|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
3-1203 |
1.27e-113 |
|
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: 383.55 E-value: 1.27e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 3 HLELLLVENFKSWRGRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKT-TNLRVKNIQELIHGAhtGKPVSSSASVT 81
Cdd:pfam02463 1 YLKRIEIEGFKSYAKTVILPFSPGFTAIVGPNGSGKSNILDAILFVLGERSaKSLRSERLSDLIHSK--SGAFVNSAEVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 82 IIYIEDSGEEKT-------FTRIIRGGCSEYHFGDKPVSRSVYVAQLENIGIIVKAQNCLVFQGTVESISMKKPKERTQF 154
Cdd:pfam02463 79 ITFDNEDHELPIdkeevsiRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPERRLEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 155 FEEISTSGEFIGEYEAKKKKLQKAEEDAQFHFNVKKNVAAERKHAKIEKEEAEHYQNLLEELKINKIQLMLFQLYYNEEK 234
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 235 INVLNTELEQMDGNLSVVKDTLSHHENIFKAKKKDYGMLTRQLQQTAKELKSVEAILNQKRPQYIKAKENTSHHLKKLDL 314
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 315 SKKLITDNEKQCSKQEDGIRALVAELADLDRAWKSFEKQMEEKILQKGRDIELENSQLDRYKLLKEQVRRKVGIMTQQLE 394
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 395 KLQWEQKAEKERLAFEKRRHGDTQGNLKQIKEQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEEALKKEIENTKSRMSEVN 474
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 475 EELSLIRNELQNAGIDNHEGKRQQKRAEVLEHLKRLYPDSVFGRLLDLCHPIHKKYQLAVTKLFGRYMVAIVVASEKIAK 554
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 555 DCIRFLKAERAEPETFLALDYLDIKPINERLREIKGCKMMIDVIKTQFPQLKKVIQFVCGNGLVCETVEEARHIAFGGPE 634
Cdd:pfam02463 559 EVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLK 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 635 RRKAVALDGTLFLKSGVISGGSSDLKHKALCWDEKELHNLRDKrsqlvqelkelmktlrketdlkqiQTLVQGTNTRLKY 714
Cdd:pfam02463 639 ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQEL------------------------QEKAESELAKEEI 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 715 SQNELEMIKKkhlatfyrEQSQLQSELLNIDSQCTMLSEGINKQQQKIEEFQDKIDEVEDDIFQDFCEEIGVENIREFEN 794
Cdd:pfam02463 695 LRRQLEIKKK--------EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK 766
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 795 KHVKQQQENDQKRLEFEKQKTRLNIQLEYSRNQLKKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEElmvKQEQIK 874
Cdd:pfam02463 767 SELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE---LALELK 843
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 875 EVLATQSSNIEKIHIQIEEERKKVLavdrevgklqkevviiqgsLEQKLLEKHNLLLDCKVQDIDISLVLGSLEDIIEME 954
Cdd:pfam02463 844 EEQKLEKLAEEELERLEEEITKEEL-------------------LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEE 904
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 955 LTETESTQATADIYEK-----EASIQIDYSPLREDLKALQSDKEVEAHLTLLLQQVASQENTLLKTTAPNLRAQENLKTV 1029
Cdd:pfam02463 905 ESQKLNLLEEKENEIEerikeEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFE 984
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1030 RDKFQESADVFEASRKEARICRQEFEQVKRRRYDAFSQCFEHISVSIDQIYKKLCRNNSAQAFLSPENPEEPYLDGISYN 1109
Cdd:pfam02463 985 EKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEIS 1064
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1110 CVAPGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQSqEQFQMIIISLKEEFY 1189
Cdd:pfam02463 1065 ARPPGKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELS-KNAQFIVISLREEML 1143
|
1210
....*....|....
gi 17978290 1190 SKADALIGVYPEHN 1203
Cdd:pfam02463 1144 EKADKLVGVTMVEN 1157
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3-1198 |
1.02e-91 |
|
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: 321.63 E-value: 1.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 3 HLELLLVENFKSWRGRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTN-LRVKNIQELIHGAHTGKPVSSsASVT 81
Cdd:TIGR02169 1 YIERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKaMRAERLSDLISNGKNGQSGNE-AYVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 82 IIYIEDSGEEKTFTRIIR-------GGCSEYHFGDKPVSRSVYVAQLENIGIIVKAQNcLVFQGTVESISMKKPKERTQF 154
Cdd:TIGR02169 80 VTFKNDDGKFPDELEVVRrlkvtddGKYSYYYLNGQRVRLSEIHDFLAAAGIYPEGYN-VVLQGDVTDFISMSPVERRKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 155 FEEISTSGEFIGEYEAKKKKLQKAEEDAQFHFNVKKNVAAERKHAKIEKEEAEHYQNLLEELKINKIQLMLfqlyyneEK 234
Cdd:TIGR02169 159 IDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELL-------KE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 235 INVLNTELEQMDGNLSvvkdtlshhenifkAKKKDYGMLTRQLQQTAKELKSVEAILNQKRPQYIKAKENTShhlkklDL 314
Cdd:TIGR02169 232 KEALERQKEAIERQLA--------------SLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ------LR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 315 SKKLITDNEKQCSKQEDGIRALVAELADLDRAwksfEKQMEEKILQKGRDIELENSQLDRYKLLKEQVRRKVGIMTQQLE 394
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEER----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 395 KLQW--------------EQKAEKERLAFEKRRHGDTQGN-------LKQIKEQIEEHKKRIEKLEEYTKTCMDCLEDK- 452
Cdd:TIGR02169 368 DLRAeleevdkefaetrdELKDYREKLEKLKREINELKREldrlqeeLQRLSEELADLNAAIAGIEAKINELEEEKEDKa 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 453 -------------KQQEEALKKEIENTKSRMSEVNEELSLIRNELQNAgidnhEGKRQQKRAEVL-----EHLKRLYPDS 514
Cdd:TIGR02169 448 leikkqewkleqlAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA-----EAQARASEERVRggravEEVLKASIQG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 515 VFGRLLDLCHpIHKKYQLAVTKLFGRYMVAIVVASEKIAKDCIRFLKAERAEPETFLALDYLDIKPINERLREIKGC-KM 593
Cdd:TIGR02169 523 VHGTVAQLGS-VGERYATAIEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGViGF 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 594 MIDVIKTQfPQLKKVIQFVCGNGLVCETVEEARHIafGGPERrkAVALDGTLFLKSGVISGGSSDLKHKAL--CWDEKEL 671
Cdd:TIGR02169 602 AVDLVEFD-PKYEPAFKYVFGDTLVVEDIEAARRL--MGKYR--MVTLEGELFEKSGAMTGGSRAPRGGILfsRSEPAEL 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 672 HNLRDKRSQLVQELKELMKTLRK-ETDLKQIQTLVQGTNTRLKYSQNELEMIKKKH------LATFYREQSQLQSELLNI 744
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRiENRLDELSQELSDASRKIGEIEKEIEQLEQEEeklkerLEELEEDLSSLEQEIENV 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 745 DSQCTMLSEGINKQQQKIEEFQDKIDEVEDDIFQDFCEEIGVEnIREFEnkhvKQQQENDQKRLEFEKQKTRLNIQLEYS 824
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAE-LSKLE----EEVSRIEARLREIEQKLNRLTLEKEYL 831
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 825 RNQLKKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELMVKQEQIKEVLATQSSNIEKIHIQIEEERKKVLAVDRE 904
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 905 VGKLQKEVVIIQGSLEQkLLEKHNLLLDCKVQDIDISLVLGSLEDIIEMELTETESTQATADIyekeasiqidysplreD 984
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEA-LEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV----------------N 974
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 985 LKALQSDKEVEAHLtlllqqvasqentllkttapnlraqenlktvrDKFQESADVFEASRKEARICRQEFEQVKRrryDA 1064
Cdd:TIGR02169 975 MLAIQEYEEVLKRL--------------------------------DELKEKRAKLEEERKAILERIEEYEKKKR---EV 1019
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1065 FSQCFEHISVSIDQIYKKLcrnNSAQAFLSPENPEEPYLDGISYNCVAPGKRFMPMDNLSGGEKCVAALALLFAVHSFRP 1144
Cdd:TIGR02169 1020 FMEAFEAINENFNEIFAEL---SGGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKP 1096
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....
gi 17978290 1145 APFFVLDEVDAALDNTNIGKVSSYIKEQSQEQfQMIIISLKEEFYSKADALIGV 1198
Cdd:TIGR02169 1097 SPFYAFDEVDMFLDGVNVERVAKLIREKAGEA-QFIVVSLRSPMIEYADRAIGV 1149
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
4-148 |
4.72e-81 |
|
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: 265.98 E-value: 4.72e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 4 LELLLVENFKSWRGRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTNLRVKNIQELIHGAHTGKPVSSSASVTII 83
Cdd:cd03275 1 LKRLELENFKSYKGRHVIGPFDRFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARVGKPDSNSAYVTAV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17978290 84 YIEDSGEEKTFTRIIRGGCSEYHFGDKPVSRSVYVAQLENIGIIVKAQNCLVFQGTVESISMKKP 148
Cdd:cd03275 81 YEDDDGEEKTFRRIITGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNP 145
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-1198 |
3.93e-76 |
|
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: 275.78 E-value: 3.93e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 12 FKSWRGRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGE-KTTNLRVKNIQELIHGAHTGKPVSSSASVTIIYIEDSG- 89
Cdd:TIGR02168 10 FKSFADPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLGEqSAKALRGGKMEDVIFNGSETRKPLSLAEVELVFDNSDGl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 90 ------EEKTFTR-IIRGGCSEYHFGDKPVSRSVYVAQLENIGIIVKAQNcLVFQGTVESISMKKPKERTQFFEEisTSG 162
Cdd:TIGR02168 90 lpgadySEISITRrLYRDGESEYFINGQPCRLKDIQDLFLDTGLGKRSYS-IIEQGKISEIIEAKPEERRAIFEE--AAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 163 efIGEYEAKKKKLQKAEEDAQFHFNVKKNVAAER----KHAKIEKEEAEHYQNLLEELKINKIQLMLF-------QLYYN 231
Cdd:TIGR02168 167 --ISKYKERRKETERKLERTRENLDRLEDILNELerqlKSLERQAEKAERYKELKAELRELELALLVLrleelreELEEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 232 EEKINVLNTELEQMDGNLSVVKDTLSHHENIFKAKKKDYGMLTRQLQQTAKELKSVE---AILNQKRPQYIKAKENTSHH 308
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEqqkQILRERLANLERQLEELEAQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 309 LKKLDLSKKLITDNEKQCSKQEDGIRALVAELADLDRAWKSFEKQMEEKILQKGRDIELENSQLDRYKLLKEQVRRKVGI 388
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 389 MTQQLEKLQweqkAEKERLAFEKRRHGD--TQGNLKQIKEQIEEHKKRIEKLEEytktcmdCLEDKKQQEEALKKEIENT 466
Cdd:TIGR02168 405 LEARLERLE----DRRERLQQEIEELLKklEEAELKELQAELEELEEELEELQE-------ELERLEEALEELREELEEA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 467 KSRMSEVNEELSLIRNELQ--NAGIDNHEGKrQQKRAEVLEHLKRLypDSVFGRLLDLCHpIHKKYQLAVTKLFGRYMVA 544
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDslERLQENLEGF-SEGVKALLKNQSGL--SGILGVLSELIS-VDEGYEAAIEAALGGRLQA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 545 IVVASEKIAKDCIRFLKAERAEPETFLALDYLDIKPIN----ERLREIKGCKMMIDVIKTQFPQLKKVIQFVCGNGLVCE 620
Cdd:TIGR02168 550 VVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQgndrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 621 TVEEARHIAFGGPERRKAVALDGTLFLKSGVISGGSSDLKHKALCwDEKELHNLRDKRSQLVQELKELMKTL-------- 692
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILE-RRREIEELEEKIEELEEKIAELEKALaelrkele 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 693 RKETDLKQIQTLVQGTNTRLKYSQNELEMIKKKHlATFYREQSQLQSELLNIDSQCTMLSEGINKQQQKIEEFQDKIDEV 772
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEV-EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 773 EDDIfqdfceeigvenirefeNKHVKQQQENDQKRLEFEKQKTRLNIQLEYSRNQLKKKLNNIDTLKTTIQKGKEDIDNL 852
Cdd:TIGR02168 788 EAQI-----------------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 853 KKTEEECLKIVEELMVKQEQIKEVLATQSSNIEKIHIQIEEERKKVLAVDREVGKLQKEVVIIQGSLEQKLLEKHNLLLD 932
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 933 CKVQDIDISLVLGSLEDIIEMELTETESTQATADIYEKEASIQIDYspLREDLKALqsdKEVeahltlllqqvasqentl 1012
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR--LENKIKEL---GPV------------------ 987
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1013 lkttapNLRAQENLKTVRDKF----QESADVFEASRKEARICRQEFEQVKRRrydaFSQCFEHISVSIDQIYKKLCRNNS 1088
Cdd:TIGR02168 988 ------NLAAIEEYEELKERYdfltAQKEDLTEAKETLEEAIEEIDREARER----FKDTFDQVNENFQRVFPKLFGGGE 1057
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1089 AQ-AFLSPENPEEPyldGISYNCVAPGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSS 1167
Cdd:TIGR02168 1058 AElRLTDPEDLLEA---GIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFAN 1134
|
1210 1220 1230
....*....|....*....|....*....|.
gi 17978290 1168 YIKEQSqEQFQMIIISLKEEFYSKADALIGV 1198
Cdd:TIGR02168 1135 LLKEFS-KNTQFIVITHNKGTMEVADQLYGV 1164
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1112-1215 |
4.18e-65 |
|
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: 220.91 E-value: 4.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1112 APGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQSQEQFQMIIISLKEEFYSK 1191
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREQAGPNFQFIVISLKEEFFSK 224
|
90 100
....*....|....*....|....
gi 17978290 1192 ADALIGVYPEHnECMFSHVLTLDL 1215
Cdd:cd03275 225 ADALVGVYRDQ-ECNSSKVLTLDL 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-1198 |
2.13e-47 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 184.76 E-value: 2.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 3 HLELLLVENFKSWRGRQVIgPF-KRFTCIIGPNGSGKSNVMDALSFVMGE-KTTNLRVKNIQELIH-GAHTGKPVSSsAS 79
Cdd:COG1196 2 RLKRLELAGFKSFADPTTI-PFePGITAIVGPNGSGKSNIVDAIRWVLGEqSAKSLRGGKMEDVIFaGSSSRKPLGR-AE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 80 VTIIyIEDSG-------EEKTFTRII-RGGCSEYHFGDKPVSRSVYVAQLENIGIIVKAQNcLVFQGTVESISMKKPKER 151
Cdd:COG1196 80 VSLT-FDNSDgtlpidyDEVTITRRLyRSGESEYYINGKPCRLKDIQDLFLDTGLGPESYS-IIGQGMIDRIIEAKPEER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 152 TQFFEEIStsGefIGEYEAKKK----KLQKAEEdaqfhfnvkkN----------VAAERKHAKIEKEEAEHYQNLLEELK 217
Cdd:COG1196 158 RAIIEEAA--G--ISKYKERKEeaerKLEATEE----------NlerledilgeLERQLEPLERQAEKAERYRELKEELK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 218 INKIQLMLFQLYYNEEKINVLNTELEQMDGNLSVVKDTLSHHENIFKAKKKDYGMLTRQLQQTAKELKSVEAILNQKRPQ 297
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 298 YIKAKENTSHHLKKLDLSKKLITDNEKQCSKQEDGIRALVAELADLDRAWKSFEKQMEEKILQKGRDIELENSQLDRYKL 377
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 378 LKEQVRRKVGIMTQQLEKLQWEQKAEKERLAFEKRRHGDTQGNLKQIKEQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEE 457
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 458 ALKKEIENTKSRMSEVNEELSLI-----RNELQNAGIDNHEGKRQQKRAEVLEHLKRLYPDSVFGRLLDLchpihKKYQL 532
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELaeaaaRLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE-----AAYEA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 533 AVTKLFGRYMVAIVVASEKIAKDCIRFLKAERAEPETFLALDylDIKPINERLREIKGCKMMIDVIKTQF------PQLK 606
Cdd:COG1196 539 ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD--KIRARAALAAALARGAIGAAVDLVASdlreadARYY 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 607 KVIQFVCGNGLVCETVEEARHIAFGGPERRKAVALDGTLFLKSGVISGGSSdlkhkalcwdEKELHNLRDKRSQLVQELK 686
Cdd:COG1196 617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSR----------RELLAALLEAEAELEELAE 686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 687 ELMKTLRKETDLKQIQtlvqgtntrlkysqnelemikkkhlatfyREQSQLQSELLNIDSQctmlseginkQQQKIEEFQ 766
Cdd:COG1196 687 RLAEEELELEEALLAE-----------------------------EEEERELAEAEEERLE----------EELEEEALE 727
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 767 DKIDEVEDDIFQDFCEEIGVENIREFENKHVKQQQENDQKRLEfekqktrlniqleysrnQLKKKLNNIdtlkttiqkgk 846
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE-----------------RLEREIEAL----------- 779
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 847 EDIDnlkkteeecLKIVEELmvkqeqiKEVlatqssniekihiqieEERKKVLAVDREVgkLQKEvviiqgsleqkllek 926
Cdd:COG1196 780 GPVN---------LLAIEEY-------EEL----------------EERYDFLSEQRED--LEEA--------------- 810
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 927 hnllldckvqdidislvLGSLEDIIEmeltetestqatadiyekeasiQIDysplredlkalqsdkeveahltlllqqva 1006
Cdd:COG1196 811 -----------------RETLEEAIE----------------------EID----------------------------- 822
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1007 sqentllkttapnlraqenlKTVRDKFQESadvfeasrkearicrqeFEQVKRRrydaFSQCFEHISvsidqiykklcrn 1086
Cdd:COG1196 823 --------------------RETRERFLET-----------------FDAVNEN----FQELFPRLF------------- 848
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1087 NSAQAFLSPENPEEPyLD-GISYNCVAPGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKV 1165
Cdd:COG1196 849 GGGEAELLLTDPDDP-LEtGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERF 927
|
1210 1220 1230
....*....|....*....|....*....|....
gi 17978290 1166 SSYIKEQSQE-QFqmIIISLKEEFYSKADALIGV 1198
Cdd:COG1196 928 AELLKEMSEDtQF--IVITHNKRTMEAADRLYGV 959
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1112-1198 |
5.99e-29 |
|
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: 115.25 E-value: 5.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1112 APGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQSqEQFQMIIISLKEEFYSK 1191
Cdd:cd03278 103 APGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFS-KETQFIVITHRKGTMEA 181
|
....*..
gi 17978290 1192 ADALIGV 1198
Cdd:cd03278 182 ADRLYGV 188
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
513-628 |
1.76e-25 |
|
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: 102.31 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 513 DSVFGRLLDLCHpIHKKYQLAVTKLFGRYMVAIVVASEKIAKDCIRFLKAERAEPETFLALDYLDIKPI-NERLREIK-- 589
Cdd:smart00968 1 PGVLGRVADLIS-VDPKYETALEAALGGRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPaGSKLREALlp 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 17978290 590 ---GCKMMIDVIKTQfPQLKKVIQFVCGNGLVCETVEEARHI 628
Cdd:smart00968 80 epgFVGPAIDLVEYD-PELRPALEYLLGNTLVVDDLETARRL 120
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1123-1203 |
2.80e-25 |
|
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: 103.93 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1123 LSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQSQEQFQMIIISLKEEFYSKADALIGVYPEH 1202
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQFIVITLKKEMFENADKLIGVLFVH 174
|
.
gi 17978290 1203 N 1203
Cdd:cd03239 175 G 175
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
4-147 |
5.21e-25 |
|
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213241 [Multi-domain] Cd Length: 212 Bit Score: 104.30 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 4 LELLLVENFKSWRGRQVIGPF-KRFTCIIGPNGSGKSNVMDALSFVMGEKTTNLRVKNIQELIHGAhTGKPVSSSASVTI 82
Cdd:cd03274 3 ITKLVLENFKSYAGEQVIGPFhKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNS-AGHPNLDSCSVEV 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17978290 83 iyiedsgeekTFTRIIrggcseyhfgDKPVSRSVyvaqleniGIIVKAQNCLVFQGTVESISM--KK 147
Cdd:cd03274 82 ----------HFQEII----------DKPLLKSK--------GIDLDHNRFLILQGEVEQIAQmpKK 120
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1113-1203 |
1.75e-24 |
|
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: 102.76 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1113 PGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQSQEQfQMIIISLKEEFYSKA 1192
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNA-QFIVISLRNNMFELA 196
|
90
....*....|.
gi 17978290 1193 DALIGVYPEHN 1203
Cdd:cd03274 197 DRLVGIYKTNN 207
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1123-1205 |
3.70e-21 |
|
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: 91.65 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1123 LSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQSQEQFQMIIISLKEEFYSKADALIGVYPEH 1202
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKKVI 157
|
...
gi 17978290 1203 NEC 1205
Cdd:cd03227 158 TGV 160
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
4-83 |
7.52e-20 |
|
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: 89.06 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 4 LELLLVENFKSWRGRQVIgPFKR-FTCIIGPNGSGKSNVMDALSFVMGEKTT-NLRVKNIQELIHGAHTGKPVSSSASVT 81
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPgLTAIVGPNGSGKSNIIDAIRWVLGEQSAkSLRGEKMSDVIFAGSETRKPANFAEVT 79
|
..
gi 17978290 82 II 83
Cdd:cd03278 80 LT 81
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
513-629 |
2.67e-19 |
|
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: 84.62 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 513 DSVFGRLLDLCHpIHKKYQLAVTKLFGRYMVAIVVASEKIAKDCIRFLKAERAEPETFLALDYLDIKPINERLREIKGCK 592
Cdd:pfam06470 2 KGVLGRLADLIE-VDEGYEKAVEAALGGRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRLKPRPRRPGADLKGGAG 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 17978290 593 MMIDVIKTQfPQLKKVIQFVCGNGLVCETVEEARHIA 629
Cdd:pfam06470 81 PLLDLVEYD-DEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
3-140 |
5.04e-19 |
|
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: 88.12 E-value: 5.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 3 HLELLLVENFKSWRGRQVIGPFKR-FTCIIGPNGSGKSNVMDALSFVMG-EKTTNLRVKNIQELIHgaHTGKPVSSSASV 80
Cdd:cd03273 2 HIKEIILDGFKSYATRTVISGFDPqFNAITGLNGSGKSNILDAICFVLGiTNLSTVRASNLQDLIY--KRGQAGITKASV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17978290 81 TIIYIEDS------GEEK----TFTRIIRGGCSEYHFGDKPVSRSVYVAQL-ENIGIIVKAQNCLVFQGTV 140
Cdd:cd03273 80 TIVFDNSDksqspiGFENypeiTVTRQIVLGGTNKYLINGHRAQQQRVQDLfQSVQLNVNNPHFLIMQGRI 150
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
4-84 |
2.48e-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: 83.90 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 4 LELLLVENFKSWRGRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTNLRVKNIQELIHGAhtGKPVSSSASVTII 83
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSNSFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGG--VKAGINSASVEIT 78
|
.
gi 17978290 84 Y 84
Cdd:cd03239 79 F 79
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1123-1199 |
1.12e-14 |
|
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: 75.41 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1123 LSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALD--NT-NIGKVssyIKEQ-SQEQFqmIIISLKEEFYSKADALIGV 1198
Cdd:cd03273 167 LSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDlsHTqNIGRM---IKTHfKGSQF--IVVSLKEGMFNNANVLFRT 241
|
.
gi 17978290 1199 Y 1199
Cdd:cd03273 242 R 242
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
7-159 |
2.70e-14 |
|
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: 73.83 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 7 LLVENFKSWRGRQVIGPF-KRFTCIIGPNGSGKSNVMDALSFVMGEKTTNLRVKNIQELIHgAHTGKPVsSSASVTII-- 83
Cdd:cd03272 4 VIIQGFKSYKDQTVIEPFsPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLH-EGSGPSV-MSAYVEIIfd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 84 ----YIEDSGEEKTFTRIIRGGCSEYHFGDKPVSRSVYVAQLENIGI-------IVKaqnclvfQGTVESISMKKPKErT 152
Cdd:cd03272 82 nsdnRFPIDKEEVRLRRTIGLKKDEYFLDKKNVTKNDVMNLLESAGFsrsnpyyIVP-------QGKINSLTNMKQDE-Q 153
|
....*..
gi 17978290 153 QFFEEIS 159
Cdd:cd03272 154 QEMQQLS 160
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1120-1198 |
3.02e-13 |
|
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: 70.75 E-value: 3.02e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17978290 1120 MDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQSqEQFQMIIISLKEEFYSKADALIGV 1198
Cdd:cd03272 156 MQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELS-DGAQFITTTFRPELLEVADKFYGV 233
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
352-926 |
1.14e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 352 KQMEEKILQKGRDIELENSQLDRYKLLKEQVRRKVgimtQQLEKLQWEQKAEKERLAFEKRRHGDTQGNLKQIKEQIEEH 431
Cdd:PRK03918 196 KEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 432 KKRIEKLEEYTKTcMDCLEDKKQQEEALKKEIENTKSRMSEVNEELSLIRNELQnaGIDNHEGKRQQKRAEVLEHLKRLy 511
Cdd:PRK03918 272 KKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN--GIEERIKELEEKEERLEELKKKL- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 512 pdSVFGRLLDLCHPIHKKYQLAVTKlfgryMVAIVVASEKIAKDCIRFLKAERAEPETFLALDYLDIKPINERLREIKGc 591
Cdd:PRK03918 348 --KELEKRLEELEERHELYEEAKAK-----KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK- 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 592 kmMIDVIKTQFPQLK--KVIQFVCGNGLVcetveearhiafggPERRKAVALDGTLFLKSgvisggssdlkhkalcwDEK 669
Cdd:PRK03918 420 --EIKELKKAIEELKkaKGKCPVCGRELT--------------EEHRKELLEEYTAELKR-----------------IEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 670 ELHNLRDKRSQLVQELKELMKTLRKETDLKQIQTLVQgtntRLKYSQNELEMIKKKHLATFYREQSQLQSELLNIDSQCt 749
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE----QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI- 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 750 mlsEGINKQQQKIEEFQDKIDEVEDDIfqDFCEEIGVENIREFENKHVKQQQENDQKRLEFEKQKTRLnIQLEYSRNQLK 829
Cdd:PRK03918 542 ---KSLKKELEKLEELKKKLAELEKKL--DELEEELAELLKELEELGFESVEELEERLKELEPFYNEY-LELKDAEKELE 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 830 KKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELMVK-----QEQIKEVLATQSSNIEKIHIQIEEERKKVLAVDRE 904
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
570 580
....*....|....*....|...
gi 17978290 905 VGKLQKEVVII-QGSLEQKLLEK 926
Cdd:PRK03918 696 LEKLKEELEEReKAKKELEKLEK 718
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-896 |
1.78e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 254 DTLS-HHENIFKAKKKdYGMLtRQLQQTAKELKSVEAILNQKRpqYIKAKENTSHHLKKLDLSKKLITDNEKQCSKQEDG 332
Cdd:COG4913 235 DDLErAHEALEDAREQ-IELL-EPIRELAERYAAARERLAELE--YLRAALRLWFAQRRLELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 333 IRALVAELADLDRAwksfEKQMEEKILQ-KGRDIELENSQLDRYKLLKEQVRRKVGIMTQQLEKLQWEQKAEKERLAfek 411
Cdd:COG4913 311 LERLEARLDALREE----LDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA--- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 412 rrhgDTQGNLKQIKEQIEEHKKRIEklEEYTKTcMDCLEDKKQQEEALKKEIENTKSRMSEVNEELSLIRNEL-QNAGID 490
Cdd:COG4913 384 ----ALRAEAAALLEALEEELEALE--EALAEA-EAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALaEALGLD 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 491 nhegkrqqkRAEVlehlkrlypdSVFGRLLDLcHPIHKKYQLAVTKLFGRYMVAIVVASEKIA-----------KDCIRF 559
Cdd:COG4913 457 ---------EAEL----------PFVGELIEV-RPEEERWRGAIERVLGGFALTLLVPPEHYAaalrwvnrlhlRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 560 LKAE---------RAEPETFLALdyLDIK--PINERLREikgckmmidviktqfpQLKKVIQFVCgnglvCETVEEARHi 628
Cdd:COG4913 517 ERVRtglpdperpRLDPDSLAGK--LDFKphPFRAWLEA----------------ELGRRFDYVC-----VDSPEELRR- 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 629 afggpeRRKAVALDGTLFLKSG--------------VIsGGSSDLKHKALcwdEKELHNLRDKRSQL---VQELKELMKT 691
Cdd:COG4913 573 ------HPRAITRAGQVKGNGTrhekddrrrirsryVL-GFDNRAKLAAL---EAELAELEEELAEAeerLEALEAELDA 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 692 LRKE-TDLKQIQTL------VQGTNTRLKYSQNELEMIKK--KHLATFYREQSQLQSELLNIDSQCTMLSEGINKQQQKI 762
Cdd:COG4913 643 LQERrEALQRLAEYswdeidVASAEREIAELEAELERLDAssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 763 EEFQDKIDEVEdDIFQDFCEEIGVENIREFENKHVKQQQENDQKRL--EFEKQKTRLNIQLEYSRNQLKKKLNN-IDTLK 839
Cdd:COG4913 723 EQAEEELDELQ-DRLEAAEDLARLELRALLEERFAAALGDAVERELreNLEERIDALRARLNRAEEELERAMRAfNREWP 801
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 17978290 840 TTIQKGKEDIDNLKKTEEECLKIVEE-LMVKQEQIKEVLATQSSN-IEKIHIQIEEERK 896
Cdd:COG4913 802 AETADLDADLESLPEYLALLDRLEEDgLPEYEERFKELLNENSIEfVADLLSKLRRAIR 860
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
11-97 |
1.16e-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: 58.53 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 11 NFKSWRGRQVIGPFK-RFTCIIGPNGSGKSNVMDALSFVMGEKTTNLRVKNiqelihGAHTGkPVSSSASVTIIYIED-- 87
Cdd:cd03227 6 RFPSYFVPNDVTFGEgSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS------GVKAG-CIVAAVSAELIFTRLql 78
|
90
....*....|
gi 17978290 88 SGEEKTFTRI 97
Cdd:cd03227 79 SGGEKELSAL 88
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
4-48 |
1.35e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 58.40 E-value: 1.35e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 17978290 4 LELLLVENFKSWRgrQVIGPFKRFTCIIGPNGSGKSNVMDALSFV 48
Cdd:COG4637 2 ITRIRIKNFKSLR--DLELPLGPLTVLIGANGSGKSNLLDALRFL 44
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
9-183 |
2.85e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.40 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 9 VENFKSWRGRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTNlRVKNIQELIHGAhtgkpvSSSASVTIIYiedS 88
Cdd:COG0419 7 LENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARS-RSKLRSDLINVG------SEEASVELEF---E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 89 GEEKTFtRIIRggcseyhfgdkpvsrsvyvaqlenigiivkaqnclvFQGTVESISMKKPKERTQFFEEISTsgefIGEY 168
Cdd:COG0419 77 HGGKRY-RIER------------------------------------RQGEFAEFLEAKPSERKEALKRLLG----LEIY 115
|
170
....*....|....*
gi 17978290 169 EAKKKKLQKAEEDAQ 183
Cdd:COG0419 116 EELKERLKELEEALE 130
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-894 |
6.13e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 6.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 4 LELLLVENFKSWRGRQVigPFKR-FTCIIGPNGSGKSNVMDA----LSFVMGEKTTNLRVKNIqelihgAHTGKpvsSSA 78
Cdd:PRK03918 3 IEELKIKNFRSHKSSVV--EFDDgINLIIGQNGSGKSSILEAilvgLYWGHGSKPKGLKKDDF------TRIGG---SGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 79 SVTIIYIEDSGEEKTFTRIIRG--------GCSEYHFGDKPVSRsvYVAQLENIGIIVKAqnCLVFQGTVESIsMKKPKE 150
Cdd:PRK03918 72 EIELKFEKNGRKYRIVRSFNRGesylkyldGSEVLEEGDSSVRE--WVERLIPYHVFLNA--IYIRQGEIDAI-LESDES 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 151 RTQFFEEISTsgefIGEYEAKKKKLQKaeedaqfhfnVKKNVAAERKHAKIEKEEAEHYQNLLEELKINKIQLmlfqlyy 230
Cdd:PRK03918 147 REKVVRQILG----LDDYENAYKNLGE----------VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEV------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 231 nEEKINVLNTELEQMDGNLSVVKDTLSHHENIfkakKKDYGMLTRQLQQTAKELKSVEAILNQKRpQYIKAKEntshhlk 310
Cdd:PRK03918 206 -LREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKELESLEGSKRKLEEKIRELE-ERIEELK------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 311 kldlskklitdnekqcsKQEDGIRALVAELADLDRAWKSFEKQME--EKILQKGRDIELEnsqLDRYKLLKEQVRRKVGI 388
Cdd:PRK03918 273 -----------------KEIEELEEKVKELKELKEKAEEYIKLSEfyEEYLDELREIEKR---LSRLEEEINGIEERIKE 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 389 MTQQLEKLQWEQKAEKE---RLAFEKRRHGDTQgNLKQIKEQIEEHKKRIEKLEeytktcmdcledkkqqEEALKKEIEN 465
Cdd:PRK03918 333 LEEKEERLEELKKKLKElekRLEELEERHELYE-EAKAKKEELERLKKRLTGLT----------------PEKLEKELEE 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 466 TKSRMSEVNEELSLIRNELQNAgidNHEGKRQQKRAEVLEHLKRLYPdsVFGRLLDLCH--PIHKKYQLAVTKlfgrymv 543
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGEL---KKEIKELKKAIEELKKAKGKCP--VCGRELTEEHrkELLEEYTAELKR------- 463
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 544 aivVASEKI-AKDCIRFLKAERAEPETFLaldyldikpinERLREIKGCKMMIDVIKTQFPQLKKViqfvcgnglvceTV 622
Cdd:PRK03918 464 ---IEKELKeIEEKERKLRKELRELEKVL-----------KKESELIKLKELAEQLKELEEKLKKY------------NL 517
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 623 EEARHiafggpERRKAVALDGTLFLKSGVISGGSSDLK-----HKALCWDEKELHNLRDKRSQLVQELKELMKTLRKETD 697
Cdd:PRK03918 518 EELEK------KAEEYEKLKEKLIKLKGEIKSLKKELEkleelKKKLAELEKKLDELEEELAELLKELEELGFESVEELE 591
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 698 LKqIQTLVQGTN--TRLKYSQNELEMIKKkhlatfyrEQSQLQSELlnidsqcTMLSEGINKQQQKIEEFQDKIDEVEdd 775
Cdd:PRK03918 592 ER-LKELEPFYNeyLELKDAEKELEREEK--------ELKKLEEEL-------DKAFEELAETEKRLEELRKELEELE-- 653
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 776 ifqdfcEEIGVENIREFENKHVKQQQENDQKRLEFEkqktrlniQLEYSRNQLKKKLNNIDTLKTTIQKGKEDIDNLKKT 855
Cdd:PRK03918 654 ------KKYSEEEYEELREEYLELSRELAGLRAELE--------ELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA 719
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 17978290 856 EEEclkiVEELMVKQEQIKEVLATQS-SNIEKIHIQIEEE 894
Cdd:PRK03918 720 LER----VEELREKVKKYKALLKERAlSKVGEIASEIFEE 755
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
4-96 |
1.65e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.99 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 4 LELLLVENFKSWRGRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVM-GEKTTNLRvkniqeliHGAHTGKPV---SSSAS 79
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALtGELPPNSK--------GGAHDPKLIregEVRAQ 72
|
90
....*....|....*..
gi 17978290 80 VTIIYIEDSGEEKTFTR 96
Cdd:cd03240 73 VKLAFENANGKKYTITR 89
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1123-1183 |
2.24e-07 |
|
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: 51.86 E-value: 2.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17978290 1123 LSGGEKCVAALALLFAvhsfRPAPFFVLDEVDAALDNTNIGKVSSYIKEQSQEQFQMIIIS 1183
Cdd:cd00267 81 LSGGQRQRVALARALL----LNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVT 137
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
669-1059 |
2.69e-07 |
|
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: 55.12 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 669 KELHNLRDKRSQLVQELKELMKTLrkETDLKQIQTLVQGTNTRLKYSQNElemikkkhlatfyreQSQLQSELLNIDSQC 748
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMY--EDKIEELEKQLVLANSELTEARTE---------------RDQFSQESGNLDDQL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 749 TMLSEGINKQQQKIEEFQDKIDEVEDdifQDFCEEIGVENIRefenkhvkqqQENDQKRLEFEKQKTRLNIQLEYSRNQL 828
Cdd:pfam15921 380 QKLLADLHKREKELSLEKEQNKRLWD---RDTGNSITIDHLR----------RELDDRNMEVQRLEALLKAMKSECQGQM 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 829 KKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELMVKqeqiKEVLATQSSNIEKIHIQIEEERKKVLAVDREVGKL 908
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAK----KMTLESSERTVSDLTASLQEKERAIEATNAEITKL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 909 QKEVVIIQGSLeQKLLEKHNLLLDCKVQDIDISLVLGSLEDIIEMELTETES-TQATADIYEKEASIQIDYSPLR----- 982
Cdd:pfam15921 523 RSRVDLKLQEL-QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENmTQLVGQHGRTAGAMQVEKAQLEkeind 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 983 -----EDLKALQSDK-----EVEAHLT-LLLQQVasqenTLLKTTAPNLRAQENLKTVRDKFQESAdvfEASRKEARICR 1051
Cdd:pfam15921 602 rrlelQEFKILKDKKdakirELEARVSdLELEKV-----KLVNAGSERLRAVKDIKQERDQLLNEV---KTSRNELNSLS 673
|
....*...
gi 17978290 1052 QEFEQVKR 1059
Cdd:pfam15921 674 EDYEVLKR 681
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
210-872 |
5.38e-07 |
|
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: 54.35 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 210 QNLLEELKI---NKIQLMLFQlyyNEEKINVLNTE--------LEQMDGNLSVVKDTLSHHENIFKAKKKDYGMLTRQLQ 278
Cdd:pfam15921 244 EDQLEALKSesqNKIELLLQQ---HQDRIEQLISEheveitglTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 279 QTAKELKSVEAILNQKRPQYIKAKENTSHHLKKLDLSKKLITDNEKQCSKQ----EDGIRALVAELADLDRAWkSFEKQM 354
Cdd:pfam15921 321 DLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnlDDQLQKLLADLHKREKEL-SLEKEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 355 EEKILQKG-----------RDIELENSQLDRYK-LLKEQVRRKVGIMTQQLEKLQWEQKAeKERLAFEKRRHGDTQGNLK 422
Cdd:pfam15921 400 NKRLWDRDtgnsitidhlrRELDDRNMEVQRLEaLLKAMKSECQGQMERQMAAIQGKNES-LEKVSSLTAQLESTKEMLR 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 423 QIKEQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEEALKKEIENTKSRMSEVNEELSLIRNE---LQNAGIDNHEGKRQQ- 498
Cdd:pfam15921 479 KVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMa 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 499 KRAEVLEHLKRlypdsvfgrlldlchPIHKKYQLAVTKlfGRYMVAIVVasekiakdcirflkaERAEPEtflaldyldi 578
Cdd:pfam15921 559 EKDKVIEILRQ---------------QIENMTQLVGQH--GRTAGAMQV---------------EKAQLE---------- 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 579 KPINERLREIKGCKMMIDVIKTQFPQLKKVIqfvcgNGLVCETVEearhIAFGGPERRKAValdgtlflksgvisggsSD 658
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARV-----SDLELEKVK----LVNAGSERLRAV-----------------KD 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 659 LKHKAlcwDE--KELHNLRDKRSQLVQELKELMKTLRKETDlkQIQTLVQGTNTRLKYSQNELEmikkkhlatfyREQSQ 736
Cdd:pfam15921 651 IKQER---DQllNEVKTSRNELNSLSEDYEVLKRNFRNKSE--EMETTTNKLKMQLKSAQSELE-----------QTRNT 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 737 LQSeLLNIDSQCTMLSEGINKQqqkIEEFQDKIDEVEDDIfqDFCEEIGVENIREfenKHVKQQQEN--DQKRLEFEKQK 814
Cdd:pfam15921 715 LKS-MEGSDGHAMKVAMGMQKQ---ITAKRGQIDALQSKI--QFLEEAMTNANKE---KHFLKEEKNklSQELSTVATEK 785
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17978290 815 TRLNIQLEYSRNQ---LKKKLNNIDTL--KTTIQKGK-EDIDNLKKTEEECLKIVEELMVKQEQ 872
Cdd:pfam15921 786 NKMAGELEVLRSQerrLKEKVANMEVAldKASLQFAEcQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
3-114 |
5.54e-07 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 53.23 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 3 HLELLLVENFKSWRgRQVIGPFKRFTCIIGPNGSGKSNVMDALSFV-MGektTNLRVKNIQELI-HGAhtgkpvsSSASV 80
Cdd:COG1195 1 RLKRLSLTNFRNYE-SLELEFSPGINVLVGPNGQGKTNLLEAIYLLaTG---RSFRTARDAELIrFGA-------DGFRV 69
|
90 100 110
....*....|....*....|....*....|....
gi 17978290 81 TIIYIEDSGEEKTFTRIIRGGCSEYHFGDKPVSR 114
Cdd:COG1195 70 RAEVERDGREVRLGLGLSRGGKKRVRINGKPVRR 103
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
9-48 |
2.12e-06 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 51.20 E-value: 2.12e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 17978290 9 VENFKSWRGRQVI------GPFKRFTCIIGPNGSGKSNVMDALSFV 48
Cdd:COG1106 7 IENFRSFKDELTLsmvasgLRLLRVNLIYGANASGKSNLLEALYFL 52
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
7-183 |
3.12e-06 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 49.03 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 7 LLVENFKSWRGrQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTNL-RVKNIQELIHGAHTGKPVSSSASVTIIYI 85
Cdd:pfam13476 1 LTIENFRSFRD-QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLkRKSGGGFVKGDIRIGLEGKGKAYVEITFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 86 EDSGE-----EKTFTRIIRGGCSEYHFGDKPVSRSVYVAQLENIGIIVKAQNCLVFQGTVESISMKKPKERTQFFEEIST 160
Cdd:pfam13476 80 NNDGRytyaiERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFLGQEREEEFERKEKKERLEELEK 159
|
170 180
....*....|....*....|...
gi 17978290 161 SgefIGEYEAKKKKLQKAEEDAQ 183
Cdd:pfam13476 160 A---LEEKEDEKKLLEKLLQLKE 179
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
27-274 |
3.30e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 50.47 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 27 FTCIIGPNGSGKSNVMDALSFvmgekttnlrVKNIQELIHGAHTGKPVSSSASVtIIYIEDSGEEKtftriiRGGCSEYH 106
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRF----------LADFDALVIGLTDERSRNGGIGG-IPSLLNGIDPK------EPIEFEIS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 107 FGDKPVSRSVYVAQLENIGIIVKAQNCLVFQGTVESISMKKPKERTQFFEEISTSGEFIGEYEAKKKKLQKAEEDAQFHF 186
Cdd:pfam13304 64 EFLEDGVRYRYGLDLEREDVEEKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 187 NVKK---NVAAERKHAKIEKEEAEHYQNLLEELKINKIQLMLFQLyYNEEKINVLNTELEQMDGNLSVVKDTLSHHENIF 263
Cdd:pfam13304 144 LLSIispLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRL-VRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLI 222
|
250
....*....|.
gi 17978290 264 KAKKKDYGMLT 274
Cdd:pfam13304 223 LLENGGGGELP 233
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1119-1198 |
3.88e-06 |
|
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: 49.14 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1119 PMDNLSGGEKCVAALALLFAVHSFRPA--PFFVLDEVDAALDNTNI-GKVSSYIKEQ-SQEQFQMIIISLKEEFYSKADA 1194
Cdd:cd03240 112 MRGRCSGGEKVLASLIIRLALAETFGSncGILALDEPTTNLDEENIeESLAEIIEERkSQKNFQLIVITHDEELVDAADH 191
|
....
gi 17978290 1195 LIGV 1198
Cdd:cd03240 192 IYRV 195
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
3-55 |
4.46e-06 |
|
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: 50.39 E-value: 4.46e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 17978290 3 HLELLLVENFKSWRgRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTN 55
Cdd:COG3593 2 KLEKIKIKNFRSIK-DLSIELSDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
333-511 |
5.38e-06 |
|
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: 49.15 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 333 IRALVAELADLDRAWKSFEKQMEEKIlqkgRDIELENSQLDRYKLLKEQVRRKVgimtQQLEKLQWEQKAEKERLAFEKr 412
Cdd:COG1579 26 LKELPAELAELEDELAALEARLEAAK----TELEDLEKEIKRLELEIEEVEARI----KKYEEQLGNVRNNKEYEALQK- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 413 rhgdtqgnlkqikeQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEEALKKEIENTKSRMSEVNEELSLIRNELQNAgIDNH 492
Cdd:COG1579 97 --------------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE-LEEL 161
|
170
....*....|....*....
gi 17978290 493 EGKRQQKRAEVLEHLKRLY 511
Cdd:COG1579 162 EAEREELAAKIPPELLALY 180
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
18-922 |
9.46e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.43 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 18 RQVIGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTNLRVKNiqELIHGAHTGKPVSSSASVTIIYIEDSGEEKTFTRI 97
Cdd:TIGR00606 21 KQIIDFFSPLTILVGPNGAGKTTIIECLKYICTGDFPPGTKGN--TFVHDPKVAQETDVRAQIRLQFRDVNGEECAVVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 98 I--------------RGGCSEYHFGDKpVSRSVYVAQ-----LENIGIIVKAQNCLVFQGTVESI-SMKKPKERTQFFEE 157
Cdd:TIGR00606 99 MvctqktkktefktlEGVITRYKHGEK-VSLSSKCAEidremISHLGVSKAVLNNVIFCHQEDSNwPLSEGKALKQKFDE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 158 ISTSGEFIGEYEAKKKKLQKAEEDAQFH--------------FNVKKNVAAERKHAKIEKEEAEHYQNLLEELK--INKI 221
Cdd:TIGR00606 178 IFSATRYIKALETLRQVRQTQGQKVQEHqmelkylkqykekaCEIRDQITSKEAQLESSREIVKSYENELDPLKnrLKEI 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 222 QLMLFQLYYNEEKINVL----------NTELEQM-----DGNLSVVKDTLSHHENIFKAKKKDYGMLTRQLQQTAKELKs 286
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALksrkkqmekdNSELELKmekvfQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 287 veaILNQKRPQYIKAKENTSHHLKKLDLSKKLiTDNEKQCSKQEDGIRALVAElADLDRAWKSFEKQMEEKILQKGRDIE 366
Cdd:TIGR00606 337 ---LLNQEKTELLVEQGRLQLQADRHQEHIRA-RDSLIQSLATRLELDGFERG-PFSERQIKNFHTLVIERQEDEAKTAA 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 367 ------LENSQLDRYKLLKEQVRRKVGIMTQQLEKLQWEQKaeKERLAFEKRRHGDTQGNLKQIKEQIEEHKKRIEKLEE 440
Cdd:TIGR00606 412 qlcadlQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK--QEELKFVIKELQQLEGSSDRILELDQELRKAERELSK 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 441 YTKTCMdcLEDKKQQEEALKKEIENTKSRMSEVNEELSLIRNELQNAGIDNHEGKRQQKRAEVLEHLKRLYPDSVFGRLL 520
Cdd:TIGR00606 490 AEKNSL--TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLG 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 521 DLchpihkKYQLAVTKLFGRYMVAIVVASEKIAKDCIRFLKAERAEPETFLALDYLD--IKPINERLREIKGCKMM---I 595
Cdd:TIGR00606 568 YF------PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEeqLSSYEDKLFDVCGSQDEesdL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 596 DVIKTQFPQLKKVIQFVCGnglvcETVEEARHIAFGGPERRKAVALDGTLFLKSGVISGGSSDLKHKALCWDEKElhnlr 675
Cdd:TIGR00606 642 ERLKEEIEKSSKQRAMLAG-----ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKL----- 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 676 dkrsqlvQELKELMKTLRKETDlkQIQTLVQGTNTRLKYSQNELEMIKKKhLATFYREQSQLQSellNIDSQCTMLsEGI 755
Cdd:TIGR00606 712 -------KSTESELKKKEKRRD--EMLGLAPGRQSIIDLKEKEIPELRNK-LQKVNRDIQRLKN---DIEEQETLL-GTI 777
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 756 NKQQQK----------IEEFQDKIDEVEDDIFQDFCEEIGVENIREFEnkHVKQQQENDQKRLEFEKQKTRLNIQLEYSR 825
Cdd:TIGR00606 778 MPEEESakvcltdvtiMERFQMELKDVERKIAQQAAKLQGSDLDRTVQ--QVNQEKQEKQHELDTVVSKIELNRKLIQDQ 855
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 826 NQ----LKKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELMVKQEQIKEVLATQSSNIEKIhiqIEEERKKVLAV 901
Cdd:TIGR00606 856 QEqiqhLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD---QQEKEELISSK 932
|
970 980
....*....|....*....|.
gi 17978290 902 DREVGKLQKEVVIIQGSLEQK 922
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKNI 953
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
321-1053 |
1.30e-05 |
|
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: 49.58 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 321 DNEKQCSKQEDGIRALVAELADLDRAWKSfEKQMEEKILQKgrdIELENSQLDRYKLLKEQVRrkvgimtqQLEKLQWEQ 400
Cdd:TIGR00618 209 CTPCMPDTYHERKQVLEKELKHLREALQQ-TQQSHAYLTQK---REAQEEQLKKQQLLKQLRA--------RIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 401 KA-EKERLAFEKRRHgdtqgnlkqiKEQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEEALKKEIENTKSRMSEVNEELSL 479
Cdd:TIGR00618 277 AVlEETQERINRARK----------AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 480 IRNELQNagiDNHEGKRQQKRAEVLEHlkrlypdsvFGRLLDLCHPIHKKYQlavtklfgryMVAIVVASEKIAKDCIRF 559
Cdd:TIGR00618 347 LQTLHSQ---EIHIRDAHEVATSIREI---------SCQQHTLTQHIHTLQQ----------QKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 560 LKAERAEPETFLAldyldikpineRLREIKGCKMMIDviKTQFPQLKKVIQfvCGNGLVCETVEEARHIAFggpERRKAV 639
Cdd:TIGR00618 405 LQREQATIDTRTS-----------AFRDLQGQLAHAK--KQQELQQRYAEL--CAAAITCTAQCEKLEKIH---LQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 640 ALDGTLFLKSGVisggssdlkhKALCWDEKELHNLRDKRSQLVQELKELMKTLRKETDLKQIQTLVQGTNTRL------- 712
Cdd:TIGR00618 467 SLKEREQQLQTK----------EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqrgeqt 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 713 -KYSQNELEMIK------KKHLATFYREQSQLQSELLNIDSQCTMLSEGINKQQQKIEEFQDKIDeveddifqdfceeig 785
Cdd:TIGR00618 537 yAQLETSEEDVYhqltseRKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE--------------- 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 786 vENIREFENKHVKQQQENDQKRLEFEKQKTRLNIQLEYSRNQLKKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEE 865
Cdd:TIGR00618 602 -KLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 866 LMVKQEQIKEVLATQSSNIEKIHIQIEEERKKVLAVDREVGKLQKEVVIIQGSLEQK------LLEKHNLLLDCKVQDID 939
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARedalnqSLKELMHQARTVLKART 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 940 ISLVLGSLEDIIEmELTETESTQATADIYEKEASIQIDYSPLREDLKALQSD-KEVEAHLTLLLQQVASQENTLLKTTAP 1018
Cdd:TIGR00618 761 EAHFNNNEEVTAA-LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEiPSDEDILNLQCETLVQEEEQFLSRLEE 839
|
730 740 750
....*....|....*....|....*....|....*.
gi 17978290 1019 NLRAQENLKTVRDKFQESADVF-EASRKEARICRQE 1053
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLaQLTQEQAKIIQLS 875
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
658-1198 |
5.24e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 658 DLKHKALcwdekELHNLRDKRSQLVQELKELMKTLRKETdlKQIQTLVQGTNTRLKYSQNELEMIKKkhlatfyrEQSQL 737
Cdd:PRK01156 350 DLNNQIL-----ELEGYEMDYNSYLKSIESLKKKIEEYS--KNIERMSAFISEILKIQEIDPDAIKK--------ELNEI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 738 QSELLNIDSQCTMLSEGINKQQQKIEEFQDKI-----------------DEVEDDIFQDFCEEIG--VENIREFEN--KH 796
Cdd:PRK01156 415 NVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgEEKSNHIINHYNEKKSrlEEKIREIEIevKD 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 797 VKQQQENDQKRLEF-EKQKTRLNI----QLEYSRNQLKKKLNNIDTLKTtiqkgKEDIDNLKKTEEECLKIvEELMVKQE 871
Cdd:PRK01156 495 IDEKIVDLKKRKEYlESEEINKSIneynKIESARADLEDIKIKINELKD-----KHDKYEEIKNRYKSLKL-EDLDSKRT 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 872 QIKEVLATQSS-NIEKIHIQIEEERKKVLAVDREVGKLQKEVVIIQGSLEQKLLE----------KHNLLLDCKVQdidI 940
Cdd:PRK01156 569 SWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREieneannlnnKYNEIQENKIL---I 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 941 SLVLGSLEDIIEMELTETESTQATADIYEKEASIQIDYSPLREDLKALQSDK-EVEAHLTLLLQQVA------SQENTLL 1013
Cdd:PRK01156 646 EKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRaRLESTIEILRTRINelsdriNDINETL 725
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1014 KTTAPNLRAQENLKTVRDKFQESAdVFEASRKEAricrQEFEQVKRRRYdAFSQCFEHISVSIDQIYK-KLCRNNSAQAf 1092
Cdd:PRK01156 726 ESMKKIKKAIGDLKRLREAFDKSG-VPAMIRKSA----SQAMTSLTRKY-LFEFNLDFDDIDVDQDFNiTVSRGGMVEG- 798
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1093 lspenpeepyldgisyncvapgkrfmpMDNLSGGEKCVAALALLFAVHSFRPA--PFFVLDEVDAALDN---TNIGKVSS 1167
Cdd:PRK01156 799 ---------------------------IDSLSGGEKTAVAFALRVAVAQFLNNdkSLLIMDEPTAFLDEdrrTNLKDIIE 851
|
570 580 590
....*....|....*....|....*....|.
gi 17978290 1168 YIKEQSQEQFQMIIISLKEEFYSKADALIGV 1198
Cdd:PRK01156 852 YSLKDSSDIPQVIMISHHRELLSVADVAYEV 882
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1120-1183 |
6.98e-05 |
|
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213243 [Multi-domain] Cd Length: 198 Bit Score: 45.28 E-value: 6.98e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17978290 1120 MDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNiGKVSS--YIKE-QSQEQFQMIIIS 1183
Cdd:cd03276 107 VKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVN-RKISTdlLVKEaKKQPGRQFIFIT 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
276-495 |
1.05e-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: 46.30 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 276 QLQQTAKELKSVEAILNQKRPQYIKAKENTSHHLKKLDLSKKLITDNEKQCSKQEDGIRALVAELADLDRAWKSFEKQME 355
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 356 EkilQKGRDIEL-----ENSQLDRYKLL------KEQVRRK--VGIMTQQLEKLQWEQKAEKERLAFEKRRHGDTQGNLK 422
Cdd:COG4942 101 A---QKEELAELlralyRLGRQPPLALLlspedfLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17978290 423 QIKEQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEEA----LKKEIENTKSRMSEVNEELSLIRNELQNAGIDNHEGK 495
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAelaeLQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
7-895 |
1.68e-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: 46.12 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 7 LLVENFKSWRGRQVI--GPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTnlRVKNIQELIHGAHTGKPVSSSASVTIIY 84
Cdd:TIGR00618 6 LTLKNFGSYKGTHTIdfTALGPIFLICGKTGAGKTTLLDAITYALYGKLP--RRSEVIRSLNSLYAAPSEAAFAELEFSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 85 iedSGEEKTFTRIIRggCSEYHF-GDKPVSRSVYV--AQLENIGIIVKAQNCLVF-----------------QGTVESIS 144
Cdd:TIGR00618 84 ---GTKIYRVHRTLR--CTRSHRkTEQPEQLYLEQkkGRGRILAAKKSETEEVIHdllkldyktftrvvllpQGEFAQFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 145 MKKPKERTQFFEEI--------------STSGEFIGEYEAKKKKLQ----KAEEDAQFHFNVKKNVAAERKHA----KIE 202
Cdd:TIGR00618 159 KAKSKEKKELLMNLfpldqytqlalmefAKKKSLHGKAELLTLRSQlltlCTPCMPDTYHERKQVLEKELKHLrealQQT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 203 KEEAEHYQNLLEELK-INKIQLMLFQLYYNEEKINVLNTELEQMDGNLSvvkdtLSHHENIFKAKKKDYGMLTRQLQQTA 281
Cdd:TIGR00618 239 QQSHAYLTQKREAQEeQLKKQQLLKQLRARIEELRAQEAVLEETQERIN-----RARKAAPLAAHIKAVTQIEQQAQRIH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 282 KELKSVEAILNQKRPQYIKAKENTSHHLKKLDLskklitdnEKQCSKQEDGIRaLVAELADLDRAWKSFEKQMEEKILQK 361
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL--------LQTLHSQEIHIR-DAHEVATSIREISCQQHTLTQHIHTL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 362 GRDIELENSQLDRYKLLKEQVRRKVG----------IMTQQLEKLQWEQKAEKERLAFEKRRHGDTQGNLKQIKEQIEEH 431
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQREQAtidtrtsafrDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQES 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 432 KKRIEKLEEYTKTcmdcLEDKKQQEEALKKEIENTKSRMSEVNEELSLIRNELQNAGIDNHEGKRQQKRAEVLEHlKRLY 511
Cdd:TIGR00618 465 AQSLKEREQQLQT----KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ-TYAQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 512 PDSVFGRLLDLCHPIHKKYQLAVTKlfgrymVAIVVASEKIAKDCIRFLKAErAEPETFLALDYLDIKPINERLREIKGC 591
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQ------MQEIQQSFSILTQCDNRSKED-IPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 592 KMMIDVIKTQFPQLKKVIQFVCGNglvcetveearhiaFGGPERRKAVALDGTLFlksgvisggssdlkhkALCWDEKEL 671
Cdd:TIGR00618 613 EQHALLRKLQPEQDLQDVRLHLQQ--------------CSQELALKLTALHALQL----------------TLTQERVRE 662
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 672 HNLRDKrsqlVQELKELMKTLRKETDLKQIQTLVQGTNTRLKYSQNELEMIkKKHLATFYREQSQLQSELLNIDSQCTML 751
Cdd:TIGR00618 663 HALSIR----VLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL-ETHIEEYDREFNEIENASSSLGSDLAAR 737
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 752 SEGINKQQQKIEEFQDKIDEVEDDIFQDFCEEIGVENIREFENKHVKQQQENDQKRLEFEKQKTRLNIQ----------- 820
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAeigqeipsded 817
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17978290 821 -LEYSRNQLKKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELMVKQEQIKEvLATQSSNIEKIHIQIEEER 895
Cdd:TIGR00618 818 iLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ-LSDKLNGINQIKIQFDGDA 892
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
7-98 |
3.38e-04 |
|
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: 43.41 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 7 LLVENFKSWRGRQVI----GPFKRFTCIIGPNGSGKSNVMDALSFVM-GEKTTNLRVKNIQELIHGAHTgkpvssSASVT 81
Cdd:cd03279 6 LELKNFGPFREEQVIdftgLDNNGLFLICGPTGAGKSTILDAITYALyGKTPRYGRQENLRSVFAPGED------TAEVS 79
|
90 100
....*....|....*....|....*..
gi 17978290 82 -------IIY-IEDSG--EEKTFTRII 98
Cdd:cd03279 80 ftfqlggKKYrVERSRglDYDQFTRIV 106
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
3-99 |
4.47e-04 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 43.99 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 3 HLELLLVENFKSWRgRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVmgEKTTNLRVKNIQELI-----HGAHTGKPVSSS 77
Cdd:PRK00064 2 YLTRLSLTDFRNYE-ELDLELSPGVNVLVGENGQGKTNLLEAIYLL--APGRSHRTARDKELIrfgaeAAVIHGRVEKGG 78
|
90 100
....*....|....*....|...
gi 17978290 78 ASVTI-IYIEDSGEEKtfTRIIR 99
Cdd:PRK00064 79 RELPLgLEIDKKGGRK--VRING 99
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
4-49 |
4.48e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 4.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 17978290 4 LELLLVENFKSWRGRQVIGPFKRFTCIIGPNGSGKSNVMDALSFVM 49
Cdd:pfam13555 1 LTRLQLINWGTFDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLL 46
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
30-91 |
4.71e-04 |
|
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: 42.59 E-value: 4.71e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17978290 30 IIGPNGSGKSNVMDALSFVMGEK--TTNlRVKNIQELIhgaHTGKpvsSSASVTiIYIEDSGEE 91
Cdd:cd03276 26 IVGNNGSGKSAILTALTIGLGGKasDTN-RGSSLKDLI---KDGE---SSAKIT-VTLKNQGLD 81
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
662-1014 |
4.89e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 662 KALCWDEKELHNLRDKRSQLVQELKELMKTLRKETDLKQIQtlVQGTNTRLKYSQNELEMIKKKhlatfyREQSQLQSel 741
Cdd:pfam05483 418 EKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQ--LTAIKTSEEHYLKEVEDLKTE------LEKEKLKN-- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 742 LNIDSQCTMLSEGINKQQQKIEEFQDKIDEVEDDIFQDF-CEEIGVENIREFENKHVKQQQENDQKRLEFEKQKTRLNIQ 820
Cdd:pfam05483 488 IELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKkQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 821 LEYSRNQLKKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELMVKQEQIKEVLATQSSNIEKIHIQIEEERKKVLA 900
Cdd:pfam05483 568 LDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 901 VDREVGKL----QKEVVIIQGSLEQKL--LEKHNLLLDCKV---QDIDISLVLGSLEDIIEME---------LTETESTQ 962
Cdd:pfam05483 648 AKQKFEEIidnyQKEIEDKKISEEKLLeeVEKAKAIADEAVklqKEIDKRCQHKIAEMVALMEkhkhqydkiIEERDSEL 727
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 17978290 963 ATADIYEKE-----ASIQIDYSPLREDLKALQSDKEVEAHLTLLLQQVASQENTLLK 1014
Cdd:pfam05483 728 GLYKNKEQEqssakAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
668-911 |
5.49e-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: 44.24 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 668 EKELHNLRDKRSQLVQELKELMKTL-RKETDLKQIQTLVQGTNTRLKYSQNELEMIKKKHLATFYREqsqLQSELLNIDS 746
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLsEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKE---LKSELKNQEK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 747 QCTMLSEGINKQQQKIEEFQDKIDEVEDDIFQDFCEEIGVEN-IREFENKHVKQQQENDQKRLEFEKQKTRLN------- 818
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQReLEEKQNEIEKLKKENQSYKQEIKNLESQINdleskiq 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 819 ----------IQLEYSRNQLKKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELMVKQEQIKEVLATQSSNIEKIH 888
Cdd:TIGR04523 402 nqeklnqqkdEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
250 260
....*....|....*....|...
gi 17978290 889 IQIEEERKKVLAVDREVGKLQKE 911
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEE 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
146-509 |
6.02e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 146 KKPKERTQFFEEISTSGEFIGEYEAKKK--KLQKAEEDAQFHFNVKKNVAAERKHAKiEKEEAEHYQNLLEELKINKIQL 223
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKKAEEAK 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 224 MLFQLYYNEEKinvlnTELEQMDGNLSVVK-DTLSHHENIFKAKKKdygmltRQLQQTAKELKSVEAILnqKRPQYIKAK 302
Cdd:PTZ00121 1523 KADEAKKAEEA-----KKADEAKKAEEKKKaDELKKAEELKKAEEK------KKAEEAKKAEEDKNMAL--RKAEEAKKA 1589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 303 ENTSHHLKKLDLSKKLITDNEKQCSKQEDGIRALVAELADLDRAWKSFEKQMEEKILQKGRDIELENsqlDRYKLLKEQV 382
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE---EENKIKAAEE 1666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 383 RRKVGIMTQQLEKLQWEQKaEKERLAFEKRRHGDTQGNLKQIKEQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEEALKKE 462
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEE-DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 17978290 463 IENTKSRMSEVNEELSLIRNELQNAgidnhEGKRQQKRAEVLEHLKR 509
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKA-----EEIRKEKEAVIEEELDE 1787
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
669-785 |
6.49e-04 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 43.44 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 669 KELHNLRDKRSQLVQELKELMKTLRKETDlkqIQTLVQGTNTRLKY----SQNELEMIKKKhlatFYREQSQLQSELLNi 744
Cdd:smart00533 148 PELDELREKLEELEEELEELLKKEREELG---IDSLKLGYNKVHGYyievTKSEAKKVPKD----FIRRSSLKNTERFT- 219
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 17978290 745 dsqctmlSEGINKQQQKIEEFQDKIDEVEDDIFQDFCEEIG 785
Cdd:smart00533 220 -------TPELKELENELLEAKEEIERLEKEILRELLEKVL 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
416-511 |
7.22e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 416 DTQGNLKQIKEQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEEALKKEIENTKSRMSEVNEELSLIRNELQNAgidnhEGK 495
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL-----RAE 98
|
90
....*....|....*.
gi 17978290 496 RQQKRAEVLEHLKRLY 511
Cdd:COG4942 99 LEAQKEELAELLRALY 114
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
668-911 |
7.27e-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: 43.86 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 668 EKELHNLRDKRSQLVQELKELMKTLR-KETDLKQIQTLVQGTNTRLKYSQNELEMIKkkhlatfyREQSQLQSELLNIDS 746
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSvKELIIKNLDNTRESLETQLKVLSRSINKIK--------QNLEQKQKELKSKEK 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 747 QCTMLSEGINKQQQKIEEFQDKIDEVEddifqdfceeigvENIREFENKHVKQQQENDQKRLEFEKQKTRLNiqleysRN 826
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLK-------------EKIEKLESEKKEKESKISDLEDELNKDDFELK------KE 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 827 QLKKKLNNIDTlktTIQKGKEDIDNLKKteeeclkiveelmvKQEQIKEVLATQSSNIEKIHIQIEEERKKVLAVDREVG 906
Cdd:TIGR04523 558 NLEKEIDEKNK---EIEELKQTQKSLKK--------------KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
....*
gi 17978290 907 KLQKE 911
Cdd:TIGR04523 621 KAKKE 625
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
3-65 |
1.20e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.29 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17978290 3 HLELLLVENFKSWRGRQV-IGPFKRFTCIIGPNGSGKSNVMDALSFVMGEKTTNLRVKNIQELI 65
Cdd:COG3950 2 RIKSLTIENFRGFEDLEIdFDNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
661-895 |
1.24e-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: 43.29 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 661 HKALCWDEKELHNLRDKRSQLVQELKELMKTLRKE--TDLKQIQTLVQGTNTRLKYS-------QNELEMIKKKHLA--- 728
Cdd:pfam12128 257 ELRLSHLHFGYKSDETLIASRQEERQETSAELNQLlrTLDDQWKEKRDELNGELSAAdaavakdRSELEALEDQHGAfld 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 729 ----TFYREQSQL---QSEL-------------------------LNIDSQCTMLSEGINKQQQKIEEFQDKIDEVEDDI 776
Cdd:pfam12128 337 adieTAAADQEQLpswQSELenleerlkaltgkhqdvtakynrrrSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDD 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 777 FQDFCEEIgvenirefenkhvkqQQENDQKRLEFEKQKTRLNIQLEysrnQLKKKLNNI---DTLKTTIQKGKEDIDNLK 853
Cdd:pfam12128 417 LQALESEL---------------REQLEAGKLEFNEEEYRLKSRLG----ELKLRLNQAtatPELLLQLENFDERIERAR 477
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17978290 854 KTEEECLKIVEELMVKQEQIKEVLATQSSNIEKIHIQIEEER 895
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ 519
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
324-510 |
1.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 324 KQCSKQEDGIRALVAELADLDRAWKSFEKQMEEkILQKGRDIELENSQLDRYKLLkEQVRRKVGIMTQQLEKLQWEQKAE 403
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEE-LREELEKLEKLLQLLPLYQEL-EALEAELAELPERLEELEERLEEL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 404 KERLAfekrrhgdtqgNLKQIKEQIEEHKKRIEKLEEYTKtcmdclEDKKQQEEALKKEIENTKSRMSEVNEELSLIRNE 483
Cdd:COG4717 159 RELEE-----------ELEELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180
....*....|....*....|....*..
gi 17978290 484 LQNAGIDNHEGKRQQKRAEVLEHLKRL 510
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEA 248
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
782-932 |
1.67e-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: 42.80 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 782 EEIGVE--NIREFENKHVKQQQENDQKRLEFEKQKtRLNIQLEYSRNQLKKKLNNIDTLKTTIQKGKEdiDNLKKTEEEC 859
Cdd:pfam17380 368 EEIAMEisRMRELERLQMERQQKNERVRQELEAAR-KVKILEEERQRKIQQQKVEMEQIRAEQEEARQ--REVRRLEEER 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17978290 860 LKIVEElmVKQEQIKevlatQSSNIEKIHIQIEEERKKVLAVDREVGKLQKEVVIIQGSLEQKLLEKHNLLLD 932
Cdd:pfam17380 445 AREMER--VRLEEQE-----RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIE 510
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
9-49 |
1.72e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 41.88 E-value: 1.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 17978290 9 VENFKSWRGRQVigPFKRFTCIIGPNGSGKSNVMDALSFVM 49
Cdd:COG4938 6 IKNFGPFKEAEL--ELKPLTLLIGPNGSGKSTLIQALLLLL 44
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
381-507 |
2.04e-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: 41.45 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 381 QVRRKVGIMTQQLEKLQWEQKAEKERLAFEKRRHGDTQGNLKQIKEQIEEHKKRIEKLE-------------------EY 441
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnkeyealqkeiES 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17978290 442 TKTCMDCLEDK----KQQEEALKKEIENTKSRMSEVNEELSLIRNELQN--AGIDNHEGKRQQKRAEVLEHL 507
Cdd:COG1579 101 LKRRISDLEDEilelMERIEELEEELAELEAELAELEAELEEKKAELDEelAELEAELEELEAEREELAAKI 172
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
755-912 |
2.62e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 755 INKQQQKIEEFQDKIDEVEDDI--FQDFCE--EIGVENIRE-FENKHVKQQQENDQKRL-----EFEKQKTRLNIQLEYS 824
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLtdFENQTEkdQTALETLEKaLKDLLTDEGGAIARKEIkdlqkELEKLNEEYAAKLKAK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 825 RNQLKKKLNNID-------TLKTTIQKGKEDIDNLKKTEEECLKIVEELMvkqeqikEVLATQSSNIEKIHIQIEEERKK 897
Cdd:cd22656 203 IDELKALIADDEaklaaalRLIADLTAADTDLDNLLALIGPAIPALEKLQ-------GAWQAIATDLDSLKDLLEDDISK 275
|
170
....*....|....*
gi 17978290 898 VLAVDREVGKLQKEV 912
Cdd:cd22656 276 IPAAILAKLELEKAI 290
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
715-911 |
2.94e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 715 SQNELEMIKKkhlatfyrEQSQLQSELLNIDSQCTMLSEGINKQQQKIEEFQDKIDEVEDDIfQDFCEEIGV--ENIREF 792
Cdd:COG4942 25 AEAELEQLQQ--------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL-AALEAELAEleKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 793 ENKHVKQQQE---------------------NDQKRLEFEKQKTRLNIQLEYSRNQ---LKKKLNNIDTLKTTIQKGKED 848
Cdd:COG4942 96 RAELEAQKEElaellralyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQaeeLRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17978290 849 IDNLKKTEEECLKIVEELMVKQEQikeVLATQSSNIEKIHIQIEEERKKVLAVDREVGKLQKE 911
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
273-487 |
3.06e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 273 LTRQLQQTAKELKSVEAILNQkrpqyIKAKENTSHHLKKLDLSKKLITDNEKQcskqedgIRALVAELADLDRAWKSFEK 352
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQ-------LAEARAELAEAEARLAALRA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 353 QmeekiLQKGRDIELENSQLDRYKLLKEQVrrkvgimtQQLEKlqweqkaekeRLAFEKRRHGDTQGNLKQIKEQIEEHK 432
Cdd:COG3206 248 Q-----LGSGPDALPELLQSPVIQQLRAQL--------AELEA----------ELAELSARYTPNHPDVIALRAQIAALR 304
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17978290 433 KRIEKLEEYTKTCMDC-LEDKKQQEEALKKEIENTKSRMSEVNE---ELSLIRNELQNA 487
Cdd:COG3206 305 AQLQQEAQRILASLEAeLEALQAREASLQAQLAQLEARLAELPEleaELRRLEREVEVA 363
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
146-502 |
3.25e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 146 KKPKERTQFFEEISTSGEFIGEYEAKKKK---LQKAEEDAQFHFNVKKNVAAERK--HAKIEKEEAEHYQNLLEELKINK 220
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKadeAKKKAEEKKKADEAKKKAEEAKKadEAKKKAEEAKKAEEAKKKAEEAK 1470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 221 IQLMLFQLYYNEEKINVLNTELEQMDGNLSVVKDTLSHHENIFKAKKKDYGMLTRQLQQTAKELKSVEAilnQKRPQYIK 300
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA---KKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 301 AKENTSHHLKKLDLSKKLITDNEKQCSKQEDGIR-ALVAELADLDRAWKSFEKQMEEKILQKGRDIELENSQLDRYKLLK 379
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 380 EQVRRKvgiMTQQLEKLQWEQKAEKERLafeKRRHGDTQGNLKQIKEQIEEHKKRIEKLEEYTktcmdclEDKKQQEEAL 459
Cdd:PTZ00121 1628 AEEEKK---KVEQLKKKEAEEKKKAEEL---KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE-------EDEKKAAEAL 1694
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 17978290 460 KKEIENTK--SRMSEVNEELSLIRNELQNAGIDNHEGKRQQKRAE 502
Cdd:PTZ00121 1695 KKEAEEAKkaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
231-497 |
3.47e-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: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 231 NEEKINVLNTELEQMDGNLSVVKDTLSHHENIFKAKKKDYGMLTRQLQQTAKELKSVEAILNQKRPQY---IKAKENTSH 307
Cdd:TIGR04523 94 NKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYndlKKQKEELEN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 308 HLKKLDLSKKLITDNEKQCSKQEDGIRALVAELADLDRAWKSFEKQMEEKILQKG---RDIELENSQLDRYKLLKEQVRR 384
Cdd:TIGR04523 174 ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNqlkDNIEKKQQEINEKTTEISNTQT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 385 KVGIMTQQLEKLQWEQKAEKERLAFEKRRHGDTQGNLKQIKEQIEEHKKriEKLEEYTKTCMDCLEDKKQQEEALKKEIE 464
Cdd:TIGR04523 254 QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQIS 331
|
250 260 270
....*....|....*....|....*....|...
gi 17978290 465 NTKSRMSEVNEELSLIRNELQNAGIDNHEGKRQ 497
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
353-502 |
3.60e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.65 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 353 QMEEKilQKGRDIELENSQLDRYKLLKEQVRRKVGIMTQQLEKLQWEQKAEKERLAfeKRRHGDTQGNLKQIKEQIEEHK 432
Cdd:pfam17380 384 QMERQ--QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV--RRLEEERAREMERVRLEEQERQ 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 433 KRIEKL----EEYTKTCMDCLEDKKQQEEA-------LKKEIENTKSRMSEVNEELSLIRNELQNAGIDNHEGKRQQKRA 501
Cdd:pfam17380 460 QQVERLrqqeEERKRKKLELEKEKRDRKRAeeqrrkiLEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAE 539
|
.
gi 17978290 502 E 502
Cdd:pfam17380 540 E 540
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1119-1204 |
4.00e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 1119 PMDNLSGGEKCVAALALLFAVHSFRPapFFVLDEVDAALDNTNIGKVSSYIKEQSQEQFQMIIISLKEEFYSKADALIGV 1198
Cdd:cd03238 84 KLSTLSGGELQRVKLASELFSEPPGT--LFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
....*.
gi 17978290 1199 YPEHNE 1204
Cdd:cd03238 162 GPGSGK 167
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
677-897 |
4.33e-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: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 677 KRSQLVQELKELMKTLR-KETDLKQIQTLVQGTNTRLKYSQNELEMIK------KKHLATFYREQSQLQSELLNIDSQCT 749
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKnKEKELKNLDKNLNKDEEKINNSNNKIKILEqqikdlNDKLKKNKDKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 750 MLSEGINKQQQKIEEFQDKIDEVEDDIFQDFCEEIGVENIREFEN------KHVKQQQENDQKRLEFEKQKTRLNIQLey 823
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkyndlKKQKEELENELNLLEKEKLNIQKNIDK-- 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17978290 824 SRNQLKKKLNNIDTLKTTIQKGKE---DIDNLKKTEEECLKIVEELMVKQEQIKEVLATQSSNIEKIHIQIEEERKK 897
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKKIQKNKSlesQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
662-1083 |
4.56e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 662 KALCWDEKELHNLRDKRSQLVQELKELMKTL-RKETDLKQIQTLVQGTNT----------RLKYSQNELEMIKKKHLAtf 730
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLsRLEEEINGIEERIKELEEkeerleelkkKLKELEKRLEELEERHEL-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 731 YREQSQLQSELLNIDSQCTMLSegINKQQQKIEEFQDKIDEVEDDIFQDFCEEIGVENIREFENKHVKQQQENDQK---- 806
Cdd:PRK03918 364 YEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvc 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 807 RLEFEKQKtRLNIQLEYSR--NQLKKKLNNIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELmvkqEQIKEVLA-TQSSN 883
Cdd:PRK03918 442 GRELTEEH-RKELLEEYTAelKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELA----EQLKELEEkLKKYN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 884 IEKIHIQIEEERKkvlaVDREVGKLQKEVVIIQGSLEQ-KLLEKHNLLLDCKVQDIDISlvLGSLEDIIEMELTEtestq 962
Cdd:PRK03918 517 LEELEKKAEEYEK----LKEKLIKLKGEIKSLKKELEKlEELKKKLAELEKKLDELEEE--LAELLKELEELGFE----- 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 963 ataDIYEKEASIQIDYSPLREDLKALQSDKEVEAhltlLLQQVASQENTLLKTTAPNLRAQENLKTVRDKFQESADVFea 1042
Cdd:PRK03918 586 ---SVEELEERLKELEPFYNEYLELKDAEKELER----EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY-- 656
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 17978290 1043 SRKEARICRQEFEQvKRRRYDAFSQCFEHISVSIDQIYKKL 1083
Cdd:PRK03918 657 SEEEYEELREEYLE-LSRELAGLRAELEELEKRREEIKKTL 696
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
111-478 |
4.71e-03 |
|
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: 41.57 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 111 PVSRSVYVAQLENIGIIVKAQNCLVF----QGTVESISMKKPKERTQFFEEISTSGEFIGEYEAK----KKKLQKAEEDA 182
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEipelRNKLQKVNRDI 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 183 QfhfNVKKNVAAERKHAKIEKEEAEHYQNLLEELKInkIQLMLFQLYYNEEKINVLNTELEQMDGNLSVVKDTLSHHEni 262
Cdd:TIGR00606 761 Q---RLKNDIEEQETLLGTIMPEEESAKVCLTDVTI--MERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQE-- 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 263 fkaKKKDYGMLTRQLQQTAKELKSveailNQKRPQYIKAKENtshhlkKLDLSKKLITDNEKQCSKQEDGIRALVAELAD 342
Cdd:TIGR00606 834 ---KQHELDTVVSKIELNRKLIQD-----QQEQIQHLKSKTN------ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 343 LDRAWKSFEKQMEEKILQKGRDIELENSQLDRYKLLKEQVRRKVGIMTQQLEKLQWEQKAEKERLAFEKRRH-GDTQGNL 421
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYlKQKETEL 979
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 17978290 422 KQIKEQIEEHKKRIEKLEEYTKTCMDCLEDKKQQEEALKKEIENTKSR--MSEVNEELS 478
Cdd:TIGR00606 980 NTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKREneLKEVEEELK 1038
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
1124-1161 |
7.12e-03 |
|
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: 39.50 E-value: 7.12e-03
10 20 30
....*....|....*....|....*....|....*...
gi 17978290 1124 SGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTN 1161
Cdd:cd03277 128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTN 165
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
702-886 |
7.19e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 702 QTLVQGTNTRLKYSQNELEMIKKKhLATFYREQSQLQSELLNIDSQCTMLSEGINKQQQKIEEFQDKIDEVEDDI----- 776
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAE-LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 777 --------------------FQDFCEEIG-VENIREFENKHVKQQQEnDQKRLEFEKQKTRLNIQ-LEYSRNQLKKKLNN 834
Cdd:COG3883 94 alyrsggsvsyldvllgsesFSDFLDRLSaLSKIADADADLLEELKA-DKAELEAKKAELEAKLAeLEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17978290 835 IDTLKTTIQKGKEDIDNLKKTEEECL-KIVEELMVKQEQIKEVLATQSSNIEK 886
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLaELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
25-132 |
9.43e-03 |
|
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: 39.49 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 25 KRFTCIIGPNGSGKSNVMDALSFVMGEK--TTNLRVKNIQELIHGAHTGKPVSSSASVTIIYIEDSGEEKTFTRII-RGG 101
Cdd:cd03241 21 EGLTVLTGETGAGKSILLDALSLLLGGRasADLIRSGAEKAVVEGVFDISDEEEAKALLLELGIEDDDDLIIRREIsRKG 100
|
90 100 110
....*....|....*....|....*....|.
gi 17978290 102 CSEYHFGDKPVSRSVyVAQLENIGIIVKAQN 132
Cdd:cd03241 101 RSRYFINGQSVTLKL-LRELGSLLVDIHGQH 130
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
744-947 |
9.74e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 744 IDSQCTMLSEGINKQQQKIEEFQDKIDEVEddifqdfceEIGVENIREFENK---HVKQQQENDQKRLEFEKQKTRLNIQ 820
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQR---------KKNGENIARKQNKydeLVEEAKTIKAEIEELTDELLNLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 821 LEYSRNQLKKkLN-------------------------------NIDTLKTTIQKGKEDIDNLKKTEEECLKIVEELMVK 869
Cdd:PHA02562 250 IEDPSAALNK-LNtaaakikskieqfqkvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978290 870 ----QEQIKEVLATQSSnIEKIHIQIEEERKKVLAVDREVGKLQKEVVIIQGSLEQKLLEKHNLLLDC--KVQDIDISLV 943
Cdd:PHA02562 329 mdefNEQSKKLLELKNK-ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKseLVKEKYHRGI 407
|
....
gi 17978290 944 LGSL 947
Cdd:PHA02562 408 VTDL 411
|
|
| |
