|
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 ... |
2-1208 |
0e+00 |
|
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: 596.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 2 YIKRVIIKGFKTYRnETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDD-YSNLKREERQGLIHQGSGGSVMSASVEI 80
Cdd:pfam02463 1 YLKRIEIEGFKSYA-KTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERsAKSLRSERLSDLIHSKSGAFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 81 VFHDPDHSmilpsgvLSRGDDEVTIRRTVGLKKD-DYQLNDRNVTKGDIVRMLETAGFSMNNPYNIVPQGKIVALTNAKD 159
Cdd:pfam02463 80 TFDNEDHE-------LPIDKEEVSIRRRVYRGGDsEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 160 KERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYDREL 239
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 240 NEVINQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLTNVNVKIKD 319
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 320 VQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLILKKGEYARFKSKDER 399
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 400 DTWIHSEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTKGQLEDFDSELIHLKQKLSESLDTR 479
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 480 KELWRKEQKLQTVLETLLSDVNQNQRNVNETMSRSLANGIINVKEITEKLKISPESVFGTLGELIKVNDKYKTCAEVIGG 559
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVE 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 560 NSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRLSLDSDVKFPSNTTTQiqftplikkikyeprfekavkhvfgkti 639
Cdd:pfam02463 553 VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILN---------------------------- 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 640 vvkdlgqglklakKHKLNAITLDGDRADKRGVLTGGYLDQHKRTRLESLKNLNESRSQHKKILEELDFVRNELNDIDTKI 719
Cdd:pfam02463 605 -------------LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 720 DQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTFAQEKLNTFENDLLQEFDSELSK 799
Cdd:pfam02463 672 TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE 751
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 800 EEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELESKLIPQENDLESKMSEVGDAFIFGLQDELKELQLEKES 879
Cdd:pfam02463 752 EEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIK 831
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 880 VEKQHENAVLELGTVQREIESLIAEETNNKKLLEKANNQQRLLLKKLDNFQKSVEKTMIKKTTLVTRREELQQRIREIGL 959
Cdd:pfam02463 832 EEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNL 911
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 960 LPEDALVNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERASELDESKDSIQDLIVKLKQQKVN 1039
Cdd:pfam02463 912 LEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1040 AVDSTFQKVSENFEAVFERLVPRGTAKLIIHRKNDNANDHDESIDVDMDAESNESQNGKDSEIMYTGVSISVSFNSKQNE 1119
Cdd:pfam02463 992 KDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKG 1071
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1120 QLHVEQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVADKFFR 1199
Cdd:pfam02463 1072 VKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVG 1151
|
1210
....*....|
gi 6322387 1200 V-KYENKIST 1208
Cdd:pfam02463 1152 VtMVENGVST 1161
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-1196 |
8.07e-110 |
|
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: 372.48 E-value: 8.07e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 2 YIKRVIIKGFKTYRNETIIdNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREER-QGLIHQGSGG-SVMSASVE 79
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERlSDLISNGKNGqSGNEAYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 80 IVFHDPDhsmilpsgvlSRGDDEVTIRRTVGLKKDD----YQLNDRNVTKGDIVRMLETAGFSMNNpYNIVPQGKIVALT 155
Cdd:TIGR02169 80 VTFKNDD----------GKFPDELEVVRRLKVTDDGkysyYYLNGQRVRLSEIHDFLAAAGIYPEG-YNVVLQGDVTDFI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 156 NAKDKERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLY 235
Cdd:TIGR02169 149 SMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 236 DRELNEVINQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSsiEASLKIKNATDLQQAKLR------ESEISQK 309
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE--ELNKKIKDLGEEEQLRVKekigelEAEIASL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 310 LTNVNVK---IKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLilk 386
Cdd:TIGR02169 307 ERSIAEKereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET--- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 387 kgeYARFKSKDERDTWIHSEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDsingpdtkgQLEDFDSELI 466
Cdd:TIGR02169 384 ---RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE---------EKEDKALEIK 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 467 HLKQKLSESLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVN--ETMSRSLANGIINVKEITEKLKISPESVFGTLGELI 544
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAeaEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLG 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 545 KVNDKYKTCAEVIGGNSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRLSLDSDVKFPSNTTTQIQFtpLIKKIKYE 624
Cdd:TIGR02169 532 SVGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGF--AVDLVEFD 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 625 PRFEKAVKHVFGKTIVVKDLGQGLKLAKKHKLnaITLDGDRADKRGVLTGGYLD---------------QHKRTRLESLK 689
Cdd:TIGR02169 610 PKYEPAFKYVFGDTLVVEDIEAARRLMGKYRM--VTLEGELFEKSGAMTGGSRAprggilfsrsepaelQRLRERLEGLK 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 690 NLNESrsqhkkILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKLE 769
Cdd:TIGR02169 688 RELSS------LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 770 KLNTNRTFAQEKLNTFEndllqefdSELSKEEKERLESLTKEISAAHNKLNITSDALEGItttIDSLNAELESKLiPQEN 849
Cdd:TIGR02169 762 ELEARIEELEEDLHKLE--------EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEAR---LREIEQKLNRLT-LEKE 829
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 850 DLESKMSEvgdafifgLQDELKELQLEKESVEKQHENAVLELGTVQREIE-------SLIAEETNNKKLLEKANNQQRLL 922
Cdd:TIGR02169 830 YLEKEIQE--------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEeleaalrDLESRLGDLKKERDELEAQLREL 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 923 LKKLDNFQKSVEKTMIKKTTLVTRREELQQRIREIGLLPEDALVNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFENF 1002
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEY 981
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1003 KKFNERRKDLAERASELDESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAVFERLvPRGTAKLIIhrknDNANDHDES 1082
Cdd:TIGR02169 982 EEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAEL-SGGTGELIL----ENPDDPFAG 1056
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1083 idvdmdaesnesqngkdseimytGVSISVSFNSKQNEQLhvEQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDK 1162
Cdd:TIGR02169 1057 -----------------------GLELSAKPKGKPVQRL--EAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDG 1111
|
1210 1220 1230
....*....|....*....|....*....|....
gi 6322387 1163 QYRTAVATLLKELSKNAQFICTTFRTDMLQVADK 1196
Cdd:TIGR02169 1112 VNVERVAKLIREKAGEAQFIVVSLRSPMIEYADR 1145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-1212 |
2.09e-97 |
|
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: 337.80 E-value: 2.09e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 2 YIKRVIIKGFKTYRNETIIdNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDD-YSNLKREERQGLIHQGSGG--SVMSASV 78
Cdd:TIGR02168 1 RLKKLELAGFKSFADPTTI-NFDKGITGIVGPNGCGKSNIVDAIRWVLGEQsAKALRGGKMEDVIFNGSETrkPLSLAEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 79 EIVFHDPDHsmILPSGvlsrGDDEVTIRRTVGLKKD-DYQLNDRNVTKGDIVRMLETAGFSmNNPYNIVPQGKIVALTNA 157
Cdd:TIGR02168 80 ELVFDNSDG--LLPGA----DYSEISITRRLYRDGEsEYFINGQPCRLKDIQDLFLDTGLG-KRSYSIIEQGKISEIIEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 158 KDKERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYDR 237
Cdd:TIGR02168 153 KPEERRAIFEEAAGISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 238 ELNEVINQMERLDgdynntvysseqyiQELDKREDMIDQVSKKLSSIEASLkikNATDLQQAKLRES--EISQKLTNVNV 315
Cdd:TIGR02168 233 RLEELREELEELQ--------------EELKEAEEELEELTAELQELEEKL---EELRLEVSELEEEieELQKELYALAN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 316 KIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKqrdliLKKGEYARFKS 395
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----LEELEAELEEL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 396 KDERDTWiHSEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTK---GQLEDFDSELIHLKQKL 472
Cdd:TIGR02168 371 ESRLEEL-EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleeAELKELQAELEELEEEL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 473 SESLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNETMSR--SLANGIINVKEITEKLK------ISPESVFGTLGELI 544
Cdd:TIGR02168 450 EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldSLERLQENLEGFSEGVKallknqSGLSGILGVLSELI 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 545 KVNDKYKTCAEVIGGNSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRLsldSDVKFPSNTTTQIQFTP-----LIK 619
Cdd:TIGR02168 530 SVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSI---KGTEIQGNDREILKNIEgflgvAKD 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 620 KIKYEPRFEKAVKHVFGKTIVVKDLGQGLKLAKK--HKLNAITLDGDRADKRGVLTGGYLDQHKrTRLESLKNLNESRSQ 697
Cdd:TIGR02168 607 LVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrPGYRIVTLDGDLVRPGGVITGGSAKTNS-SILERRREIEELEEK 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 698 HKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTF 777
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 778 AQEKLNTfENDLLQEFDSELSKEE------KERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELESKLIPQENDL 851
Cdd:TIGR02168 766 LEERLEE-AEEELAEAEAEIEELEaqieqlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 852 ESKMSEVGDafIFGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAEETNNKKLLEKANNQQRLLLKKLDNFQK 931
Cdd:TIGR02168 845 EQIEELSED--IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 932 SVEKTMIKKTTLVTRREELQQRIREIGLLPEDALVNDFSDITSD--QLLQRLNDMNTEISGLKNVNKRAFENFKKFNERR 1009
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDeeEARRRLKRLENKIKELGPVNLAAIEEYEELKERY 1002
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1010 KDLAERASELDESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAVFERLVPRGTAKLIIHRKNDnandhdesidvdmda 1089
Cdd:TIGR02168 1003 DFLTAQKEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQRVFPKLFGGGEAELRLTDPED--------------- 1067
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1090 esnesqngkdseIMYTGVSISVSFNSKQNEQLHveQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVA 1169
Cdd:TIGR02168 1068 ------------LLEAGIEIFAQPPGKKNQNLS--LLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFA 1133
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 6322387 1170 TLLKELSKNAQFICTTFRTDMLQVADKFFRVKYENK-ISTVIEV 1212
Cdd:TIGR02168 1134 NLLKEFSKNTQFIVITHNKGTMEVADQLYGVTMQEKgVSKIVSV 1177
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
3-174 |
4.84e-84 |
|
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: 273.75 E-value: 4.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 3 IKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGLIHQGSGGSVMSASVEIVF 82
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVMSAYVEIIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 83 HDPDHSMILPsgvlsrgDDEVTIRRTVGLKKDDYQLNDRNVTKGDIVRMLETAGFSMNNPYNIVPQGKIVALTNAKDKER 162
Cdd:cd03272 81 DNSDNRFPID-------KEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQDEQ 153
|
170
....*....|..
gi 6322387 163 LQLLEDVVGAKS 174
Cdd:cd03272 154 QEMQQLSGGQKS 165
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-1182 |
4.59e-64 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 236.76 E-value: 4.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIIDnFSPHQNVIIGSNGSGKSNFFAAIRFVL---SddYSNLKREERQGLIHQGSGG--SVMS 75
Cdd:COG1196 1 MRLKRLELAGFKSFADPTTIP-FEPGITAIVGPNGSGKSNIVDAIRWVLgeqS--AKSLRGGKMEDVIFAGSSSrkPLGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 76 ASVEIVFHDPDhsmilpsGVLSRGDDEVTIRRTVGLKKD-DYQLNDRNVTKGDIVRMLETAGFSMNNpYNIVPQGKIVAL 154
Cdd:COG1196 78 AEVSLTFDNSD-------GTLPIDYDEVTITRRLYRSGEsEYYINGKPCRLKDIQDLFLDTGLGPES-YSIIGQGMIDRI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 155 TNAKDKERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTL 234
Cdd:COG1196 150 IEAKPEERRAIIEEAAGISKYKERKEEAERKLEATEENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 235 YDRELNEVINQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNAtDLQQAKLRESEISQKLTNVN 314
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA-EEYELLAELARLEQDIARLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 315 VKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLILKKGEYARFK 394
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 395 SKDERdtwihsEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINgpDTKGQLEDFDSELIHLKQKLSE 474
Cdd:COG1196 389 LEALR------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE--EEEEALEEAAEEEAELEEEEEA 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 475 SLDTRKELWRKEQKLQTVLETLLSDVNQ--NQRNVNETMSRSLANGIINVKEitEKLKISPESVFGTLGELIKVNDKYKT 552
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEaaARLLLLLEAEADYEGFLEGVKA--ALLLAGLRGLAGAVAVLIGVEAAYEA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 553 CAEVIGGNSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRLsldSDVKFPSNTTTQIQFTPLIKKIKYEPRFEKAVK 632
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI---RARAALAAALARGAIGAAVDLVASDLREADARY 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 633 HVFGKTIVVKDLGQGLKLAKKHKlnAITLDGDRADKRGVLTGGYldQHKRTRLESLKNLNESRSQHKKILEEldfvrnel 712
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRR--AVTLAGRLREVTLEGEGGS--AGGSLTGGSRRELLAALLEAEAELEE-------- 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 713 ndidtkidqvngnirkvsndresvltnievyrtslntkkneklileeslnaiilkleklntnrtfaqeklntfendllqe 792
Cdd:COG1196 --------------------------------------------------------------------------------
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 793 fdsELSKEEKERLESLTKEisaahnklnitsdalegitttidslnaelesklipqendleskmsevgdafifgLQDELKE 872
Cdd:COG1196 684 ---LAERLAEEELELEEAL------------------------------------------------------LAEEEEE 706
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 873 LQLEKESVEKQHENAVLELGTVQREIEsliaeetnnkkllekannqqrlllkkldnfqksvektmikkttlvtRREELQQ 952
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAE----------------------------------------------REELLEE 740
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 953 RIREIGLLPEDALVNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERASELDESKDSIQDLIVK 1032
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERYDFLSEQREDLEEARETLEEAIEE 820
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1033 LKQQKVNAVDSTFQKVSENFEAVFERLVPRGTAKLIIHRKNDNANdhdesidvdmdaesnesqngkdseimyTGVSISVS 1112
Cdd:COG1196 821 IDRETRERFLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLE---------------------------TGIEIMAQ 873
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322387 1113 FNSKQNEQLHveQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQ--YRtaVATLLKELSKNAQFI 1182
Cdd:COG1196 874 PPGKKLQRLS--LLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDAnvER--FAELLKEMSEDTQFI 941
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1114-1209 |
1.61e-54 |
|
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: 190.16 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1114 NSKQNEQLHVEQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQV 1193
Cdd:cd03272 147 NMKQDEQQEMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEV 226
|
90
....*....|....*.
gi 6322387 1194 ADKFFRVKYENKISTV 1209
Cdd:cd03272 227 ADKFYGVKFRNKVSTI 242
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
534-650 |
7.47e-33 |
|
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: 123.50 E-value: 7.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 534 ESVFGTLGELIKVNDKYKTCAEVIGGNSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRL---SLDSDVKFPSNTTT 610
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIkprSPAGSKLREALLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 6322387 611 QIQFTPLIKKIKYEPRFEKAVKHVFGKTIVVKDLGQGLKL 650
Cdd:smart00968 81 PGFVGPAIDLVEYDPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
534-651 |
4.08e-31 |
|
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: 118.52 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 534 ESVFGTLGELIKVNDKYKTCAEVIGGNSLFHIVVDTEETATLIMNELYRMKGGRVTFIPLNRLSLDSDvkfPSNTTTQIQ 613
Cdd:pfam06470 2 KGVLGRLADLIEVDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPR---RPGADLKGG 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 6322387 614 FTPLIKKIKYEPRFEKAVKHVFGKTIVVKDLGQGLKLA 651
Cdd:pfam06470 79 AGPLLDLVEYDDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1-174 |
3.82e-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: 100.06 E-value: 3.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLS-DDYSNLKREERQGLI-HQGSGGsVMSASV 78
Cdd:cd03273 1 MHIKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIyKRGQAG-ITKASV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 79 EIVFH--DPDHSMILPSGVlsrgdDEVTIRRTVGL-KKDDYQLNDRNVTKGDIVRMLETAGFSMNNPYNIVPQGKIVALT 155
Cdd:cd03273 80 TIVFDnsDKSQSPIGFENY-----PEITVTRQIVLgGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITKVL 154
|
170
....*....|....*....
gi 6322387 156 NAKDKERLQLLEDVVGAKS 174
Cdd:cd03273 155 NMGGVWKESLTELSGGQRS 173
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1120-1208 |
3.88e-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: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1120 QLHVEQ-LSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKN-AQFICTTFRTDMLQVADKF 1197
Cdd:cd03239 88 QGKVEQiLSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKL 167
|
90
....*....|.
gi 6322387 1198 FRVKYENKIST 1208
Cdd:cd03239 168 IGVLFVHGVST 178
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1116-1205 |
7.54e-19 |
|
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: 85.98 E-value: 7.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1116 KQNEQLHveQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVAD 1195
Cdd:cd03278 106 KKVQRLS--LLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
90
....*....|
gi 6322387 1196 KFFRVKYENK 1205
Cdd:cd03278 184 RLYGVTMQES 193
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
3-99 |
2.17e-18 |
|
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: 84.28 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 3 IKRVIIKGFKTYRNETIIDNFSPHqNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGLIHQGSGGSVMSASVEIVF 82
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSF-NAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVKAGINSASVEITF 79
|
90 100
....*....|....*....|.
gi 6322387 83 HdpDHSMILPSG----VLSRG 99
Cdd:cd03239 80 D--KSYFLVLQGkveqILSGG 98
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1125-1204 |
8.47e-18 |
|
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: 82.02 E-value: 8.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1125 QLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELS-KNAQFICTTFRTDMLQVADKFFRVKYE 1203
Cdd:cd03227 77 QLSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIKKV 156
|
.
gi 6322387 1204 N 1204
Cdd:cd03227 157 I 157
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1102-1209 |
1.69e-16 |
|
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: 80.80 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1102 IMYTGVSISVSFNSKQNEQLHveQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQF 1181
Cdd:cd03273 145 IMQGRITKVLNMGGVWKESLT--ELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQF 222
|
90 100
....*....|....*....|....*...
gi 6322387 1182 ICTTFRTDMLQVADKFFRVKYENKISTV 1209
Cdd:cd03273 223 IVVSLKEGMFNNANVLFRTRFVDGTSTV 250
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1122-1207 |
5.01e-16 |
|
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: 78.11 E-value: 5.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1122 HVEQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVADKFFRVK 1201
Cdd:cd03274 124 NISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELADRLVGIY 203
|
....*.
gi 6322387 1202 YENKIS 1207
Cdd:cd03274 204 KTNNCT 209
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
3-133 |
8.90e-14 |
|
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: 72.61 E-value: 8.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 3 IKRVIIKGFKTYRNETII---DNFSphqnVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGLIHqgsGGSVM----- 74
Cdd:cd03275 1 LKRLELENFKSYKGRHVIgpfDRFT----CIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIY---RARVGkpdsn 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 6322387 75 SASVEIVFHDPDhsmilpsgvlsrgDDEVTIRRTVGLKKDDYQLNDRNVTKGDIVRMLE 133
Cdd:cd03275 74 SAYVTAVYEDDD-------------GEEKTFRRIITGGSSSYRINGKVVSLKEYNEELE 119
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
3-210 |
2.44e-13 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 70.04 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 3 IKRVIIKGFKTYRNETIIDnFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQgLIHQGSGgsvmSASVEIVF 82
Cdd:COG0419 2 LLRLRLENFRSYRDTETID-FDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSD-LINVGSE----EASVELEF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 83 hdpdhsmilpsgvlSRGDDEVTIRRtvglkkddyqlndrnvtkgdivrmletagfsmnnpynivPQGKIVALTNAKDKER 162
Cdd:COG0419 76 --------------EHGGKRYRIER---------------------------------------RQGEFAEFLEAKPSER 102
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6322387 163 LQLLEDVVGAKSFEvKLKASLKKMEETEQKKIQINKEMGELNSK-LSEM 210
Cdd:COG0419 103 KEALKRLLGLEIYE-ELKERLKELEEALESALEELAELQKLKQEiLAQL 150
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
3-91 |
2.74e-13 |
|
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: 69.80 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 3 IKRVIIKGFKTYRNETIIdNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDD-YSNLKREERQGLIHQGSGG--SVMSASVE 79
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQsAKSLRGEKMSDVIFAGSETrkPANFAEVT 79
|
90
....*....|....
gi 6322387 80 IVFHDPDH--SMIL 91
Cdd:cd03278 80 LTFDNSDGrySIIS 93
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1123-1195 |
7.99e-13 |
|
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: 69.52 E-value: 7.99e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322387 1123 VEQLSGGQKTVCAIALILAIQMVDPASFYLFDEIDAALDKQYRTAVATLLKELS-KNAQFICTTFRTDMLQVAD 1195
Cdd:cd03275 153 MDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAgPNFQFIVISLKEEFFSKAD 226
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
3-86 |
2.97e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 63.41 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 3 IKRVIIKGFKTYRNETI-IDNFsphqNVIIGSNGSGKSNFFAAIRF---VLSDDYSNLKREER--QGLIHQGSGGSVMSA 76
Cdd:COG4637 2 ITRIRIKNFKSLRDLELpLGPL----TVLIGANGSGKSNLLDALRFlsdAARGGLQDALARRGglEELLWRGPRTITEPI 77
|
90
....*....|
gi 6322387 77 SVEIVFHDPD 86
Cdd:COG4637 78 RLELEFAEED 87
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1-82 |
4.37e-10 |
|
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: 63.10 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSN-LKREErqglIHQGSGGSVMSASVE 79
Cdd:COG3593 1 MKLEKIKIKNFRSIKDLSI--ELSDDLTVLVGENNSGKSSILEALRLLLGPSSSRkFDEED----FYLGDDPDLPEIEIE 74
|
...
gi 6322387 80 IVF 82
Cdd:COG3593 75 LTF 77
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1101-1201 |
1.80e-09 |
|
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: 57.64 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1101 EIMYTGVSISVSFNSKQNEQL-HVEQLSGGQKTVCAIALILAIQmvdpASFYLFDEIDAALDKQYRTAVATLLKELS-KN 1178
Cdd:cd00267 55 EILIDGKDIAKLPLEELRRRIgYVPQLSGGQRQRVALARALLLN----PDLLLLDEPTSGLDPASRERLLELLRELAeEG 130
|
90 100
....*....|....*....|....
gi 6322387 1179 AQFICTTFRTDMLQ-VADKFFRVK 1201
Cdd:cd00267 131 RTVIIVTHDPELAElAADRVIVLK 154
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-494 |
2.43e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDY-SNLKREERQGLIHQGSGGsvmsASVE 79
Cdd:PRK03918 1 MKIEELKIKNFRSHKSSVV--EFDDGINLIIGQNGSGKSSILEAILVGLYWGHgSKPKGLKKDDFTRIGGSG----TEIE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 80 IVF-HDPDHSMILPSgvlsrgddevTIRRTVGLKKDDYQLNDRNVTKgDIVRMLETAGfsmnnPYNI------VPQGKIV 152
Cdd:PRK03918 75 LKFeKNGRKYRIVRS----------FNRGESYLKYLDGSEVLEEGDS-SVREWVERLI-----PYHVflnaiyIRQGEID 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 153 ALTNAkDKERLQLLEDVVGAKSFEVKLKASLK------------------------KMEETEQKKIQINKEMGELNSKLS 208
Cdd:PRK03918 139 AILES-DESREKVVRQILGLDDYENAYKNLGEvikeikrrierlekfikrtenieeLIKEKEKELEEVLREINEISSELP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 209 EMEQERKELEK-YNELERNRKIyqFTLYDRELNEVINQMERLDGDYNNTvyssEQYIQELDKREDMIDQVSKKLSSIE-- 285
Cdd:PRK03918 218 ELREELEKLEKeVKELEELKEE--IEELEKELESLEGSKRKLEEKIREL----EERIEELKKEIEELEEKVKELKELKek 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 286 ASLKIKNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEqrnlDSATLKEIKSIIEQRKQKLSKILPRYQELtkE 365
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHELY--E 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 366 EAMYKL-QLASLQQKQRDLILKKGEyARFKSKDERDTWIHSEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEE 444
Cdd:PRK03918 366 EAKAKKeELERLKKRLTGLTPEKLE-KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRE 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 6322387 445 LIDSingpDTKGQLEDFDSELIHLKQKLSESLDTRKELWRKEQKLQTVLE 494
Cdd:PRK03918 445 LTEE----HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
5-71 |
2.89e-09 |
|
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: 57.37 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 5 RVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKRE--------------ERQGLIHQGSG 70
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRsgvkagcivaavsaELIFTRLQLSG 80
|
.
gi 6322387 71 G 71
Cdd:cd03227 81 G 81
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1-494 |
1.14e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.53 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIIdnFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREErqgLIHQGSGgsvmSASVEI 80
Cdd:PRK01156 1 MIIKRIRLKNFLSHDDSEIE--FDTGINIITGKNGAGKSSIVDAIRFALFTDKRTEKIED---MIKKGKN----NLEVEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 81 VFHDPDHSMILPSGVLSRGDdevTIRRTVGLKKDDYQLND--RNVTKGDIVRMLETAGFSMNNPYnIVPQGKIVALTNAK 158
Cdd:PRK01156 72 EFRIGGHVYQIRRSIERRGK---GSRREAYIKKDGSIIAEgfDDTTKYIEKNILGISKDVFLNSI-FVGQGEMDSLISGD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 159 DKERLQLLEDVVGAKSFE---VKLKASLKKM----------EETEQKKI----QINKEMGELNSKLSEMEQERKELE--- 218
Cdd:PRK01156 148 PAQRKKILDEILEINSLErnyDKLKDVIDMLraeisnidylEEKLKSSNleleNIKKQIADDEKSHSITLKEIERLSiey 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 219 ---------------KYNELERNRKIYQFTL---------YDRELNEVINQMERLDGDYNNTVYSSEQYIQELDKREDMI 274
Cdd:PRK01156 228 nnamddynnlksalnELSSLEDMKNRYESEIktaesdlsmELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 275 DQVSKKLSSIEASLK-----IKNATDLQ-------QAKLRESEISQKL-------TNVNVKIKDVQQQIESNEEQRNLDS 335
Cdd:PRK01156 308 ENKKQILSNIDAEINkyhaiIKKLSVLQkdyndyiKKKSRYDDLNNQIlelegyeMDYNSYLKSIESLKKKIEEYSKNIE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 336 ATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLILKKGEYARFKSKDERDT-----WIHSEIEEL 410
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcGTTLGEEKS 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 411 KSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELI---DSINGPDTKgQLEDFDSELIHLKQKLSESLDTRKELWRKEQ 487
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkEYLESEEIN-KSINEYNKIESARADLEDIKIKINELKDKHD 546
|
....*..
gi 6322387 488 KLQTVLE 494
Cdd:PRK01156 547 KYEEIKN 553
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
6-199 |
1.76e-08 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 55.58 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 6 VIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGLIHQG---SGGSVMSASVEIVF 82
Cdd:pfam13476 1 LTIENFRSFRDQTI--DFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDiriGLEGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 83 HDPDhsmiLPSGVLSRGDDEVTIRRTVGLKKDDYQLNDRNVTKGDIVRMLETAGFSMNNpYNIVPQGKIVALTNAKDKER 162
Cdd:pfam13476 79 ENND----GRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPL-LVFLGQEREEEFERKEKKER 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 6322387 163 LQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKE 199
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEELKEE 190
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
1-65 |
5.01e-08 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 55.77 E-value: 5.01e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322387 1 MYIKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGLI 65
Cdd:COG3950 1 MRIKSLTIENFRGFEDLEIDFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1-83 |
1.99e-07 |
|
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: 53.07 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIIDNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGLIHQGSG-GSVMSASVE 79
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGhPNLDSCSVE 80
|
....
gi 6322387 80 IVFH 83
Cdd:cd03274 81 VHFQ 84
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
160-555 |
3.44e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 160 KERLQLLEDVVGAKSFEVKLKASL---------KKMEETEQKKIQINKEMGELNSKLSEMEQERKELEK-YNELERNRKI 229
Cdd:PRK03918 358 EERHELYEEAKAKKEELERLKKRLtgltpekleKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaIEELKKAKGK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 230 yqFTLYDRELNEviNQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSI--EASLKIKNATDLQQAKlresEIS 307
Cdd:PRK03918 438 --CPVCGRELTE--EHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLK----ELE 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 308 QKLTNVNVKikdvqqQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKIlpryQELTKEEAMYKLQLASLQQKQRDLiLKK 387
Cdd:PRK03918 510 EKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAEL-LKE 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 388 GEYARFKSKDERDtwihSEIEELKSSIQNLNEL---ESQLQMDRTSLRKQYSAIDEEIEELidsingPDTKGQLEDFDSE 464
Cdd:PRK03918 579 LEELGFESVEELE----ERLKELEPFYNEYLELkdaEKELEREEKELKKLEEELDKAFEEL------AETEKRLEELRKE 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 465 LIHLKQKLSEslDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNETMS--RSLANGIINVKEITEKLKiSPESVFGTLGE 542
Cdd:PRK03918 649 LEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKtlEKLKEELEEREKAKKELE-KLEKALERVEE 725
|
410
....*....|...
gi 6322387 543 LIKVNDKYKTCAE 555
Cdd:PRK03918 726 LREKVKKYKALLK 738
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
185-392 |
3.87e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 185 KMEETEQKKIQINKEMGELNSKLSEMEQErkeLEKYnelernRKIYQFTLYDRELNEVINQMERLDGDYNNTVYSSEQYI 264
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAA---LEEF------RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 265 QELDKREDMIDQVSKKLSSIEASLKIKNA-TDLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQrnldsatlkeiks 343
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLrAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------------- 306
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6322387 344 IIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLILKKGEYAR 392
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
679-1195 |
4.80e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 679 QHKRTRLESLKNLNESRSQHKKILEELDFVRNELNDIDTKIDQvngnIRKVSNDRESVLTNIEVYRTSLNTKKNEKLI-- 756
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 757 ------LEESLNAIILKLEKLNTNRTFAQEKLNTFENDLLQEFDSELSKEEKERLESLTK---------EISAAHNKLNI 821
Cdd:COG4717 191 eeelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 822 TSDALEGITTTIDSLNAELESKLIPQENDLESKMSEVGDAFIF------GLQDELKELQLEKESVEKQHENAVLELGTVQ 895
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALeeleeeELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 896 ---REIESLIAE------ETNNKKLLEKANNQQR-LLLKKLDNFQKSVEktmikkttLVTRREELQQRIREIGLLPEDAL 965
Cdd:COG4717 351 ellREAEELEEElqleelEQEIAALLAEAGVEDEeELRAALEQAEEYQE--------LKEELEELEEQLEELLGELEELL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 966 vndfSDITSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLaERASELDESKDSIQDLIVKLKQ-----QKVNA 1040
Cdd:COG4717 423 ----EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQL-EEDGELAELLQELEELKAELRElaeewAALKL 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1041 VDSTFQKVSENFEavfERLVPRgtaklIIHRkndnANDHDESIdvdmdaesnesQNGKDSEIMYTGvSISVSFNSKQNEQ 1120
Cdd:COG4717 498 ALELLEEAREEYR---EERLPP-----VLER----ASEYFSRL-----------TDGRYRLIRIDE-DLSLKVDTEDGRT 553
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322387 1121 LHVEQLSGGQKTVCAIALILA-IQMVDPASFYLF-DEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVAD 1195
Cdd:COG4717 554 RPVEELSRGTREQLYLALRLAlAELLAGEPLPLIlDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVELFQ 630
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
164-441 |
4.91e-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: 54.36 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 164 QLLEDVVGAKSfeVKLKASLKKMEETEQKKIQINKEmgelnSKLSEMEQERK--ELEKYNELERNRKIYQFTLYDRELNE 241
Cdd:pfam17380 273 QLLHIVQHQKA--VSERQQQEKFEKMEQERLRQEKE-----EKAREVERRRKleEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 242 VINQMERLDgdynntvysseqyiQELDKREdmIDQVSKKLSSIEASlKIKNATDLQQAKLRESE-ISQKLTNVNvkikdv 320
Cdd:pfam17380 346 RERELERIR--------------QEERKRE--LERIRQEEIAMEIS-RMRELERLQMERQQKNErVRQELEAAR------ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 321 QQQIESNEEQRNL--------------DSATLKEIKSIIEQRKQKLSKIlpRYQELTKEEAMYKLQLASLQQKQRDLILK 386
Cdd:pfam17380 403 KVKILEEERQRKIqqqkvemeqiraeqEEARQREVRRLEEERAREMERV--RLEEQERQQQVERLRQQEEERKRKKLELE 480
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 6322387 387 KGEYARFKSKDERDTWIHSEIEELKssiQNLNELESQLQMDRTSLRKQYSAIDEE 441
Cdd:pfam17380 481 KEKRDRKRAEEQRRKILEKELEERK---QAMIEEERKRKLLEKEMEERQKAIYEE 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1-499 |
6.26e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYsnlkrEERQGLIHQGSGgsvmsasvei 80
Cdd:COG4717 1 MKIKELEIYGFGKFRDRTI--EFSPGLNVIYGPNEAGKSTLLAFIRAMLLERL-----EKEADELFKPQG---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 81 vfhdpdhsmILPSGVLSRGDDEVTIRRTVGLKKDDYQlndrnvtkgDIVRMLETAGFSMNNpynivpqgkiVALTNAKDK 160
Cdd:COG4717 64 ---------RKPELNLKELKELEEELKEAEEKEEEYA---------ELQEELEELEEELEE----------LEAELEELR 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 161 ERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNElERNRKIYQFTLYDREln 240
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE-ELEELLEQLSLATEE-- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 241 evinQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNatdlQQAKLRESEISQKLTNVNVKIKDV 320
Cdd:COG4717 193 ----ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA----LEERLKEARLLLLIAAALLALLGL 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 321 QQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQeltkEEAMYKLQLASLQQKQRDLILKKGEYARFKSKDERD 400
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA----EELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 401 TWIHsEIEELKSSIQNLNELESQLQMD------------------------------RTSLRKQYSAIDEEIEELIDSIN 450
Cdd:COG4717 341 ELLD-RIEELQELLREAEELEEELQLEeleqeiaallaeagvedeeelraaleqaeeYQELKEELEELEEQLEELLGELE 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 6322387 451 GPDTKGQLEDFDSELIHLKQKLSESLDTRKELWRKEQKLQTVLETLLSD 499
Cdd:COG4717 420 ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-496 |
6.49e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 6.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 156 NAKDKERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEK-----------YNELE 224
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKeieeleekvkeLKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 225 RNRKIY-QFTLYDRELNEVINQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKI------------- 290
Cdd:PRK03918 290 EKAEEYiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyeeaka 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 291 ------------------KNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIE-----------------------SNEE 329
Cdd:PRK03918 370 kkeelerlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKelkkaieelkkakgkcpvcgrelTEEH 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 330 QRNLDSATLKEIKSI-------------IEQRKQKLSKILPRYQELTKEEAMYKlQLASLQQKQRDLILKKGE--YARFK 394
Cdd:PRK03918 450 RKELLEEYTAELKRIekelkeieekerkLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLKKYNLEELEkkAEEYE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 395 SKDERDTWIHSEIEELKSSIQNLNELESQLqmdrTSLRKQYSAIDEEIEELIDSIN--GPDTKGQLEDFDSELIHLKQKL 472
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKL----AELEKKLDELEEELAELLKELEelGFESVEELEERLKELEPFYNEY 604
|
410 420
....*....|....*....|....
gi 6322387 473 SESLDTRKELWRKEQKLQTVLETL 496
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEEL 628
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
286-1119 |
1.07e-06 |
|
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: 53.30 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 286 ASLKIKNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQRnldsatLKEIKSIIEQRKQKLSKiLPRYQ-ELTK 364
Cdd:pfam12128 286 AELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQH------GAFLDADIETAAADQEQ-LPSWQsELEN 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 365 EEAMYKLQLAS---LQQKQRDLILKKGE--YARFKSKDERDTWIHSEIEELKSSIQNL-----NELESQLQMDRTSLRKQ 434
Cdd:pfam12128 359 LEERLKALTGKhqdVTAKYNRRRSKIKEqnNRDIAGIKDKLAKIREARDRQLAVAEDDlqaleSELREQLEAGKLEFNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 435 YSAIDEEIEELIDSING----PDTKGQLEDFDSELIHLKQKLSESLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNET 510
Cdd:pfam12128 439 EYRLKSRLGELKLRLNQatatPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 511 MSRslangiinVKEITEKLkiSPESvfGTLGELIKvndkyktcAEVIGGNslfhivvdtEETATLIMNELyrmkggrvtf 590
Cdd:pfam12128 519 QSA--------LDELELQL--FPQA--GTLLHFLR--------KEAPDWE---------QSIGKVISPEL---------- 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 591 ipLNRLSLDsdvkfPSNTTTQIqftplikkikyeprfekavkhvfgktivvkdlGQGLKLAkkhklnAITLDGDRADkrg 670
Cdd:pfam12128 560 --LHRTDLD-----PEVWDGSV--------------------------------GGELNLY------GVKLDLKRID--- 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 671 VLTGGYLDQHKRTRLESLKN-LNESRSQHKKILEELDFVRNELNDIDtkidqvngniRKVSNDRESVLTNIEVYRTSLNT 749
Cdd:pfam12128 592 VPEWAASEEELRERLDKAEEaLQSAREKQAAAEEQLVQANGELEKAS----------REETFARTALKNARLDLRRLFDE 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 750 KKNEKLILEESLNAIILKLEKlNTNRTFAQEKLNTFE-NDLLQEFDSELSKEEKERLESLTKEISAahnklniTSDALEG 828
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSANE-RLNSLEAQLKQLDKKhQAWLEEQKEQKREARTEKQAYWQVVEGA-------LDAQLAL 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 829 ITTTIDSL--NAELESKLIPQENDLESKMSEVGDAFIFGLQDELKELQLEKESVEK------------------QHENAV 888
Cdd:pfam12128 734 LKAAIAARrsGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVrrqevlryfdwyqetwlqRRPRLA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 889 LELGTVQREIESLiaeETNNKKLLEKAnnqqRLLLKKLDNFQKSVEKTMIKKTTLVTRreeLQQRIREIGLLPEDAlvnd 968
Cdd:pfam12128 814 TQLSNIERAISEL---QQQLARLIADT----KLRRAKLEMERKASEKQQVRLSENLRG---LRCEMSKLATLKEDA---- 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 969 fsdiTSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDL--AERASELDESKDSIQDlivklKQQKVNAVDSTFQ 1046
Cdd:pfam12128 880 ----NSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNViaDHSGSGLAETWESLRE-----EDHYQNDKGIRLL 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1047 KVSENFEAVFERLVPRGTAKLIIHRK----NDNAN----DHDESIDVDMDAESNESQNGKDSEIMYTGVS-ISVSFNSKQ 1117
Cdd:pfam12128 951 DYRKLVPYLEQWFDVRVPQSIMVLREqvsiLGVDLtefyDVLADFDRRIASFSRELQREVGEEAFFEGVSeSAVRIRSKV 1030
|
..
gi 6322387 1118 NE 1119
Cdd:pfam12128 1031 SE 1032
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-370 |
1.18e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 157 AKDKERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYD 236
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFY 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 237 RELNEVINQMERLdgdynntvyssEQYIQELDKREDMIDQVSKKLSSIEASL-KIKNATDLQQAKLRESE---ISQKLTN 312
Cdd:PRK03918 602 NEYLELKDAEKEL-----------EREEKELKKLEEELDKAFEELAETEKRLeELRKELEELEKKYSEEEyeeLREEYLE 670
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322387 313 VNVKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRK------QKLSKILPRYQELTKEEAMYK 370
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREkakkelEKLEKALERVEELREKVKKYK 734
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
286-496 |
2.20e-06 |
|
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: 51.30 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 286 ASLKIKNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKE 365
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 366 ----EAMYKLQLASLQQKQRDLILKkgeyARFKSKDERDT------------WIHSEIEELKSSIQNLNELESQLQMDRT 429
Cdd:COG4942 99 leaqKEELAELLRALYRLGRQPPLA----LLLSPEDFLDAvrrlqylkylapARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322387 430 SLRKQYSAIDEEIEELidsingpdtKGQLEDFDSELIHLKQKLSESLDTRKELWRKEQKLQTVLETL 496
Cdd:COG4942 175 ELEALLAELEEERAAL---------EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
860-1037 |
2.32e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 860 DAFIFGLQDELKELQLEKESVEKQhenavleLGTVQREIESLIAEETNNKKLLEKANNQQRLLLKKLDNFQKSVEKtmik 939
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE-------LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 940 kttlvtRREELQQRIReigllpeDALVNDFSDITSDQLL--QRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERAS 1017
Cdd:COG3883 84 ------RREELGERAR-------ALYRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180
....*....|....*....|
gi 6322387 1018 ELDESKDSIQDLIVKLKQQK 1037
Cdd:COG3883 151 ELEAKLAELEALKAELEAAK 170
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
173-957 |
2.50e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.36 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 173 KSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKEL-EKYNELErNRKIYQFTLyDRELNEVI------NQ 245
Cdd:TIGR01612 540 KEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLfDKYLEID-DEIIYINKL-KLELKEKIknisdkNE 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 246 MERLDGDYNNTVYSSEQYIQELDKRE-----DMIDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLTNVNV----K 316
Cdd:TIGR01612 618 YIKKAIDLKKIIENNNAYIDELAKISpyqvpEHLKNKDKIYSTIKSELSKIYEDDIDALYNELSSIVKENAIDNTedkaK 697
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 317 IKDVQQQIESNEEQ-RNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQ--LASLQQKQRDLILKKGEYArf 393
Cdd:TIGR01612 698 LDDLKSKIDKEYDKiQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNkiLEDFKNKEKELSNKINDYA-- 775
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 394 KSKDERDTWiHSEIEELKS------SIQNLNELESQLQMDRT-SLRKQYSAIDEEIEELIDSIngpdtKGQLEDFDSEL- 465
Cdd:TIGR01612 776 KEKDELNKY-KSKISEIKNhyndqiNIDNIKDEDAKQNYDKSkEYIKTISIKEDEIFKIINEM-----KFMKDDFLNKVd 849
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 466 --IHLKQKLSESLDTRKELWrkeQKLQTVLETLLSD--VNQNQRNVNEtmSRSLANGIINvkeiteklkiSPESVFGTLG 541
Cdd:TIGR01612 850 kfINFENNCKEKIDSEHEQF---AELTNKIKAEISDdkLNDYEKKFND--SKSLINEINK----------SIEEEYQNIN 914
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 542 ELIKVNDKYKTCAEVIGGNSLFHivvdteeTATLIMNELyrmkggrvtfipLNRlsldsdvkfpsntttqiqftpLIKKI 621
Cdd:TIGR01612 915 TLKKVDEYIKICENTKESIEKFH-------NKQNILKEI------------LNK---------------------NIDTI 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 622 KYEPRFEKAVKHVFGKTIVvkdlgqglklAKKHKLNAITLDGDRADkrgvltggyLDQHKRTRLESLKNLNESRSQHKKI 701
Cdd:TIGR01612 955 KESNLIEKSYKDKFDNTLI----------DKINELDKAFKDASLND---------YEAKNNELIKYFNDLKANLGKNKEN 1015
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 702 LEELDFVRNE--LNDIDTKIDQVNGNIRKVSNDRESVLTNIevyrtslnTKKNEKLILE--ESLNAIILKLEKLN-TNRT 776
Cdd:TIGR01612 1016 MLYHQFDEKEkaTNDIEQKIEDANKNIPNIEIAIHTSIYNI--------IDEIEKEIGKniELLNKEILEEAEINiTNFN 1087
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 777 FAQEKLNTFENDllqEFDSELSKEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELESKLipqendleSKMS 856
Cdd:TIGR01612 1088 EIKEKLKHYNFD---DFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQI--------NDLE 1156
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 857 EVGDAFIFglQDELKELQLEKESVEK---QHENAVLELGTVQREIESLIAEETNNKKL----LEKANNQQRLLLKKLDNF 929
Cdd:TIGR01612 1157 DVADKAIS--NDDPEEIEKKIENIVTkidKKKNIYDEIKKLLNEIAEIEKDKTSLEEVkginLSYGKNLGKLFLEKIDEE 1234
|
810 820
....*....|....*....|....*...
gi 6322387 930 QKSVEKTMIKKTTLVTRREELQQRIREI 957
Cdd:TIGR01612 1235 KKKSEHMIKAMEAYIEDLDEIKEKSPEI 1262
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
1-79 |
2.62e-06 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 50.93 E-value: 2.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322387 1 MYIKRVIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIrFVLSDDYSnLKREERQGLIHQGSGGSVMSASVE 79
Cdd:PRK00064 1 MYLTRLSLTDFRNYEELDL--ELSPGVNVLVGENGQGKTNLLEAI-YLLAPGRS-HRTARDKELIRFGAEAAVIHGRVE 75
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
701-1210 |
3.08e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 701 ILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIE---------VYRTSLNTKKNEKLI---------LEESLN 762
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpVCGTTLGEEKSNHIInhynekksrLEEKIR 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 763 AIILKLEKLNTNRTFAQEKLNTFENDLLQEFDSELSKEEKERLEslTKEISAAHNKLNITSDALEGITTTIDSLNAEles 842
Cdd:PRK01156 487 EIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAD--LEDIKIKINELKDKHDKYEEIKNRYKSLKLE--- 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 843 klipqenDLESKMSEVGDAFIFGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLiaeETNNKKLLEKANNQQRLl 922
Cdd:PRK01156 562 -------DLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDD---KSYIDKSIREIENEANN- 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 923 lkkLDNFQKSVEKTMIKKTTLVTRREELQQRIREI-GLLPEDALVN-DFSDITSD--QLLQRLNDMNTEISGLKNVNKRA 998
Cdd:PRK01156 631 ---LNNKYNEIQENKILIEKLRGKIDNYKKQIAEIdSIIPDLKEITsRINDIEDNlkKSRKALDDAKANRARLESTIEIL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 999 FENFKKFNERRKDLAERASELDESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAVFERLVprgtakliIHRKNDNAND 1078
Cdd:PRK01156 708 RTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRKY--------LFEFNLDFDD 779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1079 hdesIDVDMDAESNESQNGKDSEImytgvsisvsfnskqneqlhvEQLSGGQKTVCAIALILAIQ--MVDPASFYLFDEI 1156
Cdd:PRK01156 780 ----IDVDQDFNITVSRGGMVEGI---------------------DSLSGGEKTAVAFALRVAVAqfLNNDKSLLIMDEP 834
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 6322387 1157 DAALDKQYRTAVATL----LKELSKNAQFICTTFRTDMLQVADKFFRVKYENKISTVI 1210
Cdd:PRK01156 835 TAFLDEDRRTNLKDIieysLKDSSDIPQVIMISHHRELLSVADVAYEVKKSSGSSKVI 892
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1-425 |
3.57e-06 |
|
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: 51.51 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIID-NFSPHQNVIIGSNGSGKSNFFAAIRFVLsddYSNLKREERQGLIHQG-SGGSVMSASV 78
Cdd:TIGR00618 1 MKPLRLTLKNFGSYKGTHTIDfTALGPIFLICGKTGAGKTTLLDAITYAL---YGKLPRRSEVIRSLNSlYAAPSEAAFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 79 EIVF-----------------HDPDHSMILPSGVLSRGDDEvtirRTVGLKKDDYQLNDRNVTKGDIVRMLETAgfsmnn 141
Cdd:TIGR00618 78 ELEFslgtkiyrvhrtlrctrSHRKTEQPEQLYLEQKKGRG----RILAAKKSETEEVIHDLLKLDYKTFTRVV------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 142 pynIVPQGKIVALTNAKDKERLQLLEDVVGAKSFEvKLKASLKKMEETEQKKIQINKEMGELNSKLSEmEQERKELEKYN 221
Cdd:TIGR00618 148 ---LLPQGEFAQFLKAKSKEKKELLMNLFPLDQYT-QLALMEFAKKKSLHGKAELLTLRSQLLTLCTP-CMPDTYHERKQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 222 ELERNRKiyQFTLYDRELNEVINQMERLDgdynntvysseQYIQELDKREDMIDQVSKKLSSIEASLKI----KNATDLQ 297
Cdd:TIGR00618 223 VLEKELK--HLREALQQTQQSHAYLTQKR-----------EAQEEQLKKQQLLKQLRARIEELRAQEAVleetQERINRA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 298 QAKLRESEISQKLTNVNVKIKDVQQQIESneeqrnldsatlkeiksiieqRKQKLSKILPRYQELTKEEAMYKLQLASLQ 377
Cdd:TIGR00618 290 RKAAPLAAHIKAVTQIEQQAQRIHTELQS---------------------KMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 6322387 378 QKQRDLILKKGEYARFKSKDERDTWIHSEIEELKSSIQNLNELESQLQ 425
Cdd:TIGR00618 349 TLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQ 396
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
689-1047 |
4.20e-06 |
|
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: 51.17 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 689 KNLNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKL 768
Cdd:TIGR04523 218 SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 769 EKLNTNRtfAQEKLNTFENDL------LQEFDSELSKEEK------ERLESLTKEISAAHNKLNITSDALEGITTTIDSL 836
Cdd:TIGR04523 298 SDLNNQK--EQDWNKELKSELknqekkLEEIQNQISQNNKiisqlnEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 837 NAELESK------LIPQENDLESKMSEVgDAFIFGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAEETNNKK 910
Cdd:TIGR04523 376 KKENQSYkqeiknLESQINDLESKIQNQ-EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKEL 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 911 LLEKANNQQRLLLKKLDNFQKSVEKTmikKTTLVTRREELQQRIREIGLLPEDA--LVNDFSDITS--DQLLQRLNDMNT 986
Cdd:TIGR04523 455 IIKNLDNTRESLETQLKVLSRSINKI---KQNLEQKQKELKSKEKELKKLNEEKkeLEEKVKDLTKkiSSLKEKIEKLES 531
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322387 987 EISGLKNVNKRAFENFKKFNERRKdlaerASELDESKDSIQDLIVKLKQQKVNAVDSTFQK 1047
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
172-382 |
1.01e-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: 49.38 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 172 AKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKynELERNRKiyqftlydrELNEVINQMERLDG 251
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA--ELEAQKE---------ELAELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 252 DYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKiknaTDLQQAKLRESEISQKLtnvnvkiKDVQQQIESNEEQR 331
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR----ADLAELAALRAELEAER-------AELEALLAELEEER 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6322387 332 NLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRD 382
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1-505 |
1.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDdySNLKREERQGLIHQGSGgsvmSASVEI 80
Cdd:PRK02224 1 MRFDRVRLENFKCYADADL--RLEDGVTVIHGVNGSGKSSLLEACFFALYG--SKALDDTLDDVITIGAE----EAEIEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 81 VFHDPDHSMILPSGVLSRGDDEVTIRRTVGLKKDDY-QLNDRNVTKGDIVRMLETAgfSMNNPYniVPQGKIVALTNAKD 159
Cdd:PRK02224 73 WFEHAGGEYHIERRVRLSGDRATTAKCVLETPEGTIdGARDVREEVTELLRMDAEA--FVNCAY--VRQGEVNKLINATP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 160 KER-------LQL--LEDV--------VGAKSFEVKLKASLkkmeetEQKKIQI-NKEMGELNSKLSEMEQERKEL-EKY 220
Cdd:PRK02224 149 SDRqdmiddlLQLgkLEEYrerasdarLGVERVLSDQRGSL------DQLKAQIeEKEEKDLHERLNGLESELAELdEEI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 221 NELERNRkiyqftlydrelnevinqmerldgdynntvyssEQYIQELDKREDMIDQVSKKLSSIEaslKIKNATDLQQAK 300
Cdd:PRK02224 223 ERYEEQR---------------------------------EQARETRDEADEVLEEHEERREELE---TLEAEIEDLRET 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 301 LRESEisQKLTNVNVKIKDVQQQIESNEEQRN--LDSATLKEIK-SIIEQRKQKLSKilpryqelTKEEAMYKLQLASLQ 377
Cdd:PRK02224 267 IAETE--REREELAEEVRDLRERLEELEEERDdlLAEAGLDDADaEAVEARREELED--------RDEELRDRLEECRVA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 378 QKQRdliLKKGEYARFKSKDerdtwIHSEIEELKSSIQnlnELESQLQMDRTSLRK---QYSAIDEEIEELIDSING-PD 453
Cdd:PRK02224 337 AQAH---NEEAESLREDADD-----LEERAEELREEAA---ELESELEEAREAVEDrreEIEELEEEIEELRERFGDaPV 405
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 6322387 454 TKGQLEDFDSELihlkqklsesLDTRKELWRKEQKLQTVLETLLSDVNQNQR 505
Cdd:PRK02224 406 DLGNAEDFLEEL----------REERDELREREAELEATLRTARERVEEAEA 447
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
3-90 |
1.29e-05 |
|
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: 47.60 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 3 IKRVIIKGFKTYRNETIIDNFSPhQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKReERQGLIHQGSGGSVmSASVEIVF 82
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSP-LTLIVGQNGAGKTTIIEALKYALTGELPPNSK-GGAHDPKLIREGEV-RAQVKLAF 77
|
....*....
gi 6322387 83 -HDPDHSMI 90
Cdd:cd03240 78 eNANGKKYT 86
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
173-529 |
1.42e-05 |
|
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: 49.25 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 173 KSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNE------LERNRKIYQFTLYDRELNEVINQM 246
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSekqrelEEKQNEIEKLKKENQSYKQEIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 247 ERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQK---LTNVNVKIKDVQQQ 323
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKeliIKNLDNTRESLETQ 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 324 IESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLILKKGEYAR--------FKS 395
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESkisdledeLNK 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 396 KDERDTWihseiEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINgpDTKGQLEDFDSELIHLKQKLSES 475
Cdd:TIGR04523 550 DDFELKK-----ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK--DLIKEIEEKEKKISSLEKELEKA 622
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 6322387 476 LDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNETMSRSlANGIINVKEITEKL 529
Cdd:TIGR04523 623 KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW-PEIIKKIKESKTKI 675
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
184-505 |
1.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 184 KKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYD-----RELNEVINQMERLDgdynntvy 258
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaeREIAELEAELERLD-------- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 259 SSEQYIQELDKRedmidqvskklssieaslkiknatdLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQRNLDSATL 338
Cdd:COG4913 682 ASSDDLAALEEQ-------------------------LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 339 KEIKSIIEQrkQKLSKILPRYQELTKEEAMYKLQlASLQQKQRDLILKKGEY--------ARFKSKDERDTW-------- 402
Cdd:COG4913 737 EAAEDLARL--ELRALLEERFAAALGDAVERELR-ENLEERIDALRARLNRAeeeleramRAFNREWPAETAdldadles 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 403 ------IHSEIEE--------------LKSSIQNLNELESQLQMDRtslrkqysaidEEIEELIDSIN--------GPDT 454
Cdd:COG4913 814 lpeylaLLDRLEEdglpeyeerfkellNENSIEFVADLLSKLRRAI-----------REIKERIDPLNdslkripfGPGR 882
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 6322387 455 KGQLE---DFDSELIHLKQKLSE-----SLDTRKELWRKEQKLQTVLETLLSDVNQNQR 505
Cdd:COG4913 883 YLRLEarpRPDPEVREFRQELRAvtsgaSLFDEELSEARFAALKRLIERLRSEEEESDR 941
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
971-1185 |
1.63e-05 |
|
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: 48.15 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 971 DITSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERASELDESKDSIQDLIVKLKQQKVNAVDSTFQKVSE 1050
Cdd:pfam13304 77 DLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1051 NFEA---------------VFERLVPRGTAKLIIHRKNDNANDHDESIDVDMDAESNESQNGKDSEIMYTGVSISVSFNs 1115
Cdd:pfam13304 157 LDEGllledwavldlaadlALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAF- 235
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322387 1116 kqneqlhveQLSGGQKTVCAIALILAIQmVDPASFYLFDEIDAALDKQYRTAVATLLKELS-KNAQFICTT 1185
Cdd:pfam13304 236 ---------ELSDGTKRLLALLAALLSA-LPKGGLLLIDEPESGLHPKLLRRLLELLKELSrNGAQLILTT 296
|
|
| AAA_15 |
pfam13175 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
1-54 |
1.74e-05 |
|
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: 48.75 E-value: 1.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 6322387 1 MYIKRVIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYS 54
Cdd:pfam13175 1 MKIKSIIIKNFRCLKDTEI--DLDEDLTVLIGKNNSGKSSILEALDIFLNNKEK 52
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
173-524 |
2.78e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 173 KSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYDRELNEVINQMERLDGD 252
Cdd:PTZ00121 1458 KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 253 YNNTVYSSEQY-----IQELDKREDMIDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIESN 327
Cdd:PTZ00121 1538 EAKKAEEKKKAdelkkAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE 1617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 328 EEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDlILKKGEYARFKSKDERDTW-IHSE 406
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE-DKKKAEEAKKAEEDEKKAAeALKK 1696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 407 IEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTKGQLEDFDSELIHLKQKLSESLDTRKELWRKE 486
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
330 340 350
....*....|....*....|....*....|....*...
gi 6322387 487 QklQTVLETLLSDVNQNQRNVNETMSRSLANGIINVKE 524
Cdd:PTZ00121 1777 K--EAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
682-1058 |
2.98e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 682 RTRLESLKNLNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKlileESL 761
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA----ESL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 762 NAIILKLEKLNTNrtfAQEKLNTFENDLlQEFDSELSKEEkERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELE 841
Cdd:PRK02224 348 REDADDLEERAEE---LREEAAELESEL-EEAREAVEDRR-EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 842 sKLIPQENDLESKMSEVGDAF----------------------------------IFGLQDELKELQLEKESVEKQHENA 887
Cdd:PRK02224 423 -ELREREAELEATLRTARERVeeaealleagkcpecgqpvegsphvetieedrerVEELEAELEDLEEEVEEVEERLERA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 888 VlELGTVQREIESLiaeeTNNKKLLEKANNQQRlllKKLDNFQKSVEKTMIKKTTLVTRREELQQRIREIGLLPEDALvn 967
Cdd:PRK02224 502 E-DLVEAEDRIERL----EERREDLEELIAERR---ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR-- 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 968 dfsdITSDQLLQRLNDMNTEISGLKNVNKR------AFENFKKFNERRKDLAERASE----LDESKDSIQDL-------- 1029
Cdd:PRK02224 572 ----EEVAELNSKLAELKERIESLERIRTLlaaiadAEDEIERLREKREALAELNDErrerLAEKRERKRELeaefdear 647
|
410 420
....*....|....*....|....*....
gi 6322387 1030 IVKLKQQKVNAvDSTFQKVSENFEAVFER 1058
Cdd:PRK02224 648 IEEAREDKERA-EEYLEQVEEKLDELREE 675
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
160-528 |
3.32e-05 |
|
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: 48.09 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 160 KERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKynelernrkiyQFTLYDREL 239
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQ-----------EINEKTTEI 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 240 NEVINQMERLDGDYNNTVYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKN-----------ATDLQQAKLRESEISQ 308
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnqkeqdwnkelKSELKNQEKKLEEIQN 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 309 KLTNVNVKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILpryqeltKEEAMYKLQLASLQQKQRDLILKKG 388
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK-------KENQSYKQEIKNLESQINDLESKIQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 389 EYARF-KSKDERDTWIHSEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINgpDTKGQLEDFDSELIH 467
Cdd:TIGR04523 402 NQEKLnQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE--SLETQLKVLSRSINK 479
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322387 468 LKQKLSeslDTRKELWRKEQKLQTvLETLLSDVNQNQRNVNETMSRSLANGIINVKEITEK 528
Cdd:TIGR04523 480 IKQNLE---QKQKELKSKEKELKK-LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
166-955 |
3.80e-05 |
|
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: 48.19 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 166 LEDVVGAKSFEVK-LKASLKKMEET-EQKKIQINKEMGELNSKLSEMEQERKELEkynELERNRKIYQFTLYDrELNEVI 243
Cdd:pfam15921 76 IERVLEEYSHQVKdLQRRLNESNELhEKQKFYLRQSVIDLQTKLQEMQMERDAMA---DIRRRESQSQEDLRN-QLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 244 NQMERLDGDYNNTVYSSEQYIQELDK----REDMIDQVSKKLSSIE--ASLKIKNATDLQQAKLRE--SEISQKLTNVNV 315
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQLRKmmlsHEGVLQEIRSILVDFEeaSGKKIYEHDSMSTMHFRSlgSAISKILRELDT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 316 KIKDVQQQIESNEEQ-RNLDSATLKEIKSIIEQRKQKLSKILPRYQ-ELTKeeamyKLQLASLQQKQRDLILKKGEYARF 393
Cdd:pfam15921 232 EISYLKGRIFPVEDQlEALKSESQNKIELLLQQHQDRIEQLISEHEvEITG-----LTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 394 KSKDERDTWihseieelkssIQNLNELESQLQMDRTSLRKQYSAIDEEIEELidsingpdtkgqledfDSELIHLKQKLS 473
Cdd:pfam15921 307 QARNQNSMY-----------MRQLSDLESTVSQLRSELREAKRMYEDKIEEL----------------EKQLVLANSELT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 474 ESLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVN--------------------ETMSRSLANGIINVKEITEKLKISP 533
Cdd:pfam15921 360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELSlekeqnkrlwdrdtgnsitiDHLRRELDDRNMEVQRLEALLKAMK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 534 ESVFGTLG-ELIKVNDKYKTCAEViggNSLFHIVVDTEETATLIMNELYRMKggrvtfiplnrLSLDSDVKFPSNTTTQI 612
Cdd:pfam15921 440 SECQGQMErQMAAIQGKNESLEKV---SSLTAQLESTKEMLRKVVEELTAKK-----------MTLESSERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 613 QftplikkikyepRFEKAVKHVFGKtivVKDLGQGLKLaKKHKLNAITLDGDRAdkrgvltggyldQHKRTRLESLKnln 692
Cdd:pfam15921 506 Q------------EKERAIEATNAE---ITKLRSRVDL-KLQELQHLKNEGDHL------------RNVQTECEALK--- 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 693 ESRSQHKKILEELdfvRNELNDIDTKIDQ----------VNGNIRKVSNDRESVLTNIEVyrtsLNTKKNEKlILEESLN 762
Cdd:pfam15921 555 LQMAEKDKVIEIL---RQQIENMTQLVGQhgrtagamqvEKAQLEKEINDRRLELQEFKI----LKDKKDAK-IRELEAR 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 763 AIILKLEKLNTNRTfAQEKLNTFEnDLLQEFDSELS--KEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAEL 840
Cdd:pfam15921 627 VSDLELEKVKLVNA-GSERLRAVK-DIKQERDQLLNevKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSA 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 841 ESKLIPQENDLESKMSEVGDAF----------------IFGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAE 904
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMkvamgmqkqitakrgqIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 6322387 905 ETNNKKLLEKANNQQRLLLKKLDNFQKSVEKTMIKKTT---LVTRREELQQRIR 955
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEcqdIIQRQEQESVRLK 838
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
695-931 |
6.80e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 695 RSQHKKILEELDFVRNELNDIDTKIDQVNGNI---RKVSNDRESVLTNIevYRTSLNTKKNEKLILEEsLNAIILKLEKL 771
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIeeqRKKNGENIARKQNK--YDELVEEAKTIKAEIEE-LTDELLNLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 772 NTNRTFAQEKLNTFENDLlqefdselskeeKERLESLTKEISAAHN---------KLNITSDALEGITTTIDSLNAELEs 842
Cdd:PHA02562 250 IEDPSAALNKLNTAAAKI------------KSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQHSLE- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 843 KLIPQENDLESKMSEVGDafifgLQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAEETNNKKLLEKANNQQRLL 922
Cdd:PHA02562 317 KLDTAIDELEEIMDEFNE-----QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
....*....
gi 6322387 923 LKKLDNFQK 931
Cdd:PHA02562 392 VKTKSELVK 400
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
3-84 |
7.58e-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: 45.28 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 3 IKRVIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKREERQGL-IHQGSggsvMSASVEIV 81
Cdd:cd03277 3 IVRIKLENFVTYDETEF--RPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEfVKRGC----DEGTIEIE 76
|
...
gi 6322387 82 FHD 84
Cdd:cd03277 77 LYG 79
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1122-1201 |
8.42e-05 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 45.15 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1122 HVEQLSGGQKTVCAIALILAIQmvdpASFYLFDEIDAALDKQYRTAVATLLKELSKNAQ-FICTTFRTDML-QVADKFFR 1199
Cdd:cd03225 131 SPFTLSGGQKQRVAIAGVLAMD----PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKtIIIVTHDLDLLlELADRVIV 206
|
..
gi 6322387 1200 VK 1201
Cdd:cd03225 207 LE 208
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
176-383 |
8.77e-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: 8.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 176 EVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEK-YNELERnrkiyQFTLYDRELNEVINQMERLDGDYN 254
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrIRALEQ-----ELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 255 NTvysSEQYIQELDKREDM--IDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQRN 332
Cdd:COG4942 101 AQ---KEELAELLRALYRLgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6322387 333 LDSATLKEIKSIIEQRKQKLSKILpryQELTKEEAMYKLQLASLQQKQRDL 383
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLL---ARLEKELAELAAELAELQQEAEEL 225
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
257-1053 |
9.83e-05 |
|
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: 46.96 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 257 VYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIknatdLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQRNLDSA 336
Cdd:TIGR00606 178 IFSATRYIKALETLRQVRQTQGQKVQEHQMELKY-----LKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 337 TLKEIK---SIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLI--LKKGEYARFKSKDERDTWIHSEIEELK 411
Cdd:TIGR00606 253 RLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLndLYHNHQRTVREKERELVDCQRELEKLN 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 412 SSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTKGQLEDFDSELIHLKQKLSESLDTRKELWRKEQKLQT 491
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 492 VLETLLSDVNQNQRNVNETMSR--SLANGIINVKEITEKLKISPESVFGTLGELIKVNDK-YKTCAEVIGGNSLFHIVVD 568
Cdd:TIGR00606 413 LCADLQSKERLKQEQADEIRDEkkGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRiLELDQELRKAERELSKAEK 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 569 TEETATLIMNELYrMKGGRVTFIPLNRLSLDSDVKFPSNTTTQIQFTPLIKK--IKYEPRFEKAVKHVFGKTIVVKDLGQ 646
Cdd:TIGR00606 493 NSLTETLKKEVKS-LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDkmDKDEQIRKIKSRHSDELTSLLGYFPN 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 647 GLKLA----KKHKLNAITLDGDRADKRGVLTGGYLDQHKRTRLESLKNLNESrsqhkkiLEELDFVRNELNDIDTKIDQV 722
Cdd:TIGR00606 572 KKQLEdwlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS-------YEDKLFDVCGSQDEESDLERL 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 723 NGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTFAQEKLNTFEnDLLQEFDSELSKEEK 802
Cdd:TIGR00606 645 KEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAP-DKLKSTESELKKKEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 803 ERLESLTKeISAAHNKLNITSDALEGITTTIDSLN---AELESKLIPQENDLESKMSEVGDAFIFgLQDE--LKELQLEK 877
Cdd:TIGR00606 724 RRDEMLGL-APGRQSIIDLKEKEIPELRNKLQKVNrdiQRLKNDIEEQETLLGTIMPEEESAKVC-LTDVtiMERFQMEL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 878 ESVEKQHENAVLELGTV--QREIESLIAEETNNKKLLEKANNQQRLLLKKLDNFQKSVEKTMIKKTTLVTRREELQQRIR 955
Cdd:TIGR00606 802 KDVERKIAQQAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 956 EIGLLPEDalvndfsditSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERASELDE-SKDSIQDLIVKLK 1034
Cdd:TIGR00606 882 RRQQFEEQ----------LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKkAQDKVNDIKEKVK 951
|
810
....*....|....*....
gi 6322387 1035 qQKVNAVDSTFQKVSENFE 1053
Cdd:TIGR00606 952 -NIHGYMKDIENKIQDGKD 969
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
194-445 |
1.11e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 194 IQINKEMGELN-SKLSEMEQERKELE-KYNELERNRKIYQftLYDRELNEVINQ-MERLDGDYNNTVYSSEQYIQELDKR 270
Cdd:PHA02562 162 ISVLSEMDKLNkDKIRELNQQIQTLDmKIDHIQQQIKTYN--KNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 271 EDMIDQVSKKLSSIEASLKiknatDLQQAKLRESEISQKLTNVNVKIKDVQ------QQIESNEEQrnldsatLKEIKSI 344
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALN-----KLNTAAAKIKSKIEQFQKVIKMYEKGGvcptctQQISEGPDR-------ITKIKDK 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 345 IEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLILKKGEYARFKSKDERdtwIHSEIEELKSSIQNLNELESQL 424
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKK---VKAAIEELQAEFVDNAEELAKL 384
|
250 260
....*....|....*....|.
gi 6322387 425 QMDRTSLRKQYSAIDEEIEEL 445
Cdd:PHA02562 385 QDELDKIVKTKSELVKEKYHR 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
322-520 |
1.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 322 QQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKIlpryQELTKEEAMYKLQLASLQQKQRDL---ILKKGEYARFKSKDE 398
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLeklLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 399 RDTWIHSEIEELKSSIQNLNELESQLQmdrtSLRKQYSAIDEEIEELIDSINgPDTKGQLEDFDSELIHLKQKLSESLDT 478
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLS-LATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 6322387 479 RKELWRKEQKLQTVLETLLSD--VNQNQRNVNETMSRSLANGII 520
Cdd:COG4717 215 LEEAQEELEELEEELEQLENEleAAALEERLKEARLLLLIAAAL 258
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
334-868 |
1.20e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 334 DSATLKEIKSIIEQRKQkLSKIlprYQELTKEEAMYKLqLASLQQKQRDLILKKGEYARFKS-KDERDTWIHS-EIEELK 411
Cdd:COG4913 220 EPDTFEAADALVEHFDD-LERA---HEALEDAREQIEL-LEPIRELAERYAAARERLAELEYlRAALRLWFAQrRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 412 SSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTkGQLEDFDSELIHLKQKLSE----------------- 474
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG-DRLEQLEREIERLERELEErerrrarleallaalgl 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 475 -SLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNETMSR----------------SLANGIINV--------KEITEKL 529
Cdd:COG4913 374 pLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAlrdlrrelreleaeiaSLERRKSNIparllalrDALAEAL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 530 KISPESV-FgtLGELIKVNDKYK---TCAE-VIGGNSlFHIVVDTE--ETATLIMNELyRMKGGRVTFIPLNRLSLDSDV 602
Cdd:COG4913 454 GLDEAELpF--VGELIEVRPEEErwrGAIErVLGGFA-LTLLVPPEhyAAALRWVNRL-HLRGRLVYERVRTGLPDPERP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 603 KFPSNTttqiqftpLIKKIKYEP-RFEKAVKHVFGKT---IVVKDLGQgLKLAKKhklnAITLDG------------DRA 666
Cdd:COG4913 530 RLDPDS--------LAGKLDFKPhPFRAWLEAELGRRfdyVCVDSPEE-LRRHPR----AITRAGqvkgngtrhekdDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 667 DKRGVLTGGYLDQHKRTRLES-LKNLNESRSQHKKILEELDFVRNELNDI-------------DTKIDQVNGNIRKVSND 732
Cdd:COG4913 597 RIRSRYVLGFDNRAKLAALEAeLAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdEIDVASAEREIAELEAE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 733 RESVLTN---IEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTFAQEKLNTFEnDLLQEFDSELSKEEKERLESLT 809
Cdd:COG4913 677 LERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-DRLEAAEDLARLELRALLEERF 755
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 6322387 810 KEISAAhnklNITSDALEGITTTIDSLNAELESKlipqENDLESKMSEVGDAFIFGLQD 868
Cdd:COG4913 756 AAALGD----AVERELRENLEERIDALRARLNRA----EEELERAMRAFNREWPAETAD 806
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
738-935 |
1.20e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 738 TNIEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTFAQEKLNTFENDL--LQEFDSELSKEEKERLESLTKEISAA 815
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIdkLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 816 HNKLNITS--DAL---EGITTTIDslNAELESKLIPQENDLeskMSEVGDAfifglQDELKELQLEKESVEKQHENAVLE 890
Cdd:COG3883 96 YRSGGSVSylDVLlgsESFSDFLD--RLSALSKIADADADL---LEELKAD-----KAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 6322387 891 LGTVQREIESLIAEetnNKKLLEKANNQQRLLLKKLDNFQKSVEK 935
Cdd:COG3883 166 LEAAKAELEAQQAE---QEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
1135-1217 |
1.34e-04 |
|
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: 45.27 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1135 AIALILAIQMVDPAsfYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVADKFFRV-KYENKISTVIEVN 1213
Cdd:cd03241 182 ALKAILARKDAVPT--LIFDEIDTGISGEVAQAVGKKLKELSRSHQVLCITHLPQVAAMADNHFLVeKEVEGGRTVTKVR 259
|
....
gi 6322387 1214 REEA 1217
Cdd:cd03241 260 ELDK 263
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
178-535 |
1.41e-04 |
|
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: 46.17 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 178 KLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKynELERNRKIYQFTLydRELNEVINQMERLDGDYNNTV 257
Cdd:TIGR04523 90 KLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEK--QKKENKKNIDKFL--TEIKKKEKELEKLNNKYNDLK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 258 YSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNATDL------QQAKLRESEISQ----------KLTNVNVKIKDVQ 321
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSnlkkkiQKNKSLESQISElkkqnnqlkdNIEKKQQEINEKT 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 322 QQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASL-QQKQRDLIlkKGEYARFKSKDERD 400
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnNQKEQDWN--KELKSELKNQEKKL 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 401 TWIHSEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEE---LIDSINGPDT--KGQLEDFDSELIHLKQKLSES 475
Cdd:TIGR04523 324 EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqnEIEKLKKENQsyKQEIKNLESQINDLESKIQNQ 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322387 476 LDTRKELWRKEQKLQTVLETLLSDVN--QNQRNVNETMSRSLANGIINVKEITEKLKISPES 535
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIErlKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
703-957 |
1.41e-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: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 703 EELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEvyrtslntkkneklILEESLNAIILKLEKLNTNRTFAQEKL 782
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA--------------ALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 783 NTFENDLlqefdSELSKEEKERLESLTKEISAAHnkLNITSDALEGITTTIDSLNAELESKLIpqendleSKMSEVGDAF 862
Cdd:COG4942 86 AELEKEI-----AELRAELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFLDAVRRLQYL-------KYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 863 IFGLQDELKELQLEKESVEKQhenavlelgtvQREIESLIAEETNNKKLLEKANNQQRLLLKKLdnfQKSVEKTMIKKTT 942
Cdd:COG4942 152 AEELRADLAELAALRAELEAE-----------RAELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAE 217
|
250
....*....|....*
gi 6322387 943 LVTRREELQQRIREI 957
Cdd:COG4942 218 LQQEAEELEALIARL 232
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1121-1201 |
1.70e-04 |
|
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: 44.14 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1121 LHVEQLSGGQKTVCAIALILAIQMV--DPASFYLFDEIDAALDKQYRT-AVATLLKELS--KNAQFICTTFRTDMLQVAD 1195
Cdd:cd03240 111 DMRGRCSGGEKVLASLIIRLALAETfgSNCGILALDEPTTNLDEENIEeSLAEIIEERKsqKNFQLIVITHDEELVDAAD 190
|
....*.
gi 6322387 1196 KFFRVK 1201
Cdd:cd03240 191 HIYRVE 196
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
3-50 |
1.83e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 45.03 E-value: 1.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 6322387 3 IKRVIIKGFKTYRNETIIDNFSPHQ-----NVIIGSNGSGKSNFFAAIRFVLS 50
Cdd:COG1106 2 LISFSIENFRSFKDELTLSMVASGLrllrvNLIYGANASGKSNLLEALYFLRN 54
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
778-1033 |
1.85e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 778 AQEKLNTFENDLlQEFDSELSkEEKERLESLTKEISAAHNKLNITSDALE---------GITTTIDSLNAELEsklipqe 848
Cdd:COG4913 608 NRAKLAALEAEL-AELEEELA-EAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELE------- 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 849 nDLESKMSEVGdafifGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAEETNNKKLLEKANN----------Q 918
Cdd:COG4913 679 -RLDASSDDLA-----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlarlelrallE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 919 QRLLLKKLDNFQKSVEKTMIKKT-TLVTRREELQQRIREI-------------GLLPEDALVNDFsditsDQLLQRLndm 984
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIdALRARLNRAEEELERAmrafnrewpaetaDLDADLESLPEY-----LALLDRL--- 824
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 6322387 985 ntEISGLKNVNKRAFENFKKFNERrkDLAERASELDESKDSIQDLIVKL 1033
Cdd:COG4913 825 --EEDGLPEYEERFKELLNENSIE--FVADLLSKLRRAIREIKERIDPL 869
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
711-891 |
1.87e-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: 44.53 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 711 ELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKLEKLNTNRTFAQEKLNTFENdlL 790
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--N 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 791 QEFDSeLSKEekerLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELESKlipqENDLESKMSEVgDAFIFGLQDEL 870
Cdd:COG1579 89 KEYEA-LQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAEL----EAELEEKKAEL-DEELAELEAEL 158
|
170 180
....*....|....*....|.
gi 6322387 871 KELQLEKESVEKQHENAVLEL 891
Cdd:COG1579 159 EELEAEREELAAKIPPELLAL 179
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
795-1044 |
1.97e-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: 45.14 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 795 SELSKEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELeSKLIPQENDLESKMSEvgdafifgLQDELKELQ 874
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-AALARRIRALEQELAA--------LEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 875 LEKESVEKQhenavleLGTVQREIESLIAEetnnkklLEKANNQQRL-LLKKLDNFQKSVEKTMIKKTTLVTRREELQQR 953
Cdd:COG4942 90 KEIAELRAE-------LEAQKEELAELLRA-------LYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 954 IREIGLLpedALVNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFENFKKFNERRKDLAERASELDESKDSIQDLIVKL 1033
Cdd:COG4942 156 RADLAEL---AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|.
gi 6322387 1034 KQQKVNAVDST 1044
Cdd:COG4942 233 EAEAAAAAERT 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1123-1196 |
2.01e-04 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. 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: 213226 [Multi-domain] Cd Length: 213 Bit Score: 44.05 E-value: 2.01e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322387 1123 VEQLSGGQKTVCAIALILAIQmvdpASFYLFDEIDAALDKQYRTAVATLLKELSKNAQfiCTTF-----RTDMLQVADK 1196
Cdd:cd03259 128 PHELSGGQQQRVALARALARE----PSLLLLDEPLSALDAKLREELREELKELQRELG--ITTIyvthdQEEALALADR 200
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
172-381 |
2.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 172 AKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKynELERNRKiyqftlydrELNEVINQMER--L 249
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA--EIEERRE---------ELGERARALYRsgG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 250 DGDYNNTVYSSE---QYIQELDKREDMIDQVSKKLSSIEAsLKIKNATDLQQAKLRESEISQKLTNVNVKIKDVQQQIES 326
Cdd:COG3883 101 SVSYLDVLLGSEsfsDFLDRLSALSKIADADADLLEELKA-DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6322387 327 NEEQrnldSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLASLQQKQR 381
Cdd:COG3883 180 QEAL----LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
681-916 |
2.34e-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: 45.14 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 681 KRTRLESL-KNLNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEE 759
Cdd:COG4942 25 AEAELEQLqQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 760 SLNAIILKLEKLNTNRT----FAQEKLNTFENDLlqEFDSELSKEEKERLESLTKEIsaahNKLNITSDALEGITTTIDS 835
Cdd:COG4942 105 ELAELLRALYRLGRQPPlallLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADL----AELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 836 LNAELESklipQENDLESKMSEVgdafifglQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAEETNNKKLLEKA 915
Cdd:COG4942 179 LLAELEE----ERAALEALKAER--------QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
.
gi 6322387 916 N 916
Cdd:COG4942 247 G 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
689-1212 |
3.00e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 689 KNLNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSN------------DRESVLTNIEVYRTSLNTKKNEKLI 756
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrelTEEHRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 757 LEESLNAIILKLEKLNTNRTFAQEKLNTFEN-DLLQEFDSELSKEEKERLESLTKEISAAHNKLNitsdaleGITTTIDS 835
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELaEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLI-------KLKGEIKS 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 836 LNAELESklipqENDLESKMSEvgdafifgLQDELKELQLEKESVEKQHENAVLE-LGTVQREIESLiaeETNNKKLLEK 914
Cdd:PRK03918 544 LKKELEK-----LEELKKKLAE--------LEKKLDELEEELAELLKELEELGFEsVEELEERLKEL---EPFYNEYLEL 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 915 ANNQQRL--LLKKLDNFQKSVEKTMIKKTTLVTRREELQQRIREIGLLPEDALVNDFSDITSdQLLQRLNDMNTEISGLK 992
Cdd:PRK03918 608 KDAEKELerEEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL-ELSRELAGLRAELEELE 686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 993 NVNKRAFENFKKFNERRKDLAERASE---LDESKDSIQDLIVKLKQQKVNAVDSTFQKVSENFEAVFERLVPRGTAKLII 1069
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKElekLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVRV 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1070 HRKndnandhDESIDVdmdaesnesqngkdsEIMYTGVSISVSFnskqneqlhveqLSGGQKTVCAIALILAIQM--VDP 1147
Cdd:PRK03918 767 KAE-------ENKVKL---------------FVVYQGKERPLTF------------LSGGERIALGLAFRLALSLylAGN 812
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322387 1148 ASFYLFDEIDAALDKQYRTAVATLL-KELSKNAQFICTTFRTDMLQVADKFFRVKYENKISTVIEV 1212
Cdd:PRK03918 813 IPLLILDEPTPFLDEERRRKLVDIMeRYLRKIPQVIIVSHDEELKDAADYVIRVSLEGGVSKVEVV 878
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1122-1182 |
3.97e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 43.51 E-value: 3.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322387 1122 HVEQLSGGQKTVCAIALILAIQmvdpASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFI 1182
Cdd:cd03236 136 NIDQLSGGELQRVAIAAALARD----ADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV 192
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
153-399 |
4.41e-04 |
|
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: 44.57 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 153 ALTNAKDKERLQLLEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEK-YNELERNRKIYQ 231
Cdd:TIGR00618 652 QLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDReFNEIENASSSLG 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 232 FTLYDRE--LNEVINQMERLdgdyNNTVYSSEQYIQELDKREDMID-QVSKKLSSIEASLKIKN---ATDLQQAKLRESE 305
Cdd:TIGR00618 732 SDLAAREdaLNQSLKELMHQ----ARTVLKARTEAHFNNNEEVTAAlQTGAELSHLAAEIQFFNrlrEEDTHLLKTLEAE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 306 ISQKLTNvNVKIKDVQQQIESNEEQrnldsatlkEIKSIIEQRKQKLSKIlpRYQELTKEEAMYKLQLASLQQKQRDLIL 385
Cdd:TIGR00618 808 IGQEIPS-DEDILNLQCETLVQEEE---------QFLSRLEEKSATLGEI--THQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
250
....*....|....
gi 6322387 386 KKGEYARFKSKDER 399
Cdd:TIGR00618 876 DKLNGINQIKIQFD 889
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
179-1044 |
4.94e-04 |
|
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: 44.65 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 179 LKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEkynelERNRKIYQFTlyDRELNEVINQMERLDGDYNNTVY 258
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELE-----LKMEKVFQGT--DEQLNDLYHNHQRTVREKERELV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 259 SSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLTN-----------VNVKIKDVQQ-QIES 326
Cdd:TIGR00606 323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRleldgfergpfSERQIKNFHTlVIER 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 327 NEEQRNLDSATLKEIKSI----------IEQRKQKLSKILPRYQE-LTKEEAMYKLQLASLQQKQ--RDLILKKGEYARf 393
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKerlkqeqadeIRDEKKGLGRTIELKKEiLEKKQEELKFVIKELQQLEgsSDRILELDQELR- 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 394 ksKDERDTwihsEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEEL--------------------------ID 447
Cdd:TIGR00606 482 --KAEREL----SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttrtqmemltkdkmdkdeqirkIK 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 448 SINGPDTKGQLEDFDSELIHLK--QKLSESLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNETMSrSLANGIINVKEI 525
Cdd:TIGR00606 556 SRHSDELTSLLGYFPNKKQLEDwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLS-SYEDKLFDVCGS 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 526 TEKlkispESVFGTLGELIKVNDKYKtcAEVIGGNSLFHIVV----DTEETATLIMNELYRMKGgrvtfiPLNRLSLDSD 601
Cdd:TIGR00606 635 QDE-----ESDLERLKEEIEKSSKQR--AMLAGATAVYSQFItqltDENQSCCPVCQRVFQTEA------ELQEFISDLQ 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 602 VKFPSNTTTQIQFTPLIKKIkyEPRFEKAVKHVFGKTIVVKDLGQGLKlAKKHKLNAITLDGDRaDKRGVLTGGYLDQHK 681
Cdd:TIGR00606 702 SKLRLAPDKLKSTESELKKK--EKRRDEMLGLAPGRQSIIDLKEKEIP-ELRNKLQKVNRDIQR-LKNDIEEQETLLGTI 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 682 RTRLESLKNLNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNiRKVSNDRESVLTNIEVYRT-SLNTKKNEKLILEES 760
Cdd:TIGR00606 778 MPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLD-RTVQQVNQEKQEKQHELDTvVSKIELNRKLIQDQQ 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 761 LNAIILKlEKLNTNRTfaqEKLNTFENDLLQEFDSELSKEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSL-NAE 839
Cdd:TIGR00606 857 EQIQHLK-SKTNELKS---EKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELiSSK 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 840 LESKLIPQenDLESKMSEVGDAFIFGLQDELKELQLEKESVEKQHENavlelgtvqrEIESLIAEETNNKKLLEKANNQQ 919
Cdd:TIGR00606 933 ETSNKKAQ--DKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKET----------ELNTVNAQLEECEKHQEKINEDM 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 920 RLLLKKLDNfQKSVEKTMIKKTTLVTRREELQQRIREigllpedaLVNDFSDITSDQLLQRLNDMN---TEISGLKNVNK 996
Cdd:TIGR00606 1001 RLMRQDIDT-QKIQERWLQDNLTLRKRENELKEVEEE--------LKQHLKEMGQMQVLQMKQEHQkleENIDLIKRNHV 1071
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 6322387 997 RAFENFKKFNERRKDLAE--RASELDESKDSIQDLIVKLKQQKVNAVDST 1044
Cdd:TIGR00606 1072 LALGRQKGYEKEIKHFKKelREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| recN |
TIGR00634 |
DNA repair protein RecN; All proteins in this family for which functions are known are ATP ... |
849-1203 |
7.95e-04 |
|
DNA repair protein RecN; All proteins in this family for which functions are known are ATP binding proteins involved in the initiation of recombination and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273187 [Multi-domain] Cd Length: 563 Bit Score: 43.57 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 849 NDLESKMSEVGDAFIFGLQDELKELQLEKESVEKQH--ENAVLELGTVQ---REIESLIAEE---TNNKKLLEKANNQQR 920
Cdd:TIGR00634 157 NEKVKAYRELYQAWLKARQQLKDRQQKEQELAQRLDflQFQLEELEEADlqpGEDEALEAEQqrlSNLEKLRELSQNALA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 921 LLLKKLDNFQKSVEKTMIK-----KTTLVTRREELQQRIREIGLLPEDA---LVNDFSDITSDQllQRLNDMNTEISGLK 992
Cdd:TIGR00634 237 ALRGDVDVQEGSLLEGLGEaqlalASVIDGSLRELAEQVGNALTEVEEAtreLQNYLDELEFDP--ERLNEIEERLAQIK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 993 NVNKRAFENFKKFNERRKDLAERASEL---DESKDSIQDLIVKLKQQkvnaVDSTFQKVSENFEAVFERLVPRGTAKLii 1069
Cdd:TIGR00634 315 RLKRKYGASVEEVLEYAEKIKEELDQLddsDESLEALEEEVDKLEEE----LDKAAVALSLIRRKAAERLAKRVEQEL-- 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1070 hrKNDNANDHDESIDVDMDAESNE----SQNGKDSeimytgVSISVSFNSKQNEQLHVEQLSGGQKTVCAIALILAIQMV 1145
Cdd:TIGR00634 389 --KALAMEKAEFTVEIKTSLPSGAkaraGAYGADQ------VEFLFSANTGEPVKPLAKVASGGELSRVMLALKVVLSSS 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 6322387 1146 DPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQFICTTFRTDMLQVADKFFRVKYE 1203
Cdd:TIGR00634 461 AAVTTLIFDEVDVGVSGETAQAIAKKLAQLSERHQVLCVTHLPQVAAHADAHFKVEKE 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1122-1174 |
8.20e-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: 8.20e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 6322387 1122 HVEQLSGGQKTVCAIALIlaiqMVDPASFYLFDEIDAALDKQYRTAVATLLKE 1174
Cdd:cd03221 67 YFEQLSGGEKMRLALAKL----LLENPNLLLLDEPTNHLDLESIEALEEALKE 115
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
264-449 |
1.18e-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: 41.83 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 264 IQELDKRedmIDQVSKKLSSIEASLKiknatDLQQAKlreSEISQKLTNVNVKIKDVQQQIESNEEQrnldsatLKEIKS 343
Cdd:COG1579 12 LQELDSE---LDRLEHRLKELPAELA-----ELEDEL---AALEARLEAAKTELEDLEKEIKRLELE-------IEEVEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 344 IIEQRKQKLSKIL-PR-YQELTKEEAMYKLQLASLQQKQRDLilkkgeYARFKSKDERDTWIHSEIEELKssiQNLNELE 421
Cdd:COG1579 74 RIKKYEEQLGNVRnNKeYEALQKEIESLKRRISDLEDEILEL------MERIEELEEELAELEAELAELE---AELEEKK 144
|
170 180
....*....|....*....|....*...
gi 6322387 422 SQLQMDRTSLRKQYSAIDEEIEELIDSI 449
Cdd:COG1579 145 AELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
686-1030 |
1.23e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 686 ESLKNLNESRSQHKKILEELDFV-------RNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTkknekliLE 758
Cdd:PRK02224 220 EEIERYEEQREQARETRDEADEVleeheerREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-------LE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 759 ESLNAIILKLEklntnrtfaqekLNTFENDLLQEFDSELSKEEKERLESLtKEISAAHNKLNITSDALEGITTTIDSLNA 838
Cdd:PRK02224 293 EERDDLLAEAG------------LDDADAEAVEARREELEDRDEELRDRL-EECRVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 839 ELESKLIPQENDLESKMSEVGDAfifglQDELKELQLEKESVEKQHENAVLELGTVQREIESLIAEetnnkklLEKANNQ 918
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDR-----REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE-------RDELRER 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 919 QRLLLKKLDNFQKSVEKTmikkttlvtrreelqQRIREIGLLPE---------DALVNDFSDITSDQLLQRLNDMNTEIS 989
Cdd:PRK02224 428 EAELEATLRTARERVEEA---------------EALLEAGKCPEcgqpvegspHVETIEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 6322387 990 GLKNVNKRAfenfkkfnERRKDLAERASELDESKDSIQDLI 1030
Cdd:PRK02224 493 EVEERLERA--------EDLVEAEDRIERLEERREDLEELI 525
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
688-1037 |
1.26e-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: 43.09 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 688 LKNLNESRSQ--HKKILEELDFVRNELNDIDTKIDQVNGNIrkvsNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAII 765
Cdd:TIGR04523 297 ISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKII----SQLNEQISQLKKELTNSESENSEKQRELEEKQNEI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 766 LKLEKLNTNRTFAQEKLNTFENDLLQEFD--SELSKEEKERLESLTKEisaahnkLNITSDALEGITTTIDSLNAELESk 843
Cdd:TIGR04523 373 EKLKKENQSYKQEIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQE-------KELLEKEIERLKETIIKNNSEIKD- 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 844 LIPQENDLESKMSEVgDAFIFGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLiaeeTNNKKLLEkanNQQRLLL 923
Cdd:TIGR04523 445 LTNQDSVKELIIKNL-DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL----NEEKKELE---EKVKDLT 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 924 KKLDNFQKSVEKTMIKKTTLVTRREELQQRIREIgllpEDALVNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFENFK 1003
Cdd:TIGR04523 517 KKISSLKEKIEKLESEKKEKESKISDLEDELNKD----DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
330 340 350
....*....|....*....|....*....|....
gi 6322387 1004 KFNERRKDLAERASELDESKDSIQDLIVKLKQQK 1037
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-521 |
1.41e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 294 TDLQQAKLRESEISQKLTNVNVKIKDVQQQIESNEEQRNldsATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQL 373
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN---ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 374 ASLQQKQR-----DLILKKGEYARFKSKDERDTWIHS----EIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEE 444
Cdd:COG3883 93 RALYRSGGsvsylDVLLGSESFSDFLDRLSALSKIADadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322387 445 LIDSINgpDTKGQLEDFDSELIHLKQKLSESLDTRKELWRKEQKLQTVLETLLSDVNQNQRNVNETMSRSLANGIIN 521
Cdd:COG3883 173 LEAQQA--EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1125-1184 |
1.53e-03 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 41.54 E-value: 1.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322387 1125 QLSGGQKTVCAIALILaiqMVDPASFyLFDEIDAALDKQYRTAVATLLKELSKNA--QFICT 1184
Cdd:PRK11124 141 HLSGGQQQRVAIARAL---MMEPQVL-LFDEPTAALDPEITAQIVSIIRELAETGitQVIVT 198
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
3-58 |
2.38e-03 |
|
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: 40.66 E-value: 2.38e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 6322387 3 IKRVIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIRFVLSDDYSNLKR 58
Cdd:cd03276 1 IESITLKNFMCHRHLQI--EFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNR 54
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
152-370 |
2.58e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 152 VALTNAKDKERLQLlEDVVGAKSFEVKLKASLKKMEETEQKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQ 231
Cdd:pfam17380 372 MEISRMRELERLQM-ERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 232 FTLYDRELNEvinQMERLDGDynntvySSEQYIQELDKREDmidQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLt 311
Cdd:pfam17380 451 VRLEEQERQQ---QVERLRQQ------EEERKRKKLELEKE---KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL- 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6322387 312 nVNVKIKDVQQQIESNEEQRNLDSATLKEIKsiIEQRKQKLSKILPRYQELTKEEAMYK 370
Cdd:pfam17380 518 -LEKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERSRLEAMER 573
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
175-482 |
2.97e-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: 42.13 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 175 FEVKLKASLKKMEETEQKKIQINKEMGELNSKLSE----MEQERKELEKYNELERNRKIYQFTLYDRELNEVINQMERLD 250
Cdd:pfam12128 609 AEEALQSAREKQAAAEEQLVQANGELEKASREETFartaLKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 251 GDYNNTVYSSEQYIQELDKredmiDQVSKKLSSIEASLKIKNATDLQQAKLREsEISQKLTNVNVKIKDVQQQIESNEEQ 330
Cdd:pfam12128 689 AQLKQLDKKHQAWLEEQKE-----QKREARTEKQAYWQVVEGALDAQLALLKA-AIAARRSGAKAELKALETWYKRDLAS 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 331 RNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEEAMYKLQLasLQQKQRdlilkkgeYARFKSKderdtwIHSEIEEL 410
Cdd:pfam12128 763 LGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETW--LQRRPR--------LATQLSN------IERAISEL 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 411 KssiQNLNELES-------QLQMDRTSLRKQYSAIDEEIEELIDSINGPDT---KGQLEDFDSELIHLKQKLSESLDTRK 480
Cdd:pfam12128 827 Q---QQLARLIAdtklrraKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkeDANSEQAQGSIGERLAQLEDLKLKRD 903
|
..
gi 6322387 481 EL 482
Cdd:pfam12128 904 YL 905
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
679-883 |
3.00e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 679 QHKRTRLESLKN-LNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIE------------VYRT 745
Cdd:COG3883 19 QAKQKELSELQAeLEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEerreelgeraraLYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 746 SLNTKKNEKLILEESLNAIIlkleklntNRTFAQEKLNTFENDLLQEFdselsKEEKERLESLTKEISAAHNKLNITSDA 825
Cdd:COG3883 99 GGSVSYLDVLLGSESFSDFL--------DRLSALSKIADADADLLEEL-----KADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 6322387 826 LEGITTTIDSLNAELESKLipqeNDLESKMSEvgdafifgLQDELKELQLEKESVEKQ 883
Cdd:COG3883 166 LEAAKAELEAQQAEQEALL----AQLSAEEAA--------AEAQLAELEAELAAAEAA 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1125-1176 |
3.18e-03 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 40.85 E-value: 3.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 6322387 1125 QLSGGQKTVCAIALILAIQmvdpASFYLFDEIDAALDKQYRTAVATLLKELS 1176
Cdd:PRK09493 136 ELSGGQQQRVAIARALAVK----PKLMLFDEPTSALDPELRHEVLKVMQDLA 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
195-482 |
3.19e-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: 41.93 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 195 QINKEMGELNSKLSEMEQERKELEKYNELERNRKIYqftlydreLNEVINQMERLDGDYNNtvysseqyiqELDKREDMI 274
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINN--------SNNKIKILEQQIKDLND----------KLKKNKDKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 275 DQVSKKLSSIEASLKIKNatdlqqaklreseisQKLTNVNVKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSK 354
Cdd:TIGR04523 99 NKLNSDLSKINSEIKNDK---------------EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 355 ILPRYQELTKEEAMYKLQLASLQQKQRDLILK--KGEYARF--KSKDERDTWIHSEIEELKSSIQNLNELESQLQMDRTS 430
Cdd:TIGR04523 164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKllKLELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 6322387 431 LRKQYSAIDEEIEELIDSINgpDTKGQLEDFDSELIHLKQKLSESLDTRKEL 482
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQN--KIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
316-513 |
3.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 316 KIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILpRYQELTKEE---AMYKLQLASLQQKQRDLILKKGEYAR 392
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEidvASAEREIAELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 393 FKSkderdtwihsEIEELKSSIQNLNELESQLQMDRTSLRKQYSAIDEEIEELIDSINGPDTKGQLEDFDseliHLKQKL 472
Cdd:COG4913 690 LEE----------QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----LLEERF 755
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 6322387 473 SESLDTRKELwRKEQKLQTVLETLLSDVNQNQRNVNETMSR 513
Cdd:COG4913 756 AAALGDAVER-ELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1125-1195 |
3.44e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.99 E-value: 3.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322387 1125 QLSGGQKTVCAIALILAIQmvdpASFYLFDEIDAALDKQYRTAVATLLKELSKNAQ--FICTTFRTDMLQVAD 1195
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQ----PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKtvFVITHTMEHVLEVAD 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
777-953 |
3.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 777 FAQEKLNTFENDLlQEFDSELSKEEKErLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELESklipQENDLESKMS 856
Cdd:COG3883 13 FADPQIQAKQKEL-SELQAELEAAQAE-LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE----AEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 857 EVGD----AFIFGLQDELKELQLEKESVEK------------QHENAVLElgtvqrEIESLIAEETNNKKLLEKANNQQR 920
Cdd:COG3883 87 ELGEraraLYRSGGSVSYLDVLLGSESFSDfldrlsalskiaDADADLLE------ELKADKAELEAKKAELEAKLAELE 160
|
170 180 190
....*....|....*....|....*....|...
gi 6322387 921 LLLKKLDNFQKSVEKTMIKKTTLVTRREELQQR 953
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1125-1175 |
3.67e-03 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 41.43 E-value: 3.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 6322387 1125 QLSGGQKTVCAIALILAiqmVDPaSFYLFDEIDAALDKQYRTAVATLLKEL 1175
Cdd:COG1123 404 ELSGGQRQRVAIARALA---LEP-KLLILDEPTSALDVSVQAQILNLLRDL 450
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1125-1221 |
3.74e-03 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 41.22 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1125 QLSGGQKTVCAIALILAiqmVDPaSFYLFDEIDAALDKQYRTAVATLLKELSKNAQFIcTTFRT----DMLQVADKFFRV 1200
Cdd:PRK10851 136 QLSGGQKQRVALARALA---VEP-QILLLDEPFGALDAQVRKELRRWLRQLHEELKFT-SVFVThdqeEAMEVADRVVVM 210
|
90 100
....*....|....*....|...
gi 6322387 1201 KYEN--KISTVIEVNREEAIGFI 1221
Cdd:PRK10851 211 SQGNieQAGTPDQVWREPATRFV 233
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
695-1050 |
3.86e-03 |
|
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: 41.64 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 695 RSQHKKILEELDFVR----NELNDIDTKIDQvngnIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILK--- 767
Cdd:pfam15921 144 RNQLQNTVHELEAAKclkeDMLEDSNTQIEQ----LRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRslg 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 768 ------LEKLNTNRTFAQEKLNTFEnDLLQEFDSE-------LSKEEKERLESL-----------TKEISAAHNKLNITS 823
Cdd:pfam15921 220 saiskiLRELDTEISYLKGRIFPVE-DQLEALKSEsqnkielLLQQHQDRIEQLiseheveitglTEKASSARSQANSIQ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 824 DALEGITTTIDSLNaeleSKLIPQENDLESKMSEvgdafifgLQDELKELQL----EKESVEKQHENAVLELGTVQREIE 899
Cdd:pfam15921 299 SQLEIIQEQARNQN----SMYMRQLSDLESTVSQ--------LRSELREAKRmyedKIEELEKQLVLANSELTEARTERD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 900 SLIAEETNNKKLLEKannqqrlLLKKLDNFQK--SVEKtmikkttlvtrreELQQRI--REIGllpedalvndfSDITSD 975
Cdd:pfam15921 367 QFSQESGNLDDQLQK-------LLADLHKREKelSLEK-------------EQNKRLwdRDTG-----------NSITID 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 976 QLLQRLNDMNTEISGLKNVNK-----------RAFENFKKFNERRKDLAERASELDESKDSIQDLIVKLKQQKVnAVDST 1044
Cdd:pfam15921 416 HLRRELDDRNMEVQRLEALLKamksecqgqmeRQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKM-TLESS 494
|
....*.
gi 6322387 1045 FQKVSE 1050
Cdd:pfam15921 495 ERTVSD 500
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
191-450 |
3.92e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 191 QKKIQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLYDRELNEVINQMERLDGDYNNTVYSSEQYIQELDKR 270
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRY 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 271 EDM-IDQVSKKLSSIEASLKIKNATDLQQAKLRESEISQKLTNvnvkIKDVQQQIESNeeqrnldsatLKEIKSIIEQRK 349
Cdd:PRK01156 556 KSLkLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLND----LESRLQEIEIG----------FPDDKSYIDKSI 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 350 QKLSKILPRYQELTKEEAMYKLQLASLQQKQRDLilkKGEYARFKSKDERDTWIHSEIEELKSsiqNLNELESQLQ---M 426
Cdd:PRK01156 622 REIENEANNLNNKYNEIQENKILIEKLRGKIDNY---KKQIAEIDSIIPDLKEITSRINDIED---NLKKSRKALDdakA 695
|
250 260
....*....|....*....|....
gi 6322387 427 DRTSLRKQYSAIDEEIEELIDSIN 450
Cdd:PRK01156 696 NRARLESTIEILRTRINELSDRIN 719
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
689-1037 |
3.98e-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: 41.54 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 689 KNLNESRSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKLILEESLNAIILKL 768
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 769 EKLNTNRTFAQEKLNtfENDLLQEFDSELSKEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLNAELesklipqe 848
Cdd:TIGR04523 197 LKLELLLSNLKKKIQ--KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK-------- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 849 NDLESKMSEVGDA--FIFGLQDELKELQLEKESVEKQHENAVL-----ELGTVQREIESLIAEETNNKKLLEKANNQQRL 921
Cdd:TIGR04523 267 KQLSEKQKELEQNnkKIKELEKQLNQLKSEISDLNNQKEQDWNkelksELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 922 LLKKLDNfqksvektmiKKTTLVTRREELQQRIREIGLLPEDalvNDFSDITSDQLLQRLNDMNTEISGLKNVNKRAFEN 1001
Cdd:TIGR04523 347 LKKELTN----------SESENSEKQRELEEKQNEIEKLKKE---NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
330 340 350
....*....|....*....|....*....|....*.
gi 6322387 1002 FKKFNERRKDLAERASELDESKDSIQDLIVKLKQQK 1037
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQD 449
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
747-921 |
4.02e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 747 LNTKKNEKLILEESLNAIILKLEKLNTNRTFAQEKLNTFENDLLQefdselsKEEKERLESLTKEISAAHNKLNITSDAL 826
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-------LEKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 827 EGITTTIDSLnAELESKLIPQENDLESKMSEVGDAFI---FGLQDELKELQLEKESVEKQHENAVLELGTVQREIESLIA 903
Cdd:COG4717 149 EELEERLEEL-RELEEELEELEAELAELQEELEELLEqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170
....*....|....*...
gi 6322387 904 EETNNKKLLEKANNQQRL 921
Cdd:COG4717 228 ELEQLENELEAAALEERL 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1123-1178 |
4.59e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 41.33 E-value: 4.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 6322387 1123 VEQLSGG--QKTvcAIALILAIQmvdpASFYLFDEIDAALDKQYRTAVATLLKELSKN 1178
Cdd:PRK13409 210 ISELSGGelQRV--AIAAALLRD----ADFYFFDEPTSYLDIRQRLNVARLIRELAEG 261
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
180-449 |
4.60e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 180 KASLKKMEETEQKKIQI-----NKEMGELNS---------KLSEMEQERKEL---------EKYNELERNRKIYQFTLYD 236
Cdd:PRK04778 25 KRNYKRIDELEERKQELenlpvNDELEKVKKlnltgqseeKFEEWRQKWDEIvtnslpdieEQLFEAEELNDKFRFRKAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 237 RELNEVINQMERLDGDYNNTVysseQYIQELDKRE----DMIDQVSKKLSSIEASLkIKNATDLQQAklrESEISQKLTN 312
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQIL----EELQELLESEeknrEEVEQLKDLYRELRKSL-LANRFSFGPA---LDELEKQLEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 313 VNVKIkdvqQQIESNEEQRNLDSA--TLKEIKSIIEQRKQKLSKILPRYQELTKEeamYKLQLASLQQKQRDLILKKgeY 390
Cdd:PRK04778 177 LEEEF----SQFVELTESGDYVEAreILDQLEEELAALEQIMEEIPELLKELQTE---LPDQLQELKAGYRELVEEG--Y 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 6322387 391 ArFKSKDerdtwIHSEIEELKSSIQNLNELESQLQMDRTSlrKQYSAIDEEIEELIDSI 449
Cdd:PRK04778 248 H-LDHLD-----IEKEIQDLKEQIDENLALLEELDLDEAE--EKNEEIQERIDQLYDIL 298
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
28-53 |
4.63e-03 |
|
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: 40.45 E-value: 4.63e-03
10 20
....*....|....*....|....*.
gi 6322387 28 NVIIGSNGSGKSNFFAAIRFVLSDDY 53
Cdd:pfam13304 2 NVLIGPNGSGKSNLLEALRFLADFDA 27
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-956 |
5.50e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 685 LESLKNLNESRSQHKKILEELDFVRN-------ELNDIDTKIDQVNGNIRKVSNDRESV---LTNIEVYRTSLNTKKNEK 754
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEElikekekELEEVLREINEISSELPELREELEKLekeVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 755 LILEESLNAIILKLEKLNTNRTFAQEKLNTFENdllQEFDSELSKEEKERLESLTKEISAAHNKLNITSDALEGITTTID 834
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEE---KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 835 SLNAELEsklipqenDLESKMSEVGDafifgLQDELKELQLEKESVEKQHEnAVLELGTVQREIESLIAEETNNKKllEK 914
Cdd:PRK03918 325 GIEERIK--------ELEEKEERLEE-----LKKKLKELEKRLEELEERHE-LYEEAKAKKEELERLKKRLTGLTP--EK 388
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 6322387 915 ANnqqrlllKKLDNFQKSVEKTMIKKTTLVTRREELQQRIRE 956
Cdd:PRK03918 389 LE-------KELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
679-844 |
5.77e-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: 39.91 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 679 QHKRTRLESLKNLNES-RSQHKKILEELDFVRNELNDIDTKIDQVNGNIRKVSNDRESVLTNIEVYRTSLNTKKNEKlil 757
Cdd:COG1579 13 QELDSELDRLEHRLKElPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 758 eeSLNAIILKLEKLNTNRTFAQEKLntfendllqefdselsKEEKERLESLTKEISAAHNKLNITSDALEGITTTIDSLN 837
Cdd:COG1579 90 --EYEALQKEIESLKRRISDLEDEI----------------LELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
....*..
gi 6322387 838 AELESKL 844
Cdd:COG1579 152 AELEAEL 158
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
164-501 |
6.63e-03 |
|
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: 40.72 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 164 QLLEDVVGAKSFEVKLKASLKKMEETEQKK-----IQINKEMGELNSKLSEMEQERKELEKYNELERNRKIYQFTLyDRE 238
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSfsiltQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL-LRK 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 239 LNEVINQMERLDGDYNNT------VYSSEQYIQELDKREDMIDQVSKKLSSIEASLKIKNATDLQQAKLRE-SEISQKLT 311
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSqelalkLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQlTYWKEMLA 700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 312 NVNVKIKDVQQQIESNEEQRNLDSATLKEIKSIIEQRKQKLSKILPRYQELTKEeAMYKLQLASLQQKQRDLILKK--GE 389
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART-VLKARTEAHFNNNEEVTAALQtgAE 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 390 YARFKSKderdtwIHSEIEELKSSIQNLNELESQLQmdrtslrkQYSAIDEEIEELIDSINGPD---TKGQLEDFDSELI 466
Cdd:TIGR00618 780 LSHLAAE------IQFFNRLREEDTHLLKTLEAEIG--------QEIPSDEDILNLQCETLVQEeeqFLSRLEEKSATLG 845
|
330 340 350
....*....|....*....|....*....|....*
gi 6322387 467 HLKQKLSESLDTRKELWRKEQKlQTVLETLLSDVN 501
Cdd:TIGR00618 846 EITHQLLKYEECSKQLAQLTQE-QAKIIQLSDKLN 879
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
3-79 |
6.73e-03 |
|
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: 39.97 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 3 IKRVIIKGFKTYRNETIidNFSPHQNVIIGSNGSGKSNFFAAIRFVL---SDDYSNLKReerqgLIHQGSGGSVMSASVE 79
Cdd:cd03242 1 LKSLELRNFRNYAELEL--EFEPGVTVLVGENAQGKTNLLEAISLLAtgkSHRTSRDKE-----LIRWGAEEAKISAVLE 73
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
1-66 |
7.30e-03 |
|
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: 39.17 E-value: 7.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1 MYIKRVIIKGFKTYRNETIIDnFSPHQN----VIIGSNGSGKSNFFAAIRFVLsddYSNLKREERQGLIH 66
Cdd:cd03279 1 MKPLKLELKNFGPFREEQVID-FTGLDNnglfLICGPTGAGKSTILDAITYAL---YGKTPRYGRQENLR 66
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
177-502 |
8.36e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 177 VKLKASLKKMEE----TEQKKIQINKEMGELNSKLSEME-QERKELEKYNELERNRKIYQFTLYDRElnevinqmERLDG 251
Cdd:pfam01576 127 VTTEAKIKKLEEdillLEDQNSKLSKERKLLEERISEFTsNLAEEEEKAKSLSKLKNKHEAMISDLE--------ERLKK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 252 DynntvyssEQYIQELDKRE--------DMIDQVSKkLSSIEASLKIKNAT---DLQQAKLRESEISQKLTNVNVKIKDV 320
Cdd:pfam01576 199 E--------EKGRQELEKAKrklegestDLQEQIAE-LQAQIAELRAQLAKkeeELQAALARLEEETAQKNNALKKIREL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 321 QQQIesNEEQRNLDSATLKEIKSiiEQRKQKLSKILpryqELTKEEAMYKLQLASLQQKQRDLilKKGEYARFKSKDERD 400
Cdd:pfam01576 270 EAQI--SELQEDLESERAARNKA--EKQRRDLGEEL----EALKTELEDTLDTTAAQQELRSK--REQEVTELKKALEEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 401 TWIH-SEIEELK----SSIQNLNELESQLQMDRTSLRKQYSAIDEEIEEL---IDSINGP--DTKGQLEDFDSELIHLKQ 470
Cdd:pfam01576 340 TRSHeAQLQEMRqkhtQALEELTEQLEQAKRNKANLEKAKQALESENAELqaeLRTLQQAkqDSEHKRKKLEGQLQELQA 419
|
330 340 350
....*....|....*....|....*....|..
gi 6322387 471 KLSESLDTRKELWRKEQKLQTVLETLLSDVNQ 502
Cdd:pfam01576 420 RLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1123-1195 |
9.20e-03 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 39.31 E-value: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322387 1123 VEQLSGGQKTVCAIALILAiqmvDPASFYLFDEIDAALDKQYRTAVATLLKELSKNAQ---------FICTTFRTDMLQV 1193
Cdd:cd03237 113 VPELSGGELQRVAIAACLS----KDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEktafvvehdIIMIDYLADRLIV 188
|
..
gi 6322387 1194 AD 1195
Cdd:cd03237 189 FE 190
|
|
| |
