlfEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERK 197
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA--DELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 198 EAKQEKEEADRYQRLKDEVVRA-QVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMRE 276
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 277 QQQIEKEIKEKDSELNQKRPQYIKAKE--NTSHKIKKLEAAKKSLQNAQKHYKKRKGDmdELEKEMLSVEKARQEFEERM 354
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAKKADEAKKKAE 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 355 EEESQSQGRDLTLEENQVKKYHRLKEEASKRAATL--------AQELEKFNRDQKADQDR-----------LDLEERKKV 415
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkaeeakkADEAKKAEEAKKADEAKkaeekkkadelKKAEELKKA 1560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 416 ETEAKIKQKLREIEENQKRIEKLEEY-------ITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK--ELNQVMEQLGD 486
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAkkaeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKaeEEKKKVEQLKK 1640
|
410 420
....*....|....*....|...
gi 1907203694 487 ARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKA 1663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-505 |
2.03e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 144 AMKNPKERTALFEEISRSGELAQEYDKRKKemvKAEEDTQFNYHRKKNIAAER-KEAKQEKEEADRYQRLKDEVVRAQVQ 222
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKK---KAEEKKKADEAKKKAEEAKKaDEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 223 LQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKE---KDSELNQKRPQYI 299
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAdeaKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 300 KAKE-NTSHKIKKLEAAKKSLQNAQKHYKK----RKGDMDELEKEM--LSVEKARQEFEERMEEESQSQGRDLTLEENQV 372
Cdd:PTZ00121 1553 KAEElKKAEEKKKAEEAKKAEEDKNMALRKaeeaKKAEEARIEEVMklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 373 KKYHRLK--EEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE 450
Cdd:PTZ00121 1633 KKVEQLKkkEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907203694 451 EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIME 505
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-508 |
2.85e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 144 AMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNiAAERKEAKQEKEEADRYQRLKDEVVRAQvql 223
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKAAAAKKKADEAKKKAEEKKKAD--- 1434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 224 QLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKE 303
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 304 -------NTSHKIKKLEAAKKSlQNAQKHYKKRKGD----MDELEK--EMLSVEKARQEFEERMEEESQSQGRDlTLEEN 370
Cdd:PTZ00121 1515 akkaeeaKKADEAKKAEEAKKA-DEAKKAEEKKKADelkkAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAK-KAEEA 1592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 371 QVKKYHRLKEEASKRAATLAQELEKfnRDQKADQDRLDLEERKKV--------ETEAKIKQKLREIEENQKRIEKLEEYI 442
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEE--AKIKAEELKKAEEEKKKVeqlkkkeaEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907203694 443 TTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKelnqvMEQLGDARIDRQESSRQQRKAEIMESIK 508
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK-----AEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-775 |
1.44e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 156 EEISRSGELAQEYDKRKKEMV-------KAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEvvRAQVQLQLFKL 228
Cdd:PTZ00121 1185 EEVRKAEELRKAEDARKAEAArkaeeerKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN--EEIRKFEEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 229 YHNEVEIEKLNKELASKNKEIEK--DKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQyikAKENTS 306
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA---AKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 307 HKIKKLEAAKKSLQNAQKHYK--KRKGDMDELEKEmlsvekarqefeermeeESQSQGRDLTLEENQVKKYHRLKEEASK 384
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEaaEEKAEAAEKKKE-----------------EAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 385 RAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE-----------EQK 453
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEakkadeakkkaEEA 1482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 454 KLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDLCQPTQKKYQIA 533
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 534 VTKVLGKNMDAiiVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKALQYAC 613
Cdd:PTZ00121 1563 KKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 614 GNALVCDNVEDARRIAFGGHQRHKTVAldgtlfQKSGVISGGASDLKaKARRWDEKAVDKLKEKKE--RLTEELKEQMKA 691
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEA------KKAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEeaKKAEELKKKEAE 1713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 692 KRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKMNQ 771
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
....
gi 1907203694 772 VEDE 775
Cdd:PTZ00121 1794 MEVD 1797
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-113 |
5.62e-09 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 59.01 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 3 FLKLIEIENFKSYKgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGekTSNLRVKTLRDLI-HGAPvgkpaanRAFVS 81
Cdd:COG1195 1 RLKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAIYLLAT--GRSFRTARDAELIrFGAD-------GFRVR 70
|
90 100 110
....*....|....*....|....*....|..
gi 1907203694 82 MVYSEEGAEDRTFARVIVGGSSEYKINNKVVQ 113
Cdd:COG1195 71 AEVERDGREVRLGLGLSRGGKKRVRINGKPVR 102
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-183 |
1.64e-08 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 55.58 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 7 IEIENFKSYKGrQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIHGAP-VGKPAANRAFVSMVYS 85
Cdd:pfam13476 1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIrIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 86 EEGAE-----DRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVF---QGAVESIAMKNPKER-TALFE 156
Cdd:pfam13476 80 NNDGRytyaiERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVflgQEREEEFERKEKKERlEELEK 159
|
170 180
....*....|....*....|....*..
gi 1907203694 157 EISRSGELAQEYDKRKKEMVKAEEDTQ 183
Cdd:pfam13476 160 ALEEKEDEKKLLEKLLQLKEKKKELEE 186
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-509 |
3.65e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 145 MKNPKERTALFEEISRSGELAQEYD--KRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQrlKDEVVRAQVQ 222
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK--KAEEAKKADE 1526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 223 LQLFKLYHNEVEIEKLN-KELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKrpQYIKA 301
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK--LYEEE 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 302 KENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERmeeesqsqgrdltlEENQVKKYH-RLKE 380
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE--------------EENKIKAAEeAKKA 1670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 381 EASKRAATLAQELEKFNRdQKADQDRLDLEERKKVEteakikQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELT 460
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEK-KAAEALKKEAEEAKKAE------ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907203694 461 EEVEMAKRRIDEINKelnqvMEQLGDARIDRQESSRQQRKAEIMESIKR 509
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-55 |
5.50e-08 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 56.16 E-value: 5.50e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907203694 3 FLKLIEIENFKSYKgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSN 55
Cdd:COG3593 2 KLEKIKIKNFRSIK-DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
194-510 |
5.74e-08 |
|
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: 56.99 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 194 AERKEAKQEKEE-ADRYQRLKDEVVRAQVQLQLFklyhnEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGK 272
Cdd:TIGR02168 677 REIEELEEKIEElEEKIAELEKALAELRKELEEL-----EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 273 MMREQQQIEKEIKEKDSELNQKRPQYIKAKEntshKIKKLEAakkSLQNAQKHYKKRKGDMDELEKEmLSVEKARQEFEE 352
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEA----EIEELEA---QIEQLKEELKALREALDELRAE-LTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 353 RMEEESQSQGRDLtleENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQ 432
Cdd:TIGR02168 824 ERLESLERRIAAT---ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 433 KRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGD------ARIDRQESSRQQRKAEIMES 506
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaealeNKIEDDEEEARRRLKRLENK 980
|
....
gi 1907203694 507 IKRL 510
Cdd:TIGR02168 981 IKEL 984
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
309-869 |
1.02e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 309 IKKLEAAKKSLQNAQKHYKKRKGDMDELE-----KEMLSVEKARQEFEERMEEESQSQGRDLTLEENqvkkyhrlKEEAS 383
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARERLAeleylRAALRLWFAQRRLELLEAELEELRAELARLEAE--------LERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 384 KRAATLAQELEKFNRD-QKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLegeltee 462
Cdd:COG4913 316 ARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE------- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 463 vemAKRRIDEINKELNQVMEQLGDARIDRQESSRQQR--KAEI--MESIKRLYPGSVY--------------------GR 518
Cdd:COG4913 389 ---AAALLEALEEELEALEEALAEAEAALRDLRRELRelEAEIasLERRKSNIPARLLalrdalaealgldeaelpfvGE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 519 LIDLcQPTQKKYQIAVTKVLGKNMDAIIVDsEKTGRDCIQYIKEQRGEPEtflpLDYLEVKPTDEKLRELKG------AK 592
Cdd:COG4913 466 LIEV-RPEEERWRGAIERVLGGFALTLLVP-PEHYAAALRWVNRLHLRGR----LVYERVRTGLPDPERPRLdpdslaGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 593 LVIDVIRYEP---PHIKKALQYACgnalvCDNVEDARRiafggHQRHKTVA----LDGTLFQKsgvisggasDLKAKARR 665
Cdd:COG4913 540 LDFKPHPFRAwleAELGRRFDYVC-----VDSPEELRR-----HPRAITRAgqvkGNGTRHEK---------DDRRRIRS 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 666 -----WD-EKAVDKLKEKKERLTEELKE-QMKAKRKEAELRQVQSQAHGLQMRLKYS--QSDLEQTKTRHLALNlQEKSK 736
Cdd:COG4913 601 ryvlgFDnRAKLAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELE-AELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 737 LE---SELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEvfeefcreigvrnIREFEEEKvkrqnEIAKKRLEFENQ 813
Cdd:COG4913 680 LDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-------------LEQAEEEL-----DELQDRLEAAED 741
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907203694 814 KTRLGIQLDFEKNQLKEDQDKVhmwEQTVKKD-ENEIEKLKKEEQRHMKIIDETMAQ 869
Cdd:COG4913 742 LARLELRALLEERFAAALGDAV---ERELRENlEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
236-505 |
1.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 236 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELnqkrPQYIKAKENTSHKIKKLEAA 315
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL----PELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKaRQEFEERMEEESQSQGRDLTLEENQVKKYHRLKE---EASKRAATLAQE 392
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEE-RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyeEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 393 LEKFNRDQKADQDRLDLEERKKVETEaKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELT-EEVEMAKRRID 471
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELE 394
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907203694 472 EINKELNQVMEQLGD--ARIDRQESSRQQRKAEIME 505
Cdd:PRK03918 395 ELEKAKEEIEEEISKitARIGELKKEIKELKKAIEE 430
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
7-49 |
1.48e-07 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 54.66 E-value: 1.48e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1907203694 7 IEIENFKSYKGRQII------GPFQRFTAIIGPNGSGKSNLMDAISFVL 49
Cdd:COG1106 5 FSIENFRSFKDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFLR 53
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
195-508 |
1.68e-07 |
|
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: 55.51 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 195 ERKEAKQEKEEADRYQRLKDEVVRAqvqlqlfklyhnevEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMM 274
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQ--------------EKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 275 REQQQIEK-EIKEKDSELNQKRPQYIKAKENTSHKIKKL--EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFE 351
Cdd:pfam17380 345 ERERELERiRQEERKRELERIRQEEIAMEISRMRELERLqmERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQ 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 352 ERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLaQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKL-REIEE 430
Cdd:pfam17380 425 IRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQV-ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILeKELEE 503
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907203694 431 N-QKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIK 508
Cdd:pfam17380 504 RkQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-65 |
1.85e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.61 E-value: 1.85e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907203694 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVL-GEKTSNLR-VKTLRDLI 65
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSKgGAHDPKLI 64
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-99 |
2.28e-07 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 52.66 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 1 MGFLKLiEIENFKSYKGRQII----GPFQRFTAIIGPNGSGKSNLMDAISFVL-GEKTSNLRVKTLRDLIHgapvgkPAA 75
Cdd:cd03279 1 MKPLKL-ELKNFGPFREEQVIdftgLDNNGLFLICGPTGAGKSTILDAITYALyGKTPRYGRQENLRSVFA------PGE 73
|
90 100 110
....*....|....*....|....*....|....
gi 1907203694 76 NRAFVSMVYS----------EEGAEDRTFARVIV 99
Cdd:cd03279 74 DTAEVSFTFQlggkkyrverSRGLDYDQFTRIVL 107
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
3-137 |
2.44e-07 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 54.01 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 3 FLKLIEIENFKSYKgRQIIGPFQRFTAIIGPNGSGKSNLMDAISFvLGeKTSNLRVKTLRDLI-HGAPvgkpaanRAFVS 81
Cdd:PRK00064 2 YLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAIYL-LA-PGRSHRTARDKELIrFGAE-------AAVIH 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907203694 82 MVYSEEGAEDRTFARVIVGGSSEYKIN-NKVVQLHEYSEEL-------EKLGILIKA----RNFL---VFQ 137
Cdd:PRK00064 72 GRVEKGGRELPLGLEIDKKGGRKVRINgEPQRKLAELAGLLnvvlftpEDLRLVKGGpserRRFLdrlLFQ 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
659-932 |
3.78e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 659 LKAKARRwdEKAVDKLKEKKERLT------EELKEQMKAKRKEAElrqVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQ 732
Cdd:COG1196 168 SKYKERK--EEAERKLEATEENLErledilGELERQLEPLERQAE---KAERYRELKEELKELEAELLLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 733 EKSKLESELANfgpRINDIKRIIQSREREMKDLKEKMNQVEDEVfeefcreigvrnirefeEEKVKRQNEIAKKRLEFEN 812
Cdd:COG1196 243 ELEAELEELEA---ELEELEAELAELEAELEELRLELEELELEL-----------------EEAQAEEYELLAELARLEQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 813 QKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEME 892
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1907203694 893 EIRKKLGGANKEMTHLQKEVTAIETKLEQKRSDRHNLLQA 932
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-65 |
5.92e-07 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 52.31 E-value: 5.92e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907203694 3 FLKLIEIENFKSYKGRQI-IGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLI 65
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIdFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-477 |
7.77e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 7.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 156 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQlfklyhnevEI 235
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK---------KA 1589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 236 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKEntSHKIKKLEAA 315
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEA 1667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKARqefeermeeesqsqgrdltlEENQVKKYHRLKEEASKRAATLAQELEK 395
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE--------------------EAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 396 fnRDQKADQDRLDLEERKKVETEAKIKqklrEIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK 475
Cdd:PTZ00121 1728 --NKIKAEEAKKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
..
gi 1907203694 476 EL 477
Cdd:PTZ00121 1802 DI 1803
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-508 |
7.98e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 156 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVE- 234
Cdd:PRK03918 384 LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKr 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEkkkelgkmMREQQQIEKEIKEKDSELNQKRPQYIKAK----ENTSHKIK 310
Cdd:PRK03918 464 IEKELKEIEEKERKLRKELRELEKVLKKESE--------LIKLKELAEQLKELEEKLKKYNLEELEKKaeeyEKLKEKLI 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 311 KLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLkeeaskraatlA 390
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE-----------Y 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 391 QELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKL------EEYITTSKQSLEEQKKLEGeLTEEVE 464
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELekkyseEEYEELREEYLELSRELAG-LRAELE 683
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907203694 465 MAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIK 508
Cdd:PRK03918 684 ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELR 727
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
287-923 |
8.67e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 287 KDSELNQKRPQyiKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEkEMLSVEKARQEFEERMEEESQSQGRDLT 366
Cdd:PTZ00121 1077 KDFDFDAKEDN--RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 367 LEENQVKKYHRLKEEASKraatlAQELEKFNRDQKADQDRlDLEERKKVETEAKIKQKLREieENQKRIEKLEEYitTSK 446
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARK-----AEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAARKA--EEERKAEEARKA--EDA 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 447 QSLEEQKKLEgELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRlypgSVYGRLIDLCQPT 526
Cdd:PTZ00121 1224 KKAEAVKKAE-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK----AEEKKKADEAKKA 1298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 527 QKKYQIAVTKVLGKNMDAiIVDSEKTGRDCIQYIKEQRGEPETFLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIK 606
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 607 KALQYACGNALVCDNVEDARRIAFGGHQRHKTValdgtlfQKSGVISGGASDLKAKARrwDEKAVDKLKEKKE--RLTEE 684
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDKKKADEL-------KKAAAAKKKADEAKKKAE--EKKKADEAKKKAEeaKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 685 LKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSRE-REMK 763
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKaDEAK 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 764 DLKEKMNQVEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVK 843
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 844 KDE--------NEIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDK------NHEMEEIRKKLGGANKEMTHLQ 909
Cdd:PTZ00121 1609 AEEakkaeeakIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeAKKAEEDKKKAEEAKKAEEDEK 1688
|
650
....*....|....
gi 1907203694 910 KEVTAIETKLEQKR 923
Cdd:PTZ00121 1689 KAAEALKKEAEEAK 1702
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7-880 |
9.37e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.05 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 7 IEIENFKSYKGRQII--GPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLR--VKTLRDLIHGAPVGKPA-------- 74
Cdd:TIGR00618 6 LTLKNFGSYKGTHTIdfTALGPIFLICGKTGAGKTTLLDAITYALYGKLPRRSevIRSLNSLYAAPSEAAFAelefslgt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 75 -ANRAFVSMVYSEEGAEDRTFARVIVG--GSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKER 151
Cdd:TIGR00618 86 kIYRVHRTLRCTRSHRKTEQPEQLYLEqkKGRGRILAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 152 TALFE----------------EISRSGELAQEYDKRKKEMVK--AEEDTQFNYHRKKNIAAERK---EAKQEKEEADRYQ 210
Cdd:TIGR00618 166 KELLMnlfpldqytqlalmefAKKKSLHGKAELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKhlrEALQQTQQSHAYL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 211 RLKDEVVRAQVQLQ--LFKLYHNEVEIEKLNKELASKNKEIEKDKKrmdkvEDELKEKKKELGKMMREQQQIEKEIKEKD 288
Cdd:TIGR00618 246 TQKREAQEEQLKKQqlLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQSKM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 289 SELNQKRPQYIKAKENTShKIKKLEAAKKSLQNAQKHYK----KRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRD 364
Cdd:TIGR00618 321 RSRAKLLMKRAAHVKQQS-SIEEQRRLLQTLHSQEIHIRdaheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 365 LTLEENQVKKYHRLKEEASKRAatLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITT 444
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRD--LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 445 SKQSLE---EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSR-QQRKAEIMESIKRLYpgsvygrli 520
Cdd:TIGR00618 478 KEQIHLqetRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSEEDVY--------- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 521 DLCQPTQKKYQIAvtkvlgKNMDAIIVDSEKTGRDCIQYIKEQRgePETFLPLDylEVKPTDEKLRELKGAKLVIDVIRY 600
Cdd:TIGR00618 549 HQLTSERKQRASL------KEQMQEIQQSFSILTQCDNRSKEDI--PNLQNITV--RLQDLTEKLSEAEDMLACEQHALL 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 601 EPPHIKKALQYACGNALVCDNVEDARRIAFGG------HQRHKTVALDGTLFQKSgviSGGASDLKAKARRWDEKAVDKL 674
Cdd:TIGR00618 619 RKLQPEQDLQDVRLHLQQCSQELALKLTALHAlqltltQERVREHALSIRVLPKE---LLASRQLALQKMQSEKEQLTYW 695
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 675 KEKKERLTEELKEQMKAKRKEAELRQVQSQA-HGLQMRLKYSQSDLEQ----------TKTRHLALNLQEKSKLESELAN 743
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENAsSSLGSDLAAREDALNQslkelmhqarTVLKARTEAHFNNNEEVTAALQ 775
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 744 FGPRINDIKRIIQSREREMKDLKEKMNQVEDEVFEEfcreigvrnIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDF 823
Cdd:TIGR00618 776 TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE---------IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907203694 824 EKNQLKEDQDKVHMWEQTVKKDENEIEKLKK-----------EEQRHMKIIDETMAQ-LQDLKNQHLAK 880
Cdd:TIGR00618 847 ITHQLLKYEECSKQLAQLTQEQAKIIQLSDKlnginqikiqfDGDALIKFLHEITLYaNVRLANQSEGR 915
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
4-49 |
1.39e-06 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 46.44 E-value: 1.39e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907203694 4 LKLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVL 49
Cdd:pfam13555 1 LTRLQLINWGTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
4-496 |
1.46e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 4 LKLIEIENFKSYKGRQIIGPfQRFTAIIGPNGSGKSNLMDAISFVLgekTSNLRVKTLRDLIhgapvgKPAANRAFVSMV 83
Cdd:PRK01156 3 IKRIRLKNFLSHDDSEIEFD-TGINIITGKNGAGKSSIVDAIRFAL---FTDKRTEKIEDMI------KKGKNNLEVELE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 84 YSEEGAEDRTFARVIVGG-----SSEYKINNKVVQ--LHEYSEELEKLGILIKARNFL----VFQGAVESIAMKNPKERT 152
Cdd:PRK01156 73 FRIGGHVYQIRRSIERRGkgsrrEAYIKKDGSIIAegFDDTTKYIEKNILGISKDVFLnsifVGQGEMDSLISGDPAQRK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 153 ALFEEISRSGELAQEYDKRKkemvkaeedtqfnyhrkkniaaerkeakqekeeadryqrlkdEVVRAqvqlqlfkLYHNE 232
Cdd:PRK01156 153 KILDEILEINSLERNYDKLK------------------------------------------DVIDM--------LRAEI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 233 VEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTShKIKKL 312
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYES-EIKTA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 313 EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQE 392
Cdd:PRK01156 262 ESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDY 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 393 LEKFNRDQKADQDRLDLE--ERKKVETEAKIKQKLREIEENQKRIEKLEEYITtskQSLEEQKKLEGELTEEVEMAKRRI 470
Cdd:PRK01156 342 IKKKSRYDDLNNQILELEgyEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIS---EILKIQEIDPDAIKKELNEINVKL 418
|
490 500
....*....|....*....|....*.
gi 1907203694 471 DEINKELNQVMEQLGDARIDRQESSR 496
Cdd:PRK01156 419 QDISSKVSSLNQRIRALRENLDELSR 444
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-253 |
2.02e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 50.85 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 27 FTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRDLIhgapvGKPAANRAFVSMVYSEEGAEDRTFARVIVGGSSEYK 106
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRN-----GGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYRYG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 107 INNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAmKNPKERTALFEEISRSGELAqEYDKRKKEMVKAEEDTQFNY 186
Cdd:pfam13304 76 LDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPP-EAEELRLGLDVEERIELSLS-ELSDLISGLLLLSIISPLSF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907203694 187 HRKKNIAAeRKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDK 253
Cdd:pfam13304 154 LLLLDEGL-LLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRER 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
188-969 |
2.69e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 188 RKKNIAAER-KEAKQEKEEADRYQRLKDEVVRaqvqlqlfklyhnEVEIEKLNKELASKNKEIEK--DKKRMDKVEDELK 264
Cdd:PTZ00121 1084 KEDNRADEAtEEAFGKAEEAKKTETGKAEEAR-------------KAEEAKKKAEDARKAEEARKaeDARKAEEARKAED 1150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 265 EKKKELGKMMREQQQIEKEIKEKDS---ELNQKRPQYIKAKE-NTSHKIKKLEAAKKSlQNAQKHYKKRKGDMDELEKEM 340
Cdd:PTZ00121 1151 AKRVEIARKAEDARKAEEARKAEDAkkaEAARKAEEVRKAEElRKAEDARKAEAARKA-EEERKAEEARKAEDAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 341 LSVEKARQEFEERMEEESQSQGRDL-TLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRlDLEERKKVETEA 419
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIrKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK-KAEEKKKADEAK 1308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 420 KIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKlegelteEVEMAKRRIDEINKELNQVMEQlgdARIDRQESSRQQR 499
Cdd:PTZ00121 1309 KKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKK-------AAEAAKAEAEAAADEAEAAEEK---AEAAEKKKEEAKK 1378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 500 KAEIMEsikrlypgsvygrlidlcqptQKKYQIAVTKVLGKNmdaiiVDSEKTGRDCIQYIKEQRGEPEtflpldylEVK 579
Cdd:PTZ00121 1379 KADAAK---------------------KKAEEKKKADEAKKK-----AEEDKKKADELKKAAAAKKKAD--------EAK 1424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 580 PTDEKLRELKGAKLVIDVIRYEPPHIKKAlqyacgnalvcdnvEDARRIAFGGHQRHKTVALDGTlfQKSGVISGGASDL 659
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKA--------------EEAKKAEEAKKKAEEAKKADEA--KKKAEEAKKADEA 1488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 660 KAKARRWDEKAVDKLKEKKERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLES 739
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 740 ELANFGPRINDIKRIIQSREREMKDLKEKMNQVEDEvfeefcREIGVRNIREFEEEKVK----RQNEIAKKRLEFENQKT 815
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE------KKMKAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKE 1642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 816 RLGIQlDFEKNQLKEDQDKVHMWEQTVKKDEN--EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNhEMEE 893
Cdd:PTZ00121 1643 AEEKK-KAEELKKAEEENKIKAAEEAKKAEEDkkKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEE 1720
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907203694 894 IRKKLGGANKEMTHLQKEVTAIETKLEQKRSD---RHNLLQACKMQDIKLPLSKGTMDDISQEEGSSQGEESVSGSQRT 969
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeeKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
156-476 |
3.27e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 156 EEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEI 235
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 236 EKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQyiKAKENTSHKIKKLEAA 315
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE--EDEKKAAEALKKEAEE 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 316 KKSLQNAQKHYKKRKGDMDELEKEMlSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEK 395
Cdd:PTZ00121 1701 AKKAEELKKKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 396 FNRD--QKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEI 473
Cdd:PTZ00121 1780 VIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNE 1859
|
...
gi 1907203694 474 NKE 476
Cdd:PTZ00121 1860 NGE 1862
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
163-439 |
3.53e-06 |
|
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: 50.89 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 163 ELAQEYDKRKKeMVKAEEDTQFNYHRKKNIAAERKEAKQEKE-EADRYQRLKDEVVRAQVQLQLFKLYHNEV-EIEKLNK 240
Cdd:pfam17380 307 EKAREVERRRK-LEEAEKARQAEMDRQAAIYAEQERMAMERErELERIRQEERKRELERIRQEEIAMEISRMrELERLQM 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 241 ELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEiKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKK--S 318
Cdd:pfam17380 386 ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE-QEEARQREVRRLEEERAREMERVRLEEQERQQQveR 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 319 LQNAQKHYKKRKGDMDELEKEMLSVEKAR-----QEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQ-- 391
Cdd:pfam17380 465 LRQQEEERKRKKLELEKEKRDRKRAEEQRrkileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERrk 544
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907203694 392 ELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLE 439
Cdd:pfam17380 545 QQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-510 |
3.54e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 333 MDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRL---KEEASKRAATLAQELEKFNRD----QKADQD 405
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELqeeLEELEEELEELEAELEELREEleklEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 406 RLDLEERKKVETE--------AKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEG--------ELTEEVEMAKRR 469
Cdd:COG4717 128 LPLYQELEALEAElaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907203694 470 IDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:COG4717 208 LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
281-503 |
3.62e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 281 EKEIKEKDSELNQKRPQYIKAKENT--SHKIKKLEAAKKSLQNAQKhykkrkgdMDELEKEMLSVEKARQEFEERMEEES 358
Cdd:TIGR00606 844 KIELNRKLIQDQQEQIQHLKSKTNElkSEKLQIGTNLQRRQQFEEQ--------LVELSTEVQSLIREIKDAKEQDSPLE 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 359 QSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRL-DLEERKKVETEAKIKQKLREIEENQKRIEK 437
Cdd:TIGR00606 916 TFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIqDGKDDYLKQKETELNTVNAQLEECEKHQEK 995
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907203694 438 LEEYITTSKQSLEEQKKLEGELTEEVEMAKRR--IDEINKELNQVMEQLGDARIDRQESSRQQRKAEI 503
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQDNLTLRKREneLKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENI 1063
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-65 |
6.55e-06 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 47.24 E-value: 6.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907203694 8 EIENF-KSYKGRQIIGPFQ------RFTAIIGPNGSGKSNLMDAISFVL----------GEKTSNLRVKTLRDLI 65
Cdd:cd00267 1 EIENLsFRYGGRTALDNVSltlkagEIVALVGPNGSGKSTLLRAIAGLLkptsgeilidGKDIAKLPLEELRRRI 75
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
149-510 |
8.67e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 8.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 149 KERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNiaaERKEAKQEKEEA-DRYQRLKDEVVRAQVQLQLFK 227
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE---ELEELEEELEELeAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 228 LYHnevEIEKLNKELASKNKEIEKDKKRMDKVEDelkekkkelgkMMREQQQIEKEIKEKDSELNQ--------KRPQYI 299
Cdd:COG4717 130 LYQ---ELEALEAELAELPERLEELEERLEELRE-----------LEEELEELEAELAELQEELEElleqlslaTEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 300 KAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQS------------------- 360
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllslilti 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 361 -----------------QGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRL-----DLEERKKVETE 418
Cdd:COG4717 276 agvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 419 AKIKQKLREIEENQKRIEKL-EEYITTSKQSLE---EQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQES 494
Cdd:COG4717 356 AEELEEELQLEELEQEIAALlAEAGVEDEEELRaalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELE 435
|
410
....*....|....*.
gi 1907203694 495 SRQQRKAEIMESIKRL 510
Cdd:COG4717 436 ELEEELEELEEELEEL 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
275-501 |
2.16e-05 |
|
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: 47.84 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 275 REQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEK---ARQEFE 351
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 352 ERMEEESQSQGRDLTLEenqvkkyHRLKEEASKRAATLAQELEKFNRDQKADQDRLdleerkkVETEAKIKQKLREIEEN 431
Cdd:COG4942 107 AELLRALYRLGRQPPLA-------LLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-------RADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907203694 432 QKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKA 501
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAliARLEAEAAAAAERTP 244
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
7-65 |
2.38e-05 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 46.44 E-value: 2.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907203694 7 IEIENFKSYKGRQI-IGPfqRFTAIIGPNGSGKSNLMDAISFVLGEKTSNL-RVKTLRDLI 65
Cdd:cd03276 4 ITLKNFMCHRHLQIeFGP--RVNFIVGNNGSGKSAILTALTIGLGGKASDTnRGSSLKDLI 62
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
24-124 |
2.42e-05 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213208 [Multi-domain] Cd Length: 276 Bit Score: 47.20 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 24 FQR-FTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKT--LRDLIHGAPVGKPAANRAFVSMVYSEEGAEDRTFARVI-V 99
Cdd:cd03241 19 FEEgLTVLTGETGAGKSILLDALSLLLGGRASADLIRSgaEKAVVEGVFDISDEEEAKALLLELGIEDDDDLIIRREIsR 98
|
90 100
....*....|....*....|....*
gi 1907203694 100 GGSSEYKINNKVVQLHEYSEELEKL 124
Cdd:cd03241 99 KGRSRYFINGQSVTLKLLRELGSLL 123
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-46 |
2.47e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 47.00 E-value: 2.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1907203694 7 IEIEN-FKSYKGRQIIG------PFQRFTAIIGPNGSGKSNLMDAIS 46
Cdd:COG4604 2 IEIKNvSKRYGGKVVLDdvsltiPKGGITALIGPNGAGKSTLLSMIS 48
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-510 |
2.76e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 4 LKLIEIENFKSYKGRQIigpfqRFTA----IIGPNGSGKSNLMDAISFVL-GEKTSNLRVKTLRDLIhgapvgKPAANRA 78
Cdd:PRK03918 3 IEELKIKNFRSHKSSVV-----EFDDginlIIGQNGSGKSSILEAILVGLyWGHGSKPKGLKKDDFT------RIGGSGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 79 FVSMVYSEEGaEDRTFARVIVGGSSEYKINNKVVQLHE----YSEELEKLGILIKARNFL-VFQGAVESIaMKNPKERTA 153
Cdd:PRK03918 72 EIELKFEKNG-RKYRIVRSFNRGESYLKYLDGSEVLEEgdssVREWVERLIPYHVFLNAIyIRQGEIDAI-LESDESREK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 154 LFEEISRSGELAQEYD---KRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRaQVQLQLFKLYH 230
Cdd:PRK03918 150 VVRQILGLDDYENAYKnlgEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELP-ELREELEKLEK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 231 NEVEIEKLNKELASKNKEIEKDKKRMDKVEDELkekkkelgkmmreqQQIEKEIKEKDSELNqkrpqyikakentshKIK 310
Cdd:PRK03918 229 EVKELEELKEEIEELEKELESLEGSKRKLEEKI--------------RELEERIEELKKEIE---------------ELE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 311 KLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKaRQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLA 390
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEK-RLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 391 QELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRI 470
Cdd:PRK03918 359 ERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC 438
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1907203694 471 DEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:PRK03918 439 PVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKL 478
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
5-479 |
3.12e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 47.81 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 5 KLIEIENFKSYKGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKTLRdlIHGAPVGKPAA----NRAFV 80
Cdd:COG4694 4 KIKKLKNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFE--IEAGGSAPNPSvrvfNRDFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 81 SM-VYSEEGAEDrtfaRVIVGGSS---EYKINNKVVQLHEYSEELEKLGILIKARNflvfqGAVESIAMKNPKERTALFE 156
Cdd:COG4694 82 EEnLRSGEEIKG----IFTLGEENielEEEIEELEKEIEDLKKELDKLEKELKEAK-----KALEKLLEDLAKSIKDDLK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 157 EISRSGElaQEYDKRK-KEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADrYQRLKDEVVRAQVQLQlfklyhnEVEI 235
Cdd:COG4694 153 KLFASSG--RNYRKANlEKKLSALKSSSEDELKEKLKLLKEEEPEPIAPITP-LPDLKALLSEAETLLE-------KSAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 236 EKLNKELASKNKEIEKD------KKRMDKVEdelkekkkelgkmmRE-----QQQIEKEIKEK-DSELNQkrpQYIKAKE 303
Cdd:COG4694 223 SSAIEELAALIQNPGNSdwveqgLAYHKEEE--------------DDtcpfcQQELAAERIEAlEAYFDD---EYEKLLA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 304 NTSHKIKKLEAAKKSL-----QNAQKHYKKRKGDMDELEKEMLS-VEKARQEFEERMEEESQSQGRDLTLEENQVKKyhr 377
Cdd:COG4694 286 ALKDLLEELESAINALsalllEILRTLLPSAKEDLKAALEALNAlLETLLAALEEKIANPSTSIDLDDQELLDELND--- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 378 LKEEASKRAATLAQELEKFnrDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEG 457
Cdd:COG4694 363 LIAALNALIEEHNAKIANL--KAEKEEARKKLEAHELAELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEA 440
|
490 500
....*....|....*....|..
gi 1907203694 458 ELTEEVEMAkrriDEINKELNQ 479
Cdd:COG4694 441 ELSSVDEAA----DEINEELKA 458
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
2-67 |
3.79e-05 |
|
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213244 [Multi-domain] Cd Length: 213 Bit Score: 46.05 E-value: 3.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907203694 2 GFLKLIEIENFKSYkGRQIIGPFQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNL-RVKTLRDLI-HG 67
Cdd:cd03277 1 GSIVRIKLENFVTY-DETEFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLgRAKKVGEFVkRG 67
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
281-502 |
5.62e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 281 EKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEK---ARQEFEERMEEE 357
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 358 SQSQGRDLTLEENQVkkyhrlkeeASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEK 437
Cdd:COG3883 95 LYRSGGSVSYLDVLL---------GSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907203694 438 LEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAE 502
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
231-469 |
6.71e-05 |
|
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: 46.30 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 231 NEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRpqyikakentshkiK 310
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE--------------K 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 311 KLEAAKKSLQNAQKHYKK------RKGDMDELeKEMLSVEKARQEFEERMEEESQSQGRdltleENQVKKYHRLKEEASK 384
Cdd:COG4942 91 EIAELRAELEAQKEELAEllralyRLGRQPPL-ALLLSPEDFLDAVRRLQYLKYLAPAR-----REQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 385 RAATLAQE---LEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTE 461
Cdd:COG4942 165 LRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*...
gi 1907203694 462 EVEMAKRR 469
Cdd:COG4942 245 AAGFAALK 252
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-46 |
8.98e-05 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 45.42 E-value: 8.98e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907203694 6 LIEIENFK-SYKGRQIIGP--FQ----RFTAIIGPNGSGKSNLMDAIS 46
Cdd:COG1120 1 MLEAENLSvGYGGRPVLDDvsLSlppgEVTALLGPNGSGKSTLLRALA 48
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
273-395 |
9.35e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 273 MMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEE 352
Cdd:PRK12704 66 IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE 145
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907203694 353 RMEEESQSQGRDLTLEEnqvkkyhrLKEEASKRAATLAQELEK 395
Cdd:PRK12704 146 RISGLTAEEAKEILLEK--------VEEEARHEAAVLIKEIEE 180
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-510 |
1.02e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 156 EEISRSGELAQEYDKRKKEMVKAEEdtqfnyhRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEI 235
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEE-------RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 236 EKLNKELAS---KNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKenTSHKIKKL 312
Cdd:PRK03918 387 EKLEKELEElekAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEE--YTAELKRI 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 313 EAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEA---SKRAATL 389
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklKGEIKSL 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 390 AQELEKFNrDQKADQDRLDLEERKKVETEAKIKQKLRE-----IEENQKRIEKLEEY------ITTSKQSLEEQKKLEGE 458
Cdd:PRK03918 545 KKELEKLE-ELKKKLAELEKKLDELEEELAELLKELEElgfesVEELEERLKELEPFyneyleLKDAEKELEREEKELKK 623
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907203694 459 LTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSREL 675
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
413-519 |
1.37e-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: 45.53 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 413 KKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVmeqlgDARIDRQ 492
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-----EKEIAEL 95
|
90 100
....*....|....*....|....*..
gi 1907203694 493 ESSRQQRKAEIMESIKRLYPGSVYGRL 519
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPL 122
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
3-90 |
1.40e-04 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 45.42 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 3 FLKLIEIENFKSYKgrQIIGPFQ-RFTAIIGPNGSGKSNLMDAIsFVLGEkTSNLRVKTLRDLI-HGAPvgkpaanRAFV 80
Cdd:TIGR00611 2 YLSRLELTDFRNYD--AVDLELSpGVNVIVGPNGQGKTNLLEAI-YYLAL-GRSHRTSRDKPLIrFGAE-------AFVI 70
|
90
....*....|
gi 1907203694 81 SMVYSEEGAE 90
Cdd:TIGR00611 71 EGRVSKGDRE 80
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
371-510 |
1.63e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 371 QVKKYHRLKEEASKRAATLAQELEKFnrdQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLE 450
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIRELA---ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907203694 451 EQKKLEGELTEEVEMAKRRIDEI-NKELNQVMEQLGDARIDRQEssRQQRKAEIMESIKRL 510
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEE--RERRRARLEALLAAL 371
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
276-511 |
1.69e-04 |
|
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: 45.50 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 276 EQQQIEKEIKEKDSELNQKRPqyIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERME 355
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRK--LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 356 EESQSQGRdLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRI 435
Cdd:pfam17380 375 SRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRL 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907203694 436 EKLE--EYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDrQESSRQQRKAEIMESIKRLY 511
Cdd:pfam17380 454 EEQErqQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE-EERKRKLLEKEMEERQKAIY 530
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
7-49 |
2.14e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 44.19 E-value: 2.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1907203694 7 IEIENFKSYKGRQIigPFQRFTAIIGPNGSGKSNLMDAISFVL 49
Cdd:COG4938 4 ISIKNFGPFKEAEL--ELKPLTLLIGPNGSGKSTLIQALLLLL 44
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
150-500 |
2.47e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.42 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 150 ERTALFEEISRSGELaQEYDKRKKEMVKaeEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLY 229
Cdd:PTZ00108 1012 SNKVRFIKHVINGEL-VITNAKKKDLVK--ELKKLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSY 1088
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 230 H----------NEVEIEKLNKELASKNKEIEKDKKRmdkvedelkekkkELGKM-MREQQQIEKEIKEKDSELNQKRPQY 298
Cdd:PTZ00108 1089 DyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNT-------------TPKDMwLEDLDKFEEALEEQEEVEEKEIAKE 1155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 299 IKAKENTSHKIKKLEAAKKSLQNAQKHYK---KRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKY 375
Cdd:PTZ00108 1156 QRLKSKTKGKASKLRKPKLKKKEKKKKKSsadKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKP 1235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 376 HRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKL 455
Cdd:PTZ00108 1236 KKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLE 1315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907203694 456 EGELTEEVEMAKRRIDEINKELNQVMEQLGDARIDRQESSRQQRK 500
Cdd:PTZ00108 1316 GSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRPRKKK 1360
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-46 |
2.58e-04 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 42.81 E-value: 2.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907203694 8 EIEN-FKSYKGRQIIGPFQ------RFTAIIGPNGSGKSNLMDAIS 46
Cdd:cd03214 1 EVENlSVGYGGRTVLDDLSlsieagEIVGILGPNGAGKSTLLKTLA 46
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
141-926 |
2.83e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 141 ESIAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQRLKdevvraq 220
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIAR------- 1158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 221 vqlqlfklyhnevEIEKLNKELASKNKEiekDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIK 300
Cdd:PTZ00121 1159 -------------KAEDARKAEEARKAE---DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 301 AKEntSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSqgrDLTLEENQVKKYHRLKE 380
Cdd:PTZ00121 1223 AKK--AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---DELKKAEEKKKADEAKK 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 381 EASKRAATLAQEleKFNRDQKADQDRLDLEERKKVETEAKIKQ---------KLREIEENQKRIEKLEEYITTSKQSLEE 451
Cdd:PTZ00121 1298 AEEKKKADEAKK--KAEEAKKADEAKKKAEEAKKKADAAKKKAeeakkaaeaAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 452 QKKLEGELTEEVEmAKRRIDEINK---ELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRLYPGSVYGRLIDlcqPTQK 528
Cdd:PTZ00121 1376 AKKKADAAKKKAE-EKKKADEAKKkaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD---EAKK 1451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 529 KyqiavtkvlgknmdaiiVDSEKTGRDCIQYIKEQRGEPEtfLPLDYLEVKPTDEKLRELKGAKLVIDVIRYEPPHIKKA 608
Cdd:PTZ00121 1452 K-----------------AEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 609 lqyacgnalvcDNVEDARRIAFGGHQRHKTVALDGTLFQKSGVISGGASDLKAKARRwdeKAVDKLKEKKERLTEELKEQ 688
Cdd:PTZ00121 1513 -----------DEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK---KAEEKKKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 689 mkAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHlalnlQEKSKLESELANfgpRINDIKRIIQSREREMKDLKEK 768
Cdd:PTZ00121 1579 --ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-----AEEAKIKAEELK---KAEEEKKKVEQLKKKEAEEKKK 1648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 769 MNQVEDEvfEEFCREIGVRNIREFEEEkvKRQNEIAKKRLEFENQKtrlgiqldfeKNQLKEDQDKVHMWEQTVKKDENE 848
Cdd:PTZ00121 1649 AEELKKA--EEENKIKAAEEAKKAEED--KKKAEEAKKAEEDEKKA----------AEALKKEAEEAKKAEELKKKEAEE 1714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 849 I---EKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKN---HEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQK 922
Cdd:PTZ00121 1715 KkkaEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKkiaHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRM 1794
|
....
gi 1907203694 923 RSDR 926
Cdd:PTZ00121 1795 EVDK 1798
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
377-509 |
2.90e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 377 RLKEEASKRAATLAQELEKFNRDQkadqdrldlEERKKVETEAKIKQKLREIEENQKRIEKLEE-------YITTSKQSL 449
Cdd:PRK12704 42 RILEEAKKEAEAIKKEALLEAKEE---------IHKLRNEFEKELRERRNELQKLEKRLLQKEEnldrkleLLEKREEEL 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907203694 450 EEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLG-----DARIDRQESSRQQRKAEIMESIKR 509
Cdd:PRK12704 113 EKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeEAKEILLEKVEEEARHEAAVLIKE 177
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
660-928 |
2.94e-04 |
|
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: 44.73 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 660 KAKARRWDEKAVDKLKEKKERL-TEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLE 738
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 739 SElanfgprindikriiQSREREMKDLKEKMNQVEDEVFEefcreigvrniREFEEEKVKRQNEIAKKRLEFENQKTRLG 818
Cdd:pfam17380 362 LE---------------RIRQEEIAMEISRMRELERLQME-----------RQQKNERVRQELEAARKVKILEEERQRKI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 819 IQLDFEKNQLKEDQDKVHMWEQTVKKDEN--EIEKLKKEEQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRK 896
Cdd:pfam17380 416 QQQKVEMEQIRAEQEEARQREVRRLEEERarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRK 495
|
250 260 270
....*....|....*....|....*....|....*
gi 1907203694 897 KLggaNKEMTHLQKEVTAIETK---LEQKRSDRHN 928
Cdd:pfam17380 496 IL---EKELEERKQAMIEEERKrklLEKEMEERQK 527
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
371-511 |
3.30e-04 |
|
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: 43.37 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 371 QVKKYHRLKEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQK---------LREIEENQKRIEKLEEY 441
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLKRRISDLEDE 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 442 ITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLgDARIDRQESSRQQRKAEIMESIKRLY 511
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL-EAELEELEAEREELAAKIPPELLALY 180
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
336-485 |
3.66e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 336 LEKEMlsvEKARQEFEERMEEESQSQGRDLTLEENQVKKY----HRLKEEASKRAATLAqELEKFNRDQKADQDRLDLEE 411
Cdd:COG2433 382 LEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLeeqvERLEAEVEELEAELE-EKDERIERLERELSEARSEE 457
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907203694 412 RKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKE-LNQVMEQLG 485
Cdd:COG2433 458 RREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEaIRRLEEEYG 532
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-80 |
4.19e-04 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 43.15 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 1 MGFLKLIEIEN--FkSYKGRQII---------GpfqRFTAIIGPNGSGKSNLMDAIsfvLGE-KTSNLRVKtlrdlIHGA 68
Cdd:COG1121 1 MMMMPAIELENltV-SYGGRPVLedvsltippG---EFVAIVGPNGAGKSTLLKAI---LGLlPPTSGTVR-----LFGK 68
|
90
....*....|..
gi 1907203694 69 PVGKPAANRAFV 80
Cdd:COG1121 69 PPRRARRRIGYV 80
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
4-75 |
4.34e-04 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 43.44 E-value: 4.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907203694 4 LKLIEIENFKSYKGRQIigPF-QRFTAIIGPNGSGKSNLMDAISFVLGEKTsnLRVKTLRDLIHgapVGKPAA 75
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFePGVTVLVGENAQGKTNLLEAISLLATGKS--HRTSRDKELIR---WGAEEA 66
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
672-954 |
5.27e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 672 DKLKEKKERLTEELKEqmkAKRKEAELRQVQSQAHGLQMRLKysqsDLEQTKTRHLALNLqEKSKLESELANFGPRINDI 751
Cdd:PRK03918 193 ELIKEKEKELEEVLRE---INEISSELPELREELEKLEKEVK----ELEELKEEIEELEK-ELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 752 KRIIQSREREMKDLKEKMNQVED--EVFEEFcreigvRNIREFEEEKVKRQNEIakkrlefENQKTRLGIQLDFEKNQLK 829
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKElkEKAEEY------IKLSEFYEEYLDELREI-------EKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 830 EDQDKVHMWEQTVKKDENEIEKLKKEEQRHMKIidETMAQLQDLKNQHLAKKsevndKNHEMEEIRKKLGGANKEMTHLQ 909
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELY--EEAKAKKEELERLKKRL-----TGLTPEKLEKELEELEKAKEEIE 404
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907203694 910 KEVTAIETK---LEQKRSDRHNLLQACKMQDIKLPLSKGTMDDISQEE 954
Cdd:PRK03918 405 EEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKE 452
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
113-466 |
5.30e-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: 43.95 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 113 QLHEYSEELEKLGILIKARNFLVfQGAVES--IAMKNPKERTALFEEISRSGELAQEYDKRKKEMVKAEEDTQFNYHRKk 190
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSEC-QGQMERqmAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERT- 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 191 niAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYH----------NEVEIEKLNKELASKNKEIEKDKKRMDKVE 260
Cdd:pfam15921 498 --VSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknegdhlrnVQTECEALKLQMAEKDKVIEILRQQIENMT 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 261 DELKEKKKELGKMMREQQQIEKEIKEKDSELNQ----KRPQYIKAKEnTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDEL 336
Cdd:pfam15921 576 QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEfkilKDKKDAKIRE-LEARVSDLELEKVKLVNAGSERLRAVKDIKQE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 337 EKEMLSVEKarqefeermeeESQSQGRDLTLEENQVKKYHRLK-EEASKRAATLAQELEKFNRDQKADQDRLDLEE---- 411
Cdd:pfam15921 655 RDQLLNEVK-----------TSRNELNSLSEDYEVLKRNFRNKsEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdg 723
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907203694 412 ---RKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQS----LEEQKKLEGEL----TEEVEMA 466
Cdd:pfam15921 724 hamKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhflKEEKNKLSQELstvaTEKNKMA 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-510 |
5.94e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 5.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 4 LKLIEIENFKSYKGRQIIGPfQRFTAIIGPNGSGKSNLMDAISFVLGEKTSNLRVKtlrdlihgapVGKPAANRAFVSMV 83
Cdd:COG4717 3 IKELEIYGFGKFRDRTIEFS-PGLNVIYGPNEAGKSTLLAFIRAMLLERLEKEADE----------LFKPQGRKPELNLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 84 YSEEGAEDRTFARvivggSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALFEEISRSGE 163
Cdd:COG4717 72 ELKELEEELKEAE-----EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 164 LAQEYDKRKKEMVKAEEDtqfnyhrkknIAAERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELA 243
Cdd:COG4717 147 RLEELEERLEELRELEEE----------LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 244 SKNKEIEKDKKRMDKVEDElkekkkelgkmmREQQQIEKEIKEKDSELN--------QKRPQYIKAKENTSHKIKKLEAA 315
Cdd:COG4717 217 EAQEELEELEEELEQLENE------------LEAAALEERLKEARLLLLiaaallalLGLGGSLLSLILTIAGVLFLVLG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 316 KKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEE-----NQVKKYHRLKEEASKRAATLa 390
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEEllellDRIEELQELLREAEELEEEL- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 391 qELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEEnqkRIEKLEEYITTSKQSLEEQKKL--EGELTEEVEMAKR 468
Cdd:COG4717 364 -QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKE---ELEELEEQLEELLGELEELLEAldEEELEEELEELEE 439
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907203694 469 RIDEINKELNQVMEQLGDARIDRQESSRQQRKAEIMESIKRL 510
Cdd:COG4717 440 ELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
378-508 |
5.98e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 378 LKEEASKRA-ATLAQELEKFNR-DQKADQDRLDLEERKKvETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEqkkl 455
Cdd:PRK00409 499 LPENIIEEAkKLIGEDKEKLNElIASLEELERELEQKAE-EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK---- 573
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907203694 456 egELTEEVEMAKRRIDEINKELNQvMEQLGDARIDRQESSRQQRK----AEIMESIK 508
Cdd:PRK00409 574 --EAQQAIKEAKKEADEIIKELRQ-LQKGGYASVKAHELIEARKRlnkaNEKKEKKK 627
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
690-921 |
6.43e-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: 43.21 E-value: 6.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 690 KAKRKEAELRQVQSQahglqmrLKYSQSDLEQTKtrhlalnlQEKSKLESELANFGPRINDIKRIIQSREREMKDLKEKM 769
Cdd:COG4942 21 AAAEAEAELEQLQQE-------IAELEKELAALK--------KEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 770 NQVEDEvfeefcreigvrnIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEI 849
Cdd:COG4942 86 AELEKE-------------IAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907203694 850 EKLKKE-------EQRHMKIIDETMAQLQDLKNQHLAKKSEVNDKNHEMEEIRKKLGGANKEMTHLQKEVTAIETKLEQ 921
Cdd:COG4942 153 EELRADlaelaalRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-46 |
6.88e-04 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 40.89 E-value: 6.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907203694 7 IEIENF-KSYKGRQIIGPFqRFT-------AIIGPNGSGKSNLMDAIS 46
Cdd:cd03221 1 IELENLsKTYGGKLLLKDI-SLTinpgdriGLVGRNGAGKSTLLKLIA 47
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
235-477 |
1.30e-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: 42.90 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 235 IEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQiekeikEKDsELNQKRPQYIKAKENtshKIKKLEA 314
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS------EKD-KKNKALAERKDSANE---RLNSLEA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 315 AKKSLQNAQKHYKKR-KGDMDELEKEMLSVEKArqefeermeeesqsqgrdltLEENQVKKYHRLKEEASKRAATLAQEL 393
Cdd:pfam12128 690 QLKQLDKKHQAWLEEqKEQKREARTEKQAYWQV--------------------VEGALDAQLALLKAAIAARRSGAKAEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 394 EKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEY---------------ITTSKQSLEEQKKLEGE 458
Cdd:pfam12128 750 KALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYfdwyqetwlqrrprlATQLSNIERAISELQQQ 829
|
250
....*....|....*....
gi 1907203694 459 LTEEVEMAKRRIDEINKEL 477
Cdd:pfam12128 830 LARLIADTKLRRAKLEMER 848
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
657-878 |
1.48e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 657 SDLKAKARRWDEKAVDKlkekkeRLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSK 736
Cdd:COG4913 255 EPIRELAERYAAARERL------AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 737 LESELANFGPRINDIKRIIQSREREMKDLKEKMNQvedevFEEFCREIGVrnirefeeekvkrqnEIAKKRLEFENQKTR 816
Cdd:COG4913 329 EAQIRGNGGDRLEQLEREIERLERELEERERRRAR-----LEALLAALGL---------------PLPASAEEFAALRAE 388
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907203694 817 LGIQLDFEKNQLKEDQDKVHMWEQTVKKDENEIEKLKKE----EQRHmKIIDETMAQLQDLKNQHL 878
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEiaslERRK-SNIPARLLALRDALAEAL 453
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
27-45 |
1.56e-03 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 40.98 E-value: 1.56e-03
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
276-510 |
1.69e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 276 EQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQ---KHYKKRKGDMDELEKEMLSV-EKARQEFE 351
Cdd:PRK02224 193 KAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLrETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 352 ERMEEESQSQGRDLTLEEnqvkkyhrLKEEASKRAATLAQElekfNRDQKADQDRLDLEERKKVETEAKIKQKLREIEEN 431
Cdd:PRK02224 273 EREELAEEVRDLRERLEE--------LEEERDDLLAEAGLD----DADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 432 QKRIEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKR-------RIDEINKELNQVMEQLGDARIDRQES-----SRQQR 499
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREavedrreEIEELEEEIEELRERFGDAPVDLGNAedfleELREE 420
|
250
....*....|.
gi 1907203694 500 KAEIMESIKRL 510
Cdd:PRK02224 421 RDELREREAEL 431
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
193-434 |
1.73e-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: 42.06 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 193 AAERKEAKQEKEEadryqrlkdevVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGK 272
Cdd:COG4942 19 ADAAAEAEAELEQ-----------LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 273 MMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKI----KKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQ 348
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 349 EFEERMEEESQsqgrdltLEENQVKKYHRLKEEASKRAATLAQelekFNRDQKADQDRLDLEERKKVETEAKIKQKLREI 428
Cdd:COG4942 168 ELEAERAELEA-------LLAELEEERAALEALKAERQKLLAR----LEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*.
gi 1907203694 429 EENQKR 434
Cdd:COG4942 237 AAAAER 242
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
26-46 |
1.79e-03 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 41.25 E-value: 1.79e-03
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
166-475 |
1.87e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 166 QEYDKRKKEMVKAEEDTQFNYHRKKNIAAERKEAKQEKEEADRYQrlkdEVVRAQVQLQLFKLYHNEVEIEKLNKELASK 245
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIA----EELKGKEQELIFLLQAREKEIHDLEIQLTAI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 246 NKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKH 325
Cdd:pfam05483 463 KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 326 YKKRKGDMDELEKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRAATLAQELEKFNRDQKADQD 405
Cdd:pfam05483 543 EMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 406 RLDLEERKKVETEAKIKQKLREIEENQkriEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINK 475
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELELASAK---QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
118-462 |
1.88e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.15 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 118 SEELEKLGILiKARNFLVFQGA--VESIAMKNPKERTALFeeiSRSGELAQEYDKRKKEMVKAEEDTQFNYHRKKNIAAE 195
Cdd:PLN03229 390 TEELLKHRML-KFRKIGGFQEGvpVDPERKVNMKKREAVK---TPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 196 R--KEAKQEKEEA-------DRYQRLKDEVVRAQVQLQLFklyhNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEK 266
Cdd:PLN03229 466 KlkKEIDLEYTEAviamglqERLENLREEFSKANSQDQLM----HPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMLN 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 267 KKELGKMMREQQQIEKEIKekdSELNQKRPQYIKAKEntshkIK-KLEAAKKSLQNAQKhykKRKGDMDELEKEmlSVEK 345
Cdd:PLN03229 542 EFSRAKALSEKKSKAEKLK---AEINKKFKEVMDRPE-----IKeKMEALKAEVASSGA---SSGDELDDDLKE--KVEK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 346 ARQEFEERMEEESQSQGRDL-------------TLEENQVKKYHRLKEEASK------RAATLAQELEKFNRDQKADQDR 406
Cdd:PLN03229 609 MKKEIELELAGVLKSMGLEVigvtkknkdtaeqTPPPNLQEKIESLNEEINKkierviRSSDLKSKIELLKLEVAKASKT 688
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907203694 407 LDLEERKKVET-EAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEE 462
Cdd:PLN03229 689 PDVTEKEKIEAlEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLKND 745
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
3-54 |
1.88e-03 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433011 [Multi-domain] Cd Length: 392 Bit Score: 41.82 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907203694 3 FLKLIEIENFKSYKGRQIigPFQ-RFTAIIGPNGSGKSNLMDAISFVLGEKTS 54
Cdd:pfam13175 2 KIKSIIIKNFRCLKDTEI--DLDeDLTVLIGKNNSGKSSILEALDIFLNNKEK 52
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-46 |
2.64e-03 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 40.23 E-value: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1907203694 8 EIENFKSYKGRQII----GPFQ--RFTAIIGPNGSGKSNLMDAIS 46
Cdd:cd03213 12 TVKSSPSKSGKQLLknvsGKAKpgELTAIMGPSGAGKSTLLNALA 56
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
27-46 |
2.86e-03 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 40.50 E-value: 2.86e-03
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
391-510 |
3.28e-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: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 391 QELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE---------LTE 461
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyeaLQK 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1907203694 462 EVEMAKRRIDEINKELNQVMEQLGDAR--IDRQESSRQQRKAEIMESIKRL 510
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEeeLAELEAELAELEAELEEKKAEL 147
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
676-950 |
3.31e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 676 EKKERLTEELKEQMKAKRKEAELRQVQSQAHglQMRLKYSQSDLEQTKTRhlALNLQEKSKLESElanfgprinDIKRII 755
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEK--ENKMKDLTFLLEESRDK--ANQLEEKTKLQDE---------NLKELI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 756 QSRE---REMKDLKEKMNQ-VEDEVFEEFCREIGVRNIREFEEEKVKRQNEIAKKR-------LEFENQKTRLGIQLDFE 824
Cdd:pfam05483 289 EKKDhltKELEDIKMSLQRsMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahsfvvTEFEATTCSLEELLRTE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 825 KNQLKEDQDKVHMWEQTVKKDENEIEKLkkeeqrhMKIIDETMAQLQDLKNQhLAKKSEVNDKNHEMEEIRKKLGGANKE 904
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEM-------TKFKNNKEVELEELKKI-LAEDEKLLDEKKQFEKIAEELKGKEQE 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1907203694 905 MTHL----QKEVTAIETKLEQKRSDRHNLLQacKMQDIKLPLSKGTMDDI 950
Cdd:pfam05483 441 LIFLlqarEKEIHDLEIQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNI 488
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-46 |
6.03e-03 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 39.75 E-value: 6.03e-03
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
679-876 |
6.16e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 679 ERLTEELKEQMKAKRKEAELRQVQSQAHGLQMRLKYSQSDLEQTKTRHLALNLQEKSKLESELANFGPRINDIKRIIQSR 758
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 759 E--REMKDLKEKMNQVEDEVfEEFCREIgvRNIREFEEEKVKRQNEIAKKRLEFENQKTRLGIQldfEKNQLKEDQDKVH 836
Cdd:COG4717 129 PlyQELEALEAELAELPERL-EELEERL--EELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907203694 837 MWEQTVKKDENEIEKLKKEEQRHMKIIDETMAQLQDLKNQ 876
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-49 |
6.21e-03 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 39.14 E-value: 6.21e-03
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
379-510 |
6.41e-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: 40.13 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 379 KEEASKRAATLAQELEKFNRDQKADQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGE 458
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907203694 459 LT---------------------EEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKAEIMESIKRL 510
Cdd:COG4942 109 LLralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRAdlAELAALRAELEAERAELEALLAEL 183
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
76-473 |
7.08e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 76 NRAFVSMVYSEEGAEDRTFARVIVGGSSEYKINNKVVQLHEYSEELEKLGILIKARNFLVFQGAVESIAMKNPKERTALF 155
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 156 EEISRSGELAQEYDKRKKEMVKAEED-TQFNYHRKKNIAAERKE---AKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHN 231
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADrVQEAQDKINEELKLLKQkidEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 232 EVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMREQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKK 311
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERL 859
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 312 LEAAKKSLQNAQKHYKKRKGDMDEL-----EKEMLSVEKARQEFEERMEEESQSQGRDLTLEENQVKKYHRLKEEASKRA 386
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLkdeleSKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 387 ATLAQELEKfnrdQKADQDRLDLEERKKVETEAKI---KQKLREIEENQKRIEKLEEYITTSKQSLEEQKKLEGELTEEV 463
Cdd:pfam02463 940 LLLEEADEK----EKEENNKEEEEERNKRLLLAKEelgKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEET 1015
|
410
....*....|
gi 1907203694 464 EMAKRRIDEI 473
Cdd:pfam02463 1016 CQRLKEFLEL 1025
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
213-467 |
7.34e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 213 KDEVVRAqvqLQLFKLYH-NEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMMR-EQQQIEKEIKEKDSE 290
Cdd:PRK05771 18 KDEVLEA---LHELGVVHiEDLKEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvSVKSLEELIKDVEEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 291 LNQKRPQyIKAKENtshKIKKLEAAKKSLQNAQKHYKKRKG-DMD---ELEKEMLSVEKARQEFEERMEEESQSQGRDLt 366
Cdd:PRK05771 95 LEKIEKE-IKELEE---EISELENEIKELEQEIERLEPWGNfDLDlslLLGFKYVSVFVGTVPEDKLEELKLESDVENV- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 367 LEENQVKKYHR-----LKEEASKRAATLAqelekfnrdqKADQDRLDLEERKKVETEakIKQKLREIEENQKRIEKLEEY 441
Cdd:PRK05771 170 EYISTDKGYVYvvvvvLKELSDEVEEELK----------KLGFERLELEEEGTPSEL--IREIKEELEEIEKERESLLEE 237
|
250 260
....*....|....*....|....*..
gi 1907203694 442 ITTSKQSLEE-QKKLEGELTEEVEMAK 467
Cdd:PRK05771 238 LKELAKKYLEeLLALYEYLEIELERAE 264
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
380-487 |
8.44e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 39.66 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 380 EEASKRAATLAQELEKFNRDQKADQDRLDLEERK---KVETEAKIKQKlREIEENQKRIEKL-EEYITTSKQSLEEQKKL 455
Cdd:cd22656 131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKAlkdLLTDEGGAIAR-KEIKDLQKELEKLnEEYAAKLKAKIDELKAL 209
|
90 100 110
....*....|....*....|....*....|....*
gi 1907203694 456 EGELTEEVEMAKR---RIDEINKELNQVMEQLGDA 487
Cdd:cd22656 210 IADDEAKLAAALRliaDLTAADTDLDNLLALIGPA 244
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
362-502 |
8.79e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.99 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 362 GRDLTLEENQVKKYHRLKEEASKRAATLAQELEKfnrdqkaDQDRLDLEERKKVETEAKIKQKLREIEENQKRIEKLEEY 441
Cdd:pfam05262 191 EKGVNFRRDMTDLKERESQEDAKRAQQLKEELDK-------KQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907203694 442 ITTskQSLEEQKKLEGELTEEVEMAKRRIDEINKELNQVMEQLGD--ARIDRQESSRQQRKAE 502
Cdd:pfam05262 264 ADT--SSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFdlKQESKASEKEAEDKEL 324
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-477 |
9.01e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 195 ERKEAKQEKEEADRYQRLKDEVVRAQVQLQLFKLYHNEVEIEKLNKELASKNKEIEKDKKRMDKVEDELKEKKKELGKMM 274
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 275 REQQQIEKEIKEKDSELNQKRPQYIKAKENTSHKIKKLEAAKKSLQNAQKHYKKRKGDMDELEKEMLSVEKARQEFEERM 354
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907203694 355 EEESQSQgrdltlEENQVKKYHRLKEEASKRAATLAQELEKfnrdqkaDQDRLDLEERKKVETEAKIKQKLREIEENQKR 434
Cdd:TIGR04523 562 EIDEKNK------EIEELKQTQKSLKKKQEEKQELIDQKEK-------EKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907203694 435 IEKLEEYITTSKQSLEEQKKLEGELTEEVEMAKRRIDEINKEL 477
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKES 671
|
|
| |
