|
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 ... |
89-1287 |
7.75e-145 |
|
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: 472.15 E-value: 7.75e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYAGEVElGPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANR-IRCKRVSTLIHSSSSyPNLRSCSVAV 167
Cdd:pfam02463 2 LKRIEIEGFKSYAKTVI-LPFSPGFTAIVGPNGSGKSNILDAILFVLGERSAKsLRSERLSDLIHSKSG-AFVNSAEVEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 168 HFkqivDKGDGTcEDVPDSSIVIERTAMSDNSSYYQINDKRAQLKDVAKLLKKHHVDLEHNRFLILQGEVESIAMMKPKG 247
Cdd:pfam02463 80 TF----DNEDHE-LPIDKEEVSIRRRVYRGGDSEYYINGKNVTKKEVAELLESQGISPEAYNFLVQGGKIEIIAMMKPER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 248 QTENETGMLEYLEDIVGTQRYIRPLQQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENELVRTKSFH 327
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 328 IQKII-------SIKKSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVES 400
Cdd:pfam02463 235 NEERIdllqellRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 401 AYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLT 480
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 481 EKRLKLSdelvglkEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEI 560
Cdd:pfam02463 395 EELELKS-------EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 561 ASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQRSNNKVLDFLMRMKMEGKIPGILGRLGDLGGIDAKYDIAIST 640
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 641 ACGRLDNIVTDNYETASAAIGALKEYNVGRATFITLDKiehHRREANSRINTPENVPRLYdlvkveddrvrtaFYFALRN 720
Cdd:pfam02463 548 AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIP---KLKLPLKSIAVLEIDPILN-------------LAQLDKA 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 721 TLVCDDLEQGTRIAYGRERYRVVTLRGemieMTGTMSGGGSRPIRGKMGTQVRTKTAESADSSQISQKALEDMQIQAEEL 800
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLK----ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 801 QARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKTTDERAVKEREEQIEAA 880
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 881 KQELEQAQFAEQAVSSQIEEIQNQYDTLRNESVKPVEAKIKKVNSQIEKLAANVRSLNVGLAtadRNITKITGNNNNLRE 960
Cdd:pfam02463 768 ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK---IKEEELEELALELKE 844
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 961 NIKAAEEKLKSLNEDRNKAKEKKEELEKEIEESeasiegaKSQSSDIKKEIDEITKEENKRNIERIEIDTKLQAAAGKMN 1040
Cdd:pfam02463 845 EQKLEKLAEEELERLEEEITKEELLQELLLKEE-------ELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1041 KVKNDIpgwqaQLAPLKLNEIPGETEPQAPLKELNEEELEAETLEALQYKQTMLEEDLKTKKPNLSCIKEFNEKRLVYLD 1120
Cdd:pfam02463 918 EIEERI-----KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1121 RVRVLEDITSKRNEMRDKYEEVRKRRYKEFMDGFSIITRKLKEMYQMITLGGDAELELVDSMDPFTEGVNFTVRPPKKSW 1200
Cdd:pfam02463 993 DELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISARPPGKGV 1072
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1201 KYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIVSLRVNMFELANFLVGI 1280
Cdd:pfam02463 1073 KNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGV 1152
|
....*..
gi 24584683 1281 YKVSDCT 1287
Cdd:pfam02463 1153 TMVENGV 1159
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
89-1280 |
8.05e-119 |
|
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: 400.98 E-value: 8.05e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYAGEVELgPFHQSFTAIIGPNGSGKSNVIDSMMFVFG-CRANRIRCKRVSTLIHSSSSYPNLRSCSVAV 167
Cdd:TIGR02169 2 IERIELENFKSFGKKKVI-PFSKGFTVISGPNGSGKSNIGDAILFALGlSSSKAMRAERLSDLISNGKNGQSGNEAYVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 168 HFKQIVDKGDGTCEdvpdssIVIERTAMSDNS-SYYQINDKRAQLKDVAKLLKKHHVDLEHNRFlILQGEVESIAMMKPK 246
Cdd:TIGR02169 81 TFKNDDGKFPDELE------VVRRLKVTDDGKySYYYLNGQRVRLSEIHDFLAAAGIYPEGYNV-VLQGDVTDFISMSPV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 247 GQTEnetgmleYLEDIVGTQRYIRPLQQ---------------------INQRVDQLTDDRtEKHNRCKLAEREMKDLEQ 305
Cdd:TIGR02169 154 ERRK-------IIDEIAGVAEFDRKKEKaleeleeveenierldliideKRQQLERLRRER-EKAERYQALLKEKREYEG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 306 pfneaVDYLKKENELVRTKSfHIQKIISIKKSKLEQYTQEHEACAEELkthdegtAALKQSRAEKETIIRKEIEEYEALV 385
Cdd:TIGR02169 226 -----YELLKEKEALERQKE-AIERQLASLEEELEKLTEEISELEKRL-------EEIEQLLEELNKKIKDLGEEEQLRV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 386 KKR-EQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLhklpeknQREIEDCNKKLESLEVSKVTLNEE 464
Cdd:TIGR02169 293 KEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL-------EREIEEERKRRDKLTEEYAELKEE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 465 LEKQQAELTKTTAPLTEKRLKLSD---ELVGLKEKVNTAKGE--------VQVFESQLKILKQAETTESRKYEtLKSSYE 533
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDyreKLEKLKREINELKREldrlqeelQRLSEELADLNAAIAGIEAKINE-LEEEKE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 534 QSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEineRSSVMQAQRSNNKVldflmRMKM 613
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ---ARASEERVRGGRAV-----EEVL 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 614 EGKIPGILGRLGDLGGIDAKYDIAISTACG-RLDNIVTDNYETASAAIGALKEYNVGRATFITLDKIEHHRREAnSRINT 692
Cdd:TIGR02169 517 KASIQGVHGTVAQLGSVGERYATAIEVAAGnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDL-SILSE 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 693 PENVPRLYDLVKVeDDRVRTAFYFALRNTLVCDDLEQGTRIAygrERYRVVTLRGEMIEMTGTMSGGgSRPIRGKMGTQV 772
Cdd:TIGR02169 596 DGVIGFAVDLVEF-DPKYEPAFKYVFGDTLVVEDIEAARRLM---GKYRMVTLEGELFEKSGAMTGG-SRAPRGGILFSR 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 773 RTKtaesadssqisqKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQmASNLKQ 852
Cdd:TIGR02169 671 SEP------------AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE-EEKLKE 737
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 853 CEAQRQRMLKKTTDERAVKERE-EQIEAAKQELEQAQFAEQavssqiEEIQNQYDTLRNESVKPVEAKIKKVNSQIEKLA 931
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSElKELEARIEELEEDLHKLE------EALNDLEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 932 ANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSLNEDRNKAKEKKEELEKEIEESEASIEGAKSQSSDIKKEI 1011
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1012 DEITKEENKRNIERIEIDTKLQAAAGKMNKVKNDIPGWQAQLAPLKLNEIPGETEPQAplkelneeeleAETLEALQYKQ 1091
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-----------ELSLEDVQAEL 960
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1092 TMLEEDLKTKKP-NLSCIKEFNEKRLVYLDRVRVLEDITSKRNEMRDKYEEVRKRRYKEFMDGFSIITRKLKEMYQMITl 1170
Cdd:TIGR02169 961 QRVEEEIRALEPvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAINENFNEIFAELS- 1039
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1171 GGDAELELVDSMDPFTEGVNFTVRPPKKSWKYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGH 1250
Cdd:TIGR02169 1040 GGTGELILENPDDPFAGGLELSAKPKGKPVQRLEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAK 1119
|
1210 1220 1230
....*....|....*....|....*....|
gi 24584683 1251 YIKERTKNAQFIIVSLRVNMFELANFLVGI 1280
Cdd:TIGR02169 1120 LIREKAGEAQFIVVSLRSPMIEYADRAIGV 1149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
89-1280 |
1.76e-106 |
|
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: 366.30 E-value: 1.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYAGEVELgPFHQSFTAIIGPNGSGKSNVIDSMMFVFG-CRANRIRCKRVSTLIHS-SSSYPNLRSCSVA 166
Cdd:TIGR02168 2 LKKLELAGFKSFADPTTI-NFDKGITGIVGPNGCGKSNIVDAIRWVLGeQSAKALRGGKMEDVIFNgSETRKPLSLAEVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 167 VHFkqivDKGDGTCEDVPDSSIVIERTAMSDNSSYYQINDKRAQLKDVakllkkhhvdleHNRFL-----------ILQG 235
Cdd:TIGR02168 81 LVF----DNSDGLLPGADYSEISITRRLYRDGESEYFINGQPCRLKDI------------QDLFLdtglgkrsysiIEQG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 236 EVESIAMMKPKGqtenetgMLEYLEDIVGTQRY-------IRPLQQINQRVDQLTDDRTEkhnrcklAEREMKDLEQPFN 308
Cdd:TIGR02168 145 KISEIIEAKPEE-------RRAIFEEAAGISKYkerrketERKLERTRENLDRLEDILNE-------LERQLKSLERQAE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 309 EAVDYLKKENELvrtksFHIQKIISI-----KKSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIIRKEIEEYEA 383
Cdd:TIGR02168 211 KAERYKELKAEL-----RELELALLVlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 384 LVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEvskvTLNE 463
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE----AELE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 464 ELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKqaettesRKYETLKSSYEQSQKSLEEKv 543
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE-------DRRERLQQEIEELLKKLEEA- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 544 tRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQRSNNKVLDFLMR------------M 611
Cdd:TIGR02168 434 -ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEnlegfsegvkalL 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 612 KMEGKIPGILGRLGDLGGIDAKYDIAISTACG-RLDNIVTDNYETASAAIGALKEYNVGRATFITLDKIEHHR---REAN 687
Cdd:TIGR02168 513 KNQSGLSGILGVLSELISVDEGYEAAIEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEiqgNDRE 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 688 SRINTPENVPRLYDLVKVeDDRVRTAFYFALRNTLVCDDLEQGTRIA-YGRERYRVVTLRGEMIEMTGTMSGGGSRPIRG 766
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKF-DPKLRKALSYLLGGVLVVDDLDNALELAkKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSS 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 767 KMGTQ-----VRTKTAESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITS 841
Cdd:TIGR02168 672 ILERRreieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 842 LEQQMASNLKQCEAQRQRMLKKTTderAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLrNESVKPVEAKIK 921
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEE---ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-NEEAANLRERLE 827
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 922 KVNSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSLNEDRNKAKEkkeelekeieeseasiegak 1001
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE-------------------- 887
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1002 sQSSDIKKEIDEITKEENKRNIERIEIDTKLQAAAGKMNKVKNDIPGWQAQLAPL--KLNEIpGETEPQAPLKELNEEEL 1079
Cdd:TIGR02168 888 -ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqeRLSEE-YSLTLEEAEALENKIED 965
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1080 EAETLealQYKQTMLEEDLKTKKP-NLSCIKEFNE--KRLVYLDRVRvlEDITSKRNEMRDKYEEVRKRRYKEFMDGFSI 1156
Cdd:TIGR02168 966 DEEEA---RRRLKRLENKIKELGPvNLAAIEEYEElkERYDFLTAQK--EDLTEAKETLEEAIEEIDREARERFKDTFDQ 1040
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1157 ITRKLKEMYQMITLGGDAELELVDSMDPFTEGVNFTVRPPKKSWKYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEI 1236
Cdd:TIGR02168 1041 VNENFQRVFPKLFGGGEAELRLTDPEDLLEAGIEIFAQPPGKKNQNLSLLSGGEKALTALALLFAIFKVKPAPFCILDEV 1120
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....
gi 24584683 1237 DAALDFKNVSIVGHYIKERTKNAQFIIVSLRVNMFELANFLVGI 1280
Cdd:TIGR02168 1121 DAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLYGV 1164
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
89-1280 |
4.88e-71 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 258.71 E-value: 4.88e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYAGEVELgPFHQSFTAIIGPNGSGKSNVIDSMMFVFG-CRANRIRCKRVSTLIHS-SSSYPNLRSCSVA 166
Cdd:COG1196 3 LKRLELAGFKSFADPTTI-PFEPGITAIVGPNGSGKSNIVDAIRWVLGeQSAKSLRGGKMEDVIFAgSSSRKPLGRAEVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 167 VHFkqivDKGDGTcEDVPDSSIVIERTAMSDNSSYYQINDKRAQLKDVAKLLKKHHVDLE-HNrfLILQGEVESIAMMKP 245
Cdd:COG1196 82 LTF----DNSDGT-LPIDYDEVTITRRLYRSGESEYYINGKPCRLKDIQDLFLDTGLGPEsYS--IIGQGMIDRIIEAKP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 246 KgqtEnetgMLEYLEDIVGTQRY-------IRPLQQINQRVDQLTDDRTEKHNRCKLAEREMKDleqpfneAVDYLKKEN 318
Cdd:COG1196 155 E---E----RRAIIEEAAGISKYkerkeeaERKLEATEENLERLEDILGELERQLEPLERQAEK-------AERYRELKE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 319 ELVRTKSFHIQKIISIKKSKLEQYTQEHEACAEELkthdegtAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTV 398
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 399 ESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKttap 478
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 479 LTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKT 558
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 559 EIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQRSNNKVLDFLM-----------RMKMEGKIPGILGRLGDL 627
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadyegflegvkAALLLAGLRGLAGAVAVL 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 628 GGIDAKYDIAISTACG-RLDNIVTDNYETASAAIGALKEYNVGRATFITLDKIEhhRREANSRINTPENVPRLYDLVkVE 706
Cdd:COG1196 530 IGVEAAYEAALEAALAaALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR--ARAALAAALARGAIGAAVDLV-AS 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 707 DDRVRTAFYFALRNTLVCDDLEQGTRiayGRERYRVVTLRGEMIEMTGTMSGGGSRPirgkmgtqvrtktaesadsSQIS 786
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARL---EAALRRAVTLAGRLREVTLEGEGGSAGG-------------------SLTG 664
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 787 QKALEDMQIQAEELQARvnycQEQQGSLEREIQTLKNGLQRDEAEYKRlavsitsleqqmasnlkqceaQRQRMLKKTTD 866
Cdd:COG1196 665 GSRRELLAALLEAEAEL----EELAERLAEEELELEEALLAEEEEERE---------------------LAEAEEERLEE 719
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 867 ERAVKEREEQIEAAKQELEQAQFAEQavssQIEEIQNQYDTLRNESVKPVEAKIKKVNSQIEKLAAnVrslnvglatadr 946
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEE----ELLEEEALEELPEPPDLEELERELERLEREIEALGP-V------------ 782
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 947 nitkitgnnnNLrenikAAEEKLKSLNEDRNKAkekkeelekeieeseasiegaKSQSSDIKKEIDEItkeenkrnieri 1026
Cdd:COG1196 783 ----------NL-----LAIEEYEELEERYDFL---------------------SEQREDLEEARETL------------ 814
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1027 eidtkLQAaagkmnkvkndipgwqaqlaplklneipgetepqaplkelneeeleaetlealqykqtmleedlktkkpnls 1106
Cdd:COG1196 815 -----EEA------------------------------------------------------------------------ 817
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1107 cIKEFNekrlvyldrvrvleditskrnemrdkyEEVRKRrykeFMDGFSIITRKLKEMYQMITLGGDAELELVDSMDPFT 1186
Cdd:COG1196 818 -IEEID---------------------------RETRER----FLETFDAVNENFQELFPRLFGGGEAELLLTDPDDPLE 865
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1187 EGVNFTVRPPKKSWKYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIVSL 1266
Cdd:COG1196 866 TGIEIMAQPPGKKLQRLSLLSGGEKALTALALLFAIFRLNPSPFCVLDEVDAPLDDANVERFAELLKEMSEDTQFIVITH 945
|
1210
....*....|....
gi 24584683 1267 RVNMFELANFLVGI 1280
Cdd:COG1196 946 NKRTMEAADRLYGV 959
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
1196-1290 |
3.01e-67 |
|
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: 225.64 E-value: 3.01e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1196 PKKSWKYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIVSLRVNMFELAN 1275
Cdd:cd03274 118 PKKSWKNISNLSGGEKTLSSLALVFALHHYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAD 197
|
90
....*....|....*
gi 24584683 1276 FLVGIYKVSDCTDSI 1290
Cdd:cd03274 198 RLVGIYKTNNCTKSV 212
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
87-246 |
2.46e-66 |
|
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: 223.33 E-value: 2.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 87 LIISKIVNRNFKSYAGEVELGPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRCKRVSTLIHSSSSYPNLRSCSVA 166
Cdd:cd03274 1 LIITKLVLENFKSYAGEQVIGPFHKSFSAIVGPNGSGKSNVIDSMLFVFGFRASKMRQKKLSDLIHNSAGHPNLDSCSVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 167 VHFKQIVDKGdgtcedvpdssiviertamsdnssyyqindkraqlkdvakLLKKHHVDLEHNRFLILQGEVESIAMMkPK 246
Cdd:cd03274 81 VHFQEIIDKP----------------------------------------LLKSKGIDLDHNRFLILQGEVEQIAQM-PK 119
|
|
| SMC_hinge |
smart00968 |
SMC proteins Flexible Hinge Domain; This entry represents the hinge region of the SMC ... |
618-733 |
1.74e-36 |
|
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: 133.90 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 618 PGILGRLGDLGGIDAKYDIAISTACG-RLDNIVTDNYETASAAIGALKEYNVGRATFITLDKIEHHRREANSR----INT 692
Cdd:smart00968 1 PGVLGRVADLISVDPKYETALEAALGgRLQAVVVDTEETAKKAIEFLKKNRLGRATFLPLDKIKPRSPAGSKLrealLPE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 24584683 693 PENVPRLYDLVKVeDDRVRTAFYFALRNTLVCDDLEQGTRI 733
Cdd:smart00968 81 PGFVGPAIDLVEY-DPELRPALEYLLGNTLVVDDLETARRL 120
|
|
| SMC_hinge |
pfam06470 |
SMC proteins Flexible Hinge Domain; This family represents the hinge region of the SMC ... |
617-734 |
2.46e-32 |
|
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: 121.98 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 617 IPGILGRLGDLGGIDAKYDIAISTACG-RLDNIVTDNYETASAAIGALKEYNVGRATFITLDKIehHRREANSRINTPEN 695
Cdd:pfam06470 1 LKGVLGRLADLIEVDEGYEKAVEAALGgRLQAVVVDDEDDAKRAIEFLKKNKLGRATFLPLDRL--KPRPRRPGADLKGG 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 24584683 696 VPRLYDLVKVeDDRVRTAFYFALRNTLVCDDLEQGTRIA 734
Cdd:pfam06470 79 AGPLLDLVEY-DDEYRKALRYLLGNTLVVDDLDEALELA 116
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
96-247 |
5.70e-32 |
|
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: 125.76 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 96 NFKSYAGEVELGPFHqSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRCKRVSTLIHSSS-SYPNLRSCSVAVHFKqivd 174
Cdd:cd03275 8 NFKSYKGRHVIGPFD-RFTCIIGPNGSGKSNLMDAISFVLGEKSSHLRSKNLKDLIYRARvGKPDSNSAYVTAVYE---- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584683 175 kgdGTCEDVPDSSIVIertamSDNSSYYQINDKRAQLKDVAKLLKKHHVDLEHNRFLILQGEVESIAMMKPKG 247
Cdd:cd03275 83 ---DDDGEEKTFRRII-----TGGSSSYRINGKVVSLKEYNEELEKINILVKARNFLVFQGDVESIASKNPPG 147
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
1195-1292 |
2.86e-29 |
|
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: 118.06 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1195 PPKKSWKYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKE-RTKNAQFIIVSLRVNMFEL 1273
Cdd:cd03275 145 PPGKRFRDMDNLSGGEKTMAALALLFAIHSYQPAPFFVLDEVDAALDNTNVGKVASYIREqAGPNFQFIVISLKEEFFSK 224
|
90
....*....|....*....
gi 24584683 1274 ANFLVGIYKVSDCTDSITM 1292
Cdd:cd03275 225 ADALVGVYRDQECNSSKVL 243
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
1206-1284 |
8.33e-29 |
|
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: 114.33 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1206 LSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKN-AQFIIVSLRVNMFELANFLVGIYKVS 1284
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHtSQFIVITLKKEMFENADKLIGVLFVH 174
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
1196-1280 |
1.33e-27 |
|
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: 111.40 E-value: 1.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1196 PKKSWKYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIVSLRVNMFELAN 1275
Cdd:cd03278 104 PGKKVQRLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
....*
gi 24584683 1276 FLVGI 1280
Cdd:cd03278 184 RLYGV 188
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
1200-1277 |
3.11e-21 |
|
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: 94.67 E-value: 3.11e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24584683 1200 WK-YISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIVSLRVNMFELANFL 1277
Cdd:cd03273 160 WKeSLTELSGGQRSLVALSLILALLLFKPAPMYILDEVDAALDLSHTQNIGRMIKTHFKGSQFIVVSLKEGMFNNANVL 238
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1206-1285 |
4.96e-20 |
|
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: 88.57 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1206 LSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERT-KNAQFIIVSLRVNMFELANFLVGIYKVS 1284
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHIKKVI 157
|
.
gi 24584683 1285 D 1285
Cdd:cd03227 158 T 158
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
89-173 |
1.21e-19 |
|
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: 87.75 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYAGEVELGPFHqSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRCKRVSTLIHSSSSyPNLRSCSVAVH 168
Cdd:cd03239 1 IKQITLKNFKSYRDETVVGGSN-SFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLFLAGGGVK-AGINSASVEIT 78
|
....*
gi 24584683 169 FKQIV 173
Cdd:cd03239 79 FDKSY 83
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
89-169 |
4.29e-17 |
|
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: 80.97 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYAGEVELgPFHQSFTAIIGPNGSGKSNVIDSMMFVFG-CRANRIRCKRVSTLIHSSSSY-PNLRSCSVA 166
Cdd:cd03278 1 LKKLELKGFKSFADKTTI-PFPPGLTAIVGPNGSGKSNIIDAIRWVLGeQSAKSLRGEKMSDVIFAGSETrKPANFAEVT 79
|
...
gi 24584683 167 VHF 169
Cdd:cd03278 80 LTF 82
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
89-267 |
5.91e-16 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 79.26 E-value: 5.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYAGEVELGPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRA-NRIRCKRVSTLIHSSSSyPNLRSCSVAV 167
Cdd:cd03273 3 IKEIILDGFKSYATRTVISGFDPQFNAITGLNGSGKSNILDAICFVLGITNlSTVRASNLQDLIYKRGQ-AGITKASVTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 168 HFKQivdkgdgtcEDVPDSS--------IVIERTAMSDNSSYYQINDKRAQLKDVAKLLKKHHVDLEHNRFLILQGEVES 239
Cdd:cd03273 82 VFDN---------SDKSQSPigfenypeITVTRQIVLGGTNKYLINGHRAQQQRVQDLFQSVQLNVNNPHFLIMQGRITK 152
|
170 180
....*....|....*....|....*...
gi 24584683 240 IAMMkpkGQTENETgmleyLEDIVGTQR 267
Cdd:cd03273 153 VLNM---GGVWKES-----LTELSGGQR 172
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
1203-1284 |
1.28e-15 |
|
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: 78.07 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1203 ISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIVSLRVNMFELANFLVGIY- 1281
Cdd:cd03272 156 MQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQFITTTFRPELLEVADKFYGVKf 235
|
....*
gi 24584683 1282 --KVS 1284
Cdd:cd03272 236 rnKVS 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
381-975 |
9.73e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 9.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 381 YEALVKKREQIKkRLVTVESAYTEIQSTMENTNKQRK-KDKAQIEKNEKELEDLhklpeknQREIEDCNKKLESLEVSKV 459
Cdd:COG4913 241 HEALEDAREQIE-LLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELL-------EAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 460 TLNEELEKQQAELTKTTAPLTE---KRLK-LSDELVGLKEKVNTAKGEVQVFESQLKilkqaettesrkyeTLKSSYEQS 535
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGnggDRLEqLEREIERLERELEERERRRARLEALLA--------------ALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 536 QKSLEEKVTRVDELKESIPRMKTEIAsksAEVDKMVKEERNLSMQCNKLRTEINErssvMQAQRSNN--KVLDFLMRMKM 613
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALE---EALAEAEAALRDLRRELRELEAEIAS----LERRKSNIpaRLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 614 EGKIPG----ILGRLGDLGGIDAKYDIAISTACG--RLDNIVTDNYEtaSAAIGALKEYNVGRAtfITLDKIEHHRREAN 687
Cdd:COG4913 452 ALGLDEaelpFVGELIEVRPEEERWRGAIERVLGgfALTLLVPPEHY--AAALRWVNRLHLRGR--LVYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 688 SRINTPEnvpRLYDLVKVEDdrvrTAFYFALRNTLV-------CDDLEQgtriaYGRERYRVvTLrgemiemTGTMSGGG 760
Cdd:COG4913 528 RPRLDPD---SLAGKLDFKP----HPFRAWLEAELGrrfdyvcVDSPEE-----LRRHPRAI-TR-------AGQVKGNG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 761 SRpirGKMGTQVRTKTA----ESAdssqisQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQ--RDEAEYKR 834
Cdd:COG4913 588 TR---HEKDDRRRIRSRyvlgFDN------RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSW 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 835 LAVSITSLEQQMASNlkqcEAQRQRMLKKTTD----ERAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRN 910
Cdd:COG4913 659 DEIDVASAEREIAEL----EAELERLDASSDDlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584683 911 ESVKPVEAKIKKVNSQIEKLAANvrslnvglATADRNITKITgnnNNLRENIKAAEEKLKSLNED 975
Cdd:COG4913 735 RLEAAEDLARLELRALLEERFAA--------ALGDAVERELR---ENLEERIDALRARLNRAEEE 788
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-589 |
1.58e-11 |
|
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: 68.89 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 273 QQINQRVDQLTDDRTEKHNRcklaEREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKIISiKKSKLEQYTQEHEACAEE 352
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNS----ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES-QINDLESKIQNQEKLNQQ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 353 LKTHdegtaaLKQSRAEKETIIrkeiEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELED 432
Cdd:TIGR04523 410 KDEQ------IKKLQQEKELLE----KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 433 LHKLPEKNQREIEDCNKKLESLEVSKVTLNEE---LEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKgevqvFES 509
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKvkdLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDD-----FEL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 510 QLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEIN 589
Cdd:TIGR04523 555 KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
91-143 |
3.39e-11 |
|
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: 63.15 E-value: 3.39e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 24584683 91 KIVNRNFKSYAGEVELGPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIR 143
Cdd:cd03227 1 KIVLGRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATR 53
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
350-975 |
4.28e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.24 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 350 AEELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKE 429
Cdd:PTZ00121 1286 AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 430 LEDLHKLPEKNQREIEDCNKKLEslEVSKVtlnEELEKQQAELTKTTAPLTEKRL--KLSDELVGLKEKVNTA-----KG 502
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAE--EKKKA---DEAKKKAEEDKKKADELKKAAAakKKADEAKKKAEEKKKAdeakkKA 1440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 503 EVQVFESQLKilKQAEttESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCN 582
Cdd:PTZ00121 1441 EEAKKADEAK--KKAE--EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 583 KLRteinERSSVMQAQRSNNKVLDFLMRMKMEGKIPGILGRLGDLGGIDAKYDIAISTACGRLDNIVTDNYETASAAIGA 662
Cdd:PTZ00121 1517 KAE----EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 663 LKEYNVGRATFITLDKIEHHRREANSRINTP------ENVPRLYDLVKVEDDRVRTAFYFALRNTLVCDDLEQGTRIAYg 736
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEelkkaeEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE- 1671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 737 RERYRVVTLRGEMIEMTGTMSGGGSRPIRGKMGTQVRTKTAESADSSQISQKALEDMQIQAEELQARvnycqeqqgslER 816
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE-----------AE 1740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 817 EIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKtTDERAVKEREEQIEAAKQELEQAQ-------- 888
Cdd:PTZ00121 1741 EDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE-EDEKRRMEVDKKIKDIFDNFANIIeggkegnl 1819
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 889 ---FAEQAVSSQIEEIQNQYDTLRNESvkpveakikkvnSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAA 965
Cdd:PTZ00121 1820 vinDSKEMEDSAIKEVADSKNMQLEEA------------DAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
650
....*....|
gi 24584683 966 EEKLKSLNED 975
Cdd:PTZ00121 1888 DEIEKIDKDD 1897
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
299-970 |
6.46e-11 |
|
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: 67.45 E-value: 6.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 299 EMKDLEQPFNEAvdylkkeNELVRTKSFHIQKIISIKKSKLEQYTQEHEACA----------EELKTHDEGTA-ALKQSR 367
Cdd:pfam15921 86 QVKDLQRRLNES-------NELHEKQKFYLRQSVIDLQTKLQEMQMERDAMAdirrresqsqEDLRNQLQNTVhELEAAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 368 AEKETIIRKEIEEYealvkkrEQIKKRLVTVESAYTEIQSTMenTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDC 447
Cdd:pfam15921 159 CLKEDMLEDSNTQI-------EQLRKMMLSHEGVLQEIRSIL--VDFEEASGKKIYEHDSMSTMHFRSLGSAISKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 448 NKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELV--------GLKEKVNTAKGEVQVFESQLKILKQAET 519
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLIseheveitGLTEKASSARSQANSIQSQLEIIQEQAR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 520 TESRKY-----------ETLKSSYEQSQKSLEEKvtrVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEI 588
Cdd:pfam15921 310 NQNSMYmrqlsdlestvSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 589 NERSSVMQAQRSNNKvldflmrmkmegkipgilgRLGDlggidakydiaistacgrldnivtdnyetasaaigalkeYNV 668
Cdd:pfam15921 387 HKREKELSLEKEQNK-------------------RLWD---------------------------------------RDT 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 669 GRAtfITLDkieHHRREANSRintPENVPRLYDLVKveddrvrtafyfALRNTLVCDDLEQGTRIAYGRERYRVVTLRGE 748
Cdd:pfam15921 409 GNS--ITID---HLRRELDDR---NMEVQRLEALLK------------AMKSECQGQMERQMAAIQGKNESLEKVSSLTA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 749 MIEMTGTMSGGGSRPIRG-KMGTQVRTKTAESADSS-QISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGlq 826
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAkKMTLESSERTVSDLTASlQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNV-- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 827 RDEAEYKRLAVS-----ITSLEQQMaSNLKQCEAQRQRMLKKTTDERAVKEREeqIEAAKQELEQAQFAEQAVSSQIEEI 901
Cdd:pfam15921 547 QTECEALKLQMAekdkvIEILRQQI-ENMTQLVGQHGRTAGAMQVEKAQLEKE--INDRRLELQEFKILKDKKDAKIREL 623
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584683 902 QNQYDTLRNESVKPVEA------KIKKVNSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLK 970
Cdd:pfam15921 624 EARVSDLELEKVKLVNAgserlrAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLK 698
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
374-590 |
1.14e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 374 IRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEknqrEIEDCNKKLES 453
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE----EIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 454 LEVSKVTLNE---ELEKQQAELTKTTAPLTEKRLKLSD---------ELVGLKEKVNTAKGEVQVFESQLKILKQAETTE 521
Cdd:PRK03918 250 LEGSKRKLEEkirELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24584683 522 SRKYETLKSSYEQSQKSLEEKVTRVDELKESIpRMKTEIASKSAEVDKMVKEERNLSMQcnKLRTEINE 590
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRLTGLTPE--KLEKELEE 395
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
89-250 |
2.89e-10 |
|
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: 62.28 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYAGEVELGPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRCKRVSTLIHSSSSYPNLrSCSVAVH 168
Cdd:cd03272 1 IKQVIIQGFKSYKDQTVIEPFSPKHNVVVGRNGSGKSNFFAAIRFVLSDEYTHLREEQRQALLHEGSGPSVM-SAYVEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 169 FkqivDKGDGTCEdVPDSSIVIERT--AMSDnssYYQINDKRAQLKDVAKLLKKHHVDLEHNRFLILQGEVESIAMMKPK 246
Cdd:cd03272 80 F----DNSDNRFP-IDKEEVRLRRTigLKKD---EYFLDKKNVTKNDVMNLLESAGFSRSNPYYIVPQGKINSLTNMKQD 151
|
....
gi 24584683 247 GQTE 250
Cdd:cd03272 152 EQQE 155
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
280-915 |
4.37e-10 |
|
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: 64.75 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 280 DQLTDDRTEKHNRCKLAEREMKD-LEQPFNE---AVDYLKKENELVRTKSFHIQKIISIKKsklEQYTQEHEACAEELKT 355
Cdd:pfam15921 245 DQLEALKSESQNKIELLLQQHQDrIEQLISEhevEITGLTEKASSARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 356 HDEGTAALKQSRAEKETIIRKEIEEYEalvkkreqikKRLVTVESAYTEIQSTME-------NTNKQRKKDKAQIEKNEK 428
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYEDKIEELE----------KQLVLANSELTEARTERDqfsqesgNLDDQLQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 429 EL----EDLHKLPEKN----------QREIEDCNKKLESLEVSKVTLNEELekqQAELTKTTAPLTEKRLKLsdelvglk 494
Cdd:pfam15921 392 ELslekEQNKRLWDRDtgnsitidhlRRELDDRNMEVQRLEALLKAMKSEC---QGQMERQMAAIQGKNESL-------- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 495 EKVNTAKGEVqvfESQLKILKQAETTESRKYETLkssyEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEE 574
Cdd:pfam15921 461 EKVSSLTAQL---ESTKEMLRKVVEELTAKKMTL----ESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQEL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 575 RNLSMQCNKLRTEINERSSVMQAQRSNNKVLDFLmRMKMEgKIPGILGRLGDLGGidakydiAISTACGRLDNIVTDNYE 654
Cdd:pfam15921 534 QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL-RQQIE-NMTQLVGQHGRTAG-------AMQVEKAQLEKEINDRRL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 655 tasaaigALKEYNVGRatfitlDKIEHHRREANSRINTPEnvPRLYDLVKVEDDRVRTAFYFAL-RNTLVCDDLEQGTRI 733
Cdd:pfam15921 605 -------ELQEFKILK------DKKDAKIRELEARVSDLE--LEKVKLVNAGSERLRAVKDIKQeRDQLLNEVKTSRNEL 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 734 AYGRERYRVVTL----RGEMIEMTGTMSGGGSRPIRGKM-GTQVRTKTAESADSSQIS-----QKALEDMQIQAEELQAR 803
Cdd:pfam15921 670 NSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELeQTRNTLKSMEGSDGHAMKvamgmQKQITAKRGQIDALQSK 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 804 VNYCQEQQGSLEREiqtlKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKTT------DERAVKEREEQI 877
Cdd:pfam15921 750 IQFLEEAMTNANKE----KHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAnmevalDKASLQFAECQD 825
|
650 660 670
....*....|....*....|....*....|....*...
gi 24584683 878 EAAKQELEQAQFAEQAvSSQIEEIQNQYDTlRNESVKP 915
Cdd:pfam15921 826 IIQRQEQESVRLKLQH-TLDVKELQGPGYT-SNSSMKP 861
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-590 |
5.97e-10 |
|
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: 63.89 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 273 QQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLK-KENELVRTKSFHIQKIISIKKSKLEQYTQEHEACAE 351
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSeKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 352 ELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELE 431
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 432 DLHKlpeknqrEIEDCNKKLESLEVSKVTLNEELEKQQAE---LTKTTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFE 508
Cdd:TIGR04523 388 NLES-------QINDLESKIQNQEKLNQQKDEQIKKLQQEkelLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 509 SQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEI 588
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
..
gi 24584683 589 NE 590
Cdd:TIGR04523 541 SD 542
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
331-590 |
1.02e-09 |
|
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: 63.12 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 331 IISIKKSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTME 410
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 411 NTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREI---------------------EDCNKKLESLEVSKVTLNEELEKQQ 469
Cdd:TIGR04523 107 KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIdkflteikkkekeleklnnkyNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 470 AELTKTTAPLTEKRLKLSDeLVGLKEKVNTAKGEVQVFESQLKILKQaettesrKYETLKSSYEQSQKSLEEKVTRVDEL 549
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLSN-LKKKIQKNKSLESQISELKKQNNQLKD-------NIEKKQQEINEKTTEISNTQTQLNQL 258
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24584683 550 KESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINE 590
Cdd:TIGR04523 259 KDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
296-590 |
1.07e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.16 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 296 AEREMKDLEQPFNEAVDYLKKEneLVRTKSfhIQKIISIKKSKLEqytqeheacaEELKTHDEGTAALKQSRAEKETIiR 375
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKF--IKRTEN--IEELIKEKEKELE----------EVLREINEISSELPELREELEKL-E 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 376 KEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREI------EDCNK 449
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIklsefyEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 450 KLESLEVSKVTLNEELEKQQAELTKTTApLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLK 529
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEE-KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584683 530 SSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINE 590
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTE 447
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
383-598 |
1.21e-09 |
|
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: 62.09 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 383 ALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLN 462
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 463 EELEKQQAELTK------TTAPLTEKRLKLSDE--------LVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETL 528
Cdd:COG4942 97 AELEAQKEELAEllralyRLGRQPPLALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 529 KSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQ 598
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
95-560 |
2.46e-09 |
|
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: 62.29 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 95 RNFKSYAGE--VELGPFHQSFtAIIGPNGSGKSNVIDSMmfvfgCRANRIRCKRVSTLIHSSSSYPNLRSCSVAVHFKQI 172
Cdd:TIGR00618 9 KNFGSYKGThtIDFTALGPIF-LICGKTGAGKTTLLDAI-----TYALYGKLPRRSEVIRSLNSLYAAPSEAAFAELEFS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 173 VD------KGDGTCE-DVPDSSIVIERTAMSDNSSYYQINDK-RAQLKDVAKLLKkhhvdLEHNRF----LILQGEVESI 240
Cdd:TIGR00618 83 LGtkiyrvHRTLRCTrSHRKTEQPEQLYLEQKKGRGRILAAKkSETEEVIHDLLK-----LDYKTFtrvvLLPQGEFAQF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 241 AMMKPKGQTEnetgMLEYLEdivgtqryirPLQQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENEL 320
Cdd:TIGR00618 158 LKAKSKEKKE----LLMNLF----------PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 321 VRTKSFHIQKIISIKKSKLEQYTQEHEACAEELKTHDEgtaaLKQSRAEKETiIRKEIEEYEALVKKREQ---------I 391
Cdd:TIGR00618 224 LEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQL----LKQLRARIEE-LRAQEAVLEETQERINRarkaaplaaH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 392 KKRLVTV----ESAYTEIQSTMENTNKQRK------KDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKvTL 461
Cdd:TIGR00618 299 IKAVTQIeqqaQRIHTELQSKMRSRAKLLMkraahvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH-TL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 462 NEELEKQQAELTKttapLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEE 541
Cdd:TIGR00618 378 TQHIHTLQQQKTT----LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC 453
|
490
....*....|....*....
gi 24584683 542 KVTRVDELKESIPRMKTEI 560
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKERE 472
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
272-605 |
8.20e-09 |
|
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: 60.12 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 272 LQQINQRVDQLTDdrtekhnRCKLAEREMKDLeqpfNEAVDYLKKENELVRT---KSFHIQKII----SIKKSKLEQYTQ 344
Cdd:pfam05483 263 LEESRDKANQLEE-------KTKLQDENLKEL----IEKKDHLTKELEDIKMslqRSMSTQKALeedlQIATKTICQLTE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 345 EHEACAEELK----THDEGTAALKQSRAEKETIIRKEIEEYEalvKKREQIKKRLVTVESAYTEIQSTMENTNKQRKK-- 418
Cdd:pfam05483 332 EKEAQMEELNkakaAHSFVVTEFEATTCSLEELLRTEQQRLE---KNEDQLKIITMELQKKSSELEEMTKFKNNKEVEle 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 419 --------------DKAQIEKNEKEL----EDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTK---TTA 477
Cdd:pfam05483 409 elkkilaedeklldEKKQFEKIAEELkgkeQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKeklKNI 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 478 PLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLE----EKVTRVDELKESI 553
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELEsvreEFIQKGDEVKCKL 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 24584683 554 PRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQRSNNKVL 605
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAL 620
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
291-573 |
8.30e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 291 NRCKLAEREMKDLEQPFNEAVDYLKKENELVRTKSfhIQKIISIKKSKLEQYTQEH-EACAEELKTHDEGTAALKQsrae 369
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKE--LAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKG---- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 370 KETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTN-KQRKKDKAQIE-------------KNEKELEDLHK 435
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKelepfyneylelkDAEKELEREEK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 436 LPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTT-APLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKIL 514
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 515 KqaETTESRKyetlksSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKS-AEVDKMVKE 573
Cdd:PRK03918 700 K--EELEERE------KAKKELEKLEKALERVEELREKVKKYKALLKERAlSKVGEIASE 751
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1202-1274 |
1.62e-08 |
|
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: 55.33 E-value: 1.62e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24584683 1202 YISNLSGGEKTLSSLALVFALhyyKPsPLYFMDEIDAALDFKNVSIVGHYIKE-RTKNAQFIIVSLRVNMFELA 1274
Cdd:cd00267 77 YVPQLSGGQRQRVALARALLL---NP-DLLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELA 146
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
88-169 |
1.79e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 56.17 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 88 IISKIVNRNFKSYAGEVELgPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRcKRVSTLIHSSSSypnlrSCSVAV 167
Cdd:COG0419 1 KLLRLRLENFRSYRDTETI-DFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRS-KLRSDLINVGSE-----EASVEL 73
|
..
gi 24584683 168 HF 169
Cdd:COG0419 74 EF 75
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
268-612 |
2.40e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 268 YIRPLQQINQRVDQLtdDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKIISIKK--SKLEQYTQE 345
Cdd:PRK03918 360 RHELYEEAKAKKEEL--ERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 346 HEACAEELKTHDEG------TAALKQSRAEKETIIRKEIEEYEALVKKREQIKK--RLVTVESAYTEIQSTMENTNKQrk 417
Cdd:PRK03918 438 CPVCGRELTEEHRKelleeyTAELKRIEKELKEIEEKERKLRKELRELEKVLKKesELIKLKELAEQLKELEEKLKKY-- 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 418 kDKAQIEKNEKELEDLHKLP---EKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVG-L 493
Cdd:PRK03918 516 -NLEELEKKAEEYEKLKEKLiklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEErL 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 494 KE------KVNTAKGEVQVFESQLKILKQAETTESRKYETL---KSSYEQSQKSLEEKVTRVDE-----LKESIPRMKTE 559
Cdd:PRK03918 595 KElepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELaetEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRE 674
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 24584683 560 IASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQRSNNKVLDFLMRMK 612
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELR 727
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
203-592 |
3.17e-08 |
|
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: 58.59 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 203 QINDKRAQLKDVAKLLKKHHVDLE---HNRFLILQGEVESIAMMKP-KGQTENETGML-EYLEDIVG-------TQRYIR 270
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSECQgqmERQMAAIQGKNESLEKVSSlTAQLESTKEMLrKVVEELTAkkmtlesSERTVS 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 271 ----PLQQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQPfNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEQYTQ-- 344
Cdd:pfam15921 500 dltaSLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE-GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlv 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 345 -EHEACAeelkthdeGTAALKQSRAEKETIIRK-EIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQ 422
Cdd:pfam15921 579 gQHGRTA--------GAMQVEKAQLEKEINDRRlELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKD 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 423 IEKNEKEL--------EDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLteKRLKLSDE----- 489
Cdd:pfam15921 651 IKQERDQLlnevktsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL--KSMEGSDGhamkv 728
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 490 LVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKssyeqsqkslEEKvtrvDELKESIPRMKTEIASKSAEVDK 569
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLK----------EEK----NKLSQELSTVATEKNKMAGELEV 794
|
410 420
....*....|....*....|...
gi 24584683 570 MVKEERNLSMQCNKLRTEINERS 592
Cdd:pfam15921 795 LRSQERRLKEKVANMEVALDKAS 817
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
361-567 |
3.44e-08 |
|
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: 57.47 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 361 AALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKN 440
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 441 QREI---------------EDCNKKLESLEVSKvTLNEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAkgevq 505
Cdd:COG4942 110 LRALyrlgrqpplalllspEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL----- 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584683 506 vfESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEV 567
Cdd:COG4942 184 --EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
374-932 |
5.06e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 5.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 374 IRKEIEEyealvKKREQIKKRLVTVESAYTEIQSTMENTNKQRK-----KDKAQ------------IEKNEKELEDLHKL 436
Cdd:PRK02224 192 LKAQIEE-----KEEKDLHERLNGLESELAELDEEIERYEEQREqaretRDEADevleeheerreeLETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 437 PEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTA---PLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKI 513
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAdaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 514 L-KQAETTESR------KYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDK------MVKEERN-LSM 579
Cdd:PRK02224 347 LrEDADDLEERaeelreEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNaedfleELREERDeLRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 580 QCNKLRTEI-NERSSVMQAQRsnnkVLDflmrmkmEGKIPgilgrlgdlggidakydiaistACGRldnIVTDnyetaSA 658
Cdd:PRK02224 427 REAELEATLrTARERVEEAEA----LLE-------AGKCP----------------------ECGQ---PVEG-----SP 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 659 AIGALKEYNVGRATFIT-LDKIEHHRREANSRINtpenvpRLYDLVKVEDDRVRtafyfaLRNTLvcDDLEQgtRIAYGR 737
Cdd:PRK02224 466 HVETIEEDRERVEELEAeLEDLEEEVEEVEERLE------RAEDLVEAEDRIER------LEERR--EDLEE--LIAERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 738 ERYRVVTLRGEmiemtgtmsgggsrpirgkmgtQVRTKTAESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLERE 817
Cdd:PRK02224 530 ETIEEKRERAE----------------------ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 818 IQTLkNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKTTDERAVKER--EEQIEAAKQELEQAQFAEQAVS 895
Cdd:PRK02224 588 IESL-ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVE 666
|
570 580 590
....*....|....*....|....*....|....*..
gi 24584683 896 SQIEEIQNQYDTLRNEsVKPVEAKIKKVNSQIEKLAA 932
Cdd:PRK02224 667 EKLDELREERDDLQAE-IGAVENELEELEELRERREA 702
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
89-134 |
7.55e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 56.09 E-value: 7.55e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 24584683 89 ISKIVNRNFKSYAG-EVELGPFhqsfTAIIGPNGSGKSNVIDSMMFV 134
Cdd:COG4637 2 ITRIRIKNFKSLRDlELPLGPL----TVLIGANGSGKSNLLDALRFL 44
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
796-976 |
1.53e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 796 QAEELQARVNYCQEQqgslEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKTTDER--AVKER 873
Cdd:COG4717 72 ELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElaELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 874 EEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRNESVKPVEAKIKKVNSQIEKLAANVRSLNVGLATADRNItkitg 953
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL----- 222
|
170 180
....*....|....*....|...
gi 24584683 954 nnNNLRENIKAAEEKLKSLNEDR 976
Cdd:COG4717 223 --EELEEELEQLENELEAAALEE 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
787-910 |
2.04e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.79 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 787 QKALEDMQIQAEELQARVNYCQEQQGSLERE---------IQTLKNGLQRDEAEYKRLAV-------SITSLEQQMASNL 850
Cdd:COG3206 225 ESQLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALR 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584683 851 KQCEAQRQRMLKKTTDERAV-KEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRN 910
Cdd:COG3206 305 AQLQQEAQRILASLEAELEAlQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARE 365
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
345-591 |
2.37e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.43 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 345 EHEACAEELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIE 424
Cdd:PRK02224 308 DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 425 KNEKELEDLHK--------------LPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAEL-----------------T 473
Cdd:PRK02224 388 ELEEEIEELRErfgdapvdlgnaedFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgqpvegsphV 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 474 KTTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKyETLKSSYEQSQKSLEEKVTRVDELKESI 553
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERR-EDLEELIAERRETIEEKRERAEELRERA 546
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 24584683 554 PRMKTEIASKSAEVDKM---VKEERNLSMQCNKLRTEINER 591
Cdd:PRK02224 547 AELEAEAEEKREAAAEAeeeAEEAREEVAELNSKLAELKER 587
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
423-905 |
2.66e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 423 IEKNEKELEDLHK----LPEKNQREIEDCNKKLESLEVSKVTLNE------ELEKQQAELTKTTAPLTEKRLKLSD--EL 490
Cdd:COG4717 48 LERLEKEADELFKpqgrKPELNLKELKELEEELKEAEEKEEEYAElqeeleELEEELEELEAELEELREELEKLEKllQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 491 VGLKEKVNTAKGEVQVFESQLKILKQAEttesRKYETLKSSYEQSQKSLEEKVTRVDELKESIPrmkteiASKSAEVDKM 570
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEELEELLEQLS------LATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 571 VKEERNLSMQCNKLRTEINE-RSSVMQAQRSNNKVLDFLMRMKMEGKIPGILGRLGDLGGIdakydIAISTACGRLDNIV 649
Cdd:COG4717 198 AEELEELQQRLAELEEELEEaQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAL-----LALLGLGGSLLSLI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 650 TDNYETASAAIGALkeynvgratFITLDKIEHHRREANSRINTPENVPRLYDLVKVEDDRVRTAFYFALRNTL-----VC 724
Cdd:COG4717 273 LTIAGVLFLVLGLL---------ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeelleLL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 725 DDLEQG----TRIAYGRERYRVVTLRGEMIEMTgTMSGGGSRPIRGKMGTQVRTKTAESADSSQISQkaledmQIQAEEL 800
Cdd:COG4717 344 DRIEELqellREAEELEEELQLEELEQEIAALL-AEAGVEDEEELRAALEQAEEYQELKEELEELEE------QLEELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 801 QARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMasnlkqceaqrQRMLKKTTDERAVKEREEQIEAA 880
Cdd:COG4717 417 ELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-----------EQLEEDGELAELLQELEELKAEL 485
|
490 500
....*....|....*....|....*...
gi 24584683 881 KQELEQ---AQFAEQAVSSQIEEIQNQY 905
Cdd:COG4717 486 RELAEEwaaLKLALELLEEAREEYREER 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
189-606 |
2.67e-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: 55.51 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 189 VIERTAMSDNSSYYQ--------INDKRAQLKDVAKLLKKHHVDLEHNRFLilqGEVESIAMMKPKGQTENETGMLEyle 260
Cdd:pfam15921 303 IIQEQARNQNSMYMRqlsdlestVSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTERDQFSQESGNLD--- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 261 divgtQRYIRPLQQINQRVDQLTddrTEKHNRCKLAEREMKDleqpfNEAVDYLKKENELVRTKSFHIQKIISIKKSKLE 340
Cdd:pfam15921 377 -----DQLQKLLADLHKREKELS---LEKEQNKRLWDRDTGN-----SITIDHLRRELDDRNMEVQRLEALLKAMKSECQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 341 QYTQEHEACAEELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDK 420
Cdd:pfam15921 444 GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 421 AQIEKNEKELEDLHKLPEKNQREIEDCNK-KLESLEVSKVTlneELEKQQAE-LTKTTAPLTEKRLKLSDELVGLKEKVN 498
Cdd:pfam15921 524 SRVDLKLQELQHLKNEGDHLRNVQTECEAlKLQMAEKDKVI---EILRQQIEnMTQLVGQHGRTAGAMQVEKAQLEKEIN 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 499 TAKGEVQvfesQLKILKQAETTESRKYETLKSSYEQSQKSL----EEKVTRVDELKESIPRMKTEIASKSAEVDKMVKE- 573
Cdd:pfam15921 601 DRRLELQ----EFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDy 676
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 24584683 574 ---ERN-------LSMQCNKLRTEINERSSVMQAQRSNNKVLD 606
Cdd:pfam15921 677 evlKRNfrnkseeMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
294-574 |
3.65e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 294 KLAEREMKDLEQPFNEAVDylKKENELVRTKSFHIQKIISIKKSKLE-QYTQEHEACAEELKTHDEgtAALKQSRAEKET 372
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAA--KKKADEAKKKAEEKKKADEAKKKAEEaKKADEAKKKAEEAKKAEE--AKKKAEEAKKAD 1473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 373 IIRKEIEEyealVKKREQIKKRlvtVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKnqREIEDCNKKLE 452
Cdd:PTZ00121 1474 EAKKKAEE----AKKADEAKKK---AEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA--KKADEAKKAEE 1544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 453 SLEVSKVTLNEEL----EKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKI--LKQAE-----TTE 521
Cdd:PTZ00121 1545 KKKADELKKAEELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeAKKAEeakikAEE 1624
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24584683 522 SRKYETLKSSYEQSQKSLEEKVTRVDELK--ESIPRMKTEIASKSAEVDKMVKEE 574
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKkaEEENKIKAAEEAKKAEEDKKKAEE 1679
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
386-554 |
4.17e-07 |
|
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: 52.62 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 386 KKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLhklpeknQREIEDCNKKLESLE--VSKVTLNE 463
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-------ELEIEEVEARIKKYEeqLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 464 ELEKQQAELTKttapLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKv 543
Cdd:COG1579 90 EYEALQKEIES----LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE- 164
|
170
....*....|.
gi 24584683 544 trVDELKESIP 554
Cdd:COG1579 165 --REELAAKIP 173
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
284-596 |
5.16e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 284 DDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENElvRTKSFHIQKIISIKKS----KLEQYTQEHEA-CAEELKTHDE 358
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA--KKKADEAKKAEEAKKAdeakKAEEAKKADEAkKAEEKKKADE 1550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 359 GTAALKQSRAE---KETIIRKEIEEYEALVKKREQIKK----RLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKE-- 429
Cdd:PTZ00121 1551 LKKAEELKKAEekkKAEEAKKAEEDKNMALRKAEEAKKaeeaRIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAee 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 430 ----LEDLHKLPEKNQREIEDCNKKLESLEVSKVTL--NEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKGE 503
Cdd:PTZ00121 1631 ekkkVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEakKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 504 VQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEkvTRVDE-LKESIPRMKTEIASKSAEVDK---------MVKE 573
Cdd:PTZ00121 1711 EAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE--AKKDEeEKKKIAHLKKEEEKKAEEIRKekeavieeeLDEE 1788
|
330 340
....*....|....*....|...
gi 24584683 574 ERNLSMQCNKLRTEINERSSVMQ 596
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIFDNFANII 1811
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
216-599 |
5.23e-07 |
|
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: 54.34 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 216 KLLKKHHVDLEHN----RFLILQGEVESIAMMKPKGQTENETGMLEYLEDIVG-TQRYIRPLQQINQRVDQLTDDRTEKH 290
Cdd:pfam05483 363 ELLRTEQQRLEKNedqlKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAeDEKLLDEKKQFEKIAEELKGKEQELI 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 291 NRCKLAEREMKDLE----------QPFNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEQYTQEHEACAEELKTHDEGT 360
Cdd:pfam05483 443 FLLQAREKEIHDLEiqltaiktseEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDI 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 361 AALKQSR----------AEKETIIRKEIEEY-EALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKD-------KAQ 422
Cdd:pfam05483 523 INCKKQEermlkqienlEEKEMNLRDELESVrEEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILenkcnnlKKQ 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 423 IEKNEKELEDLHKLPEKNQREIEDCNKKLESLE--VSKVTLNEELEKQQ-AELTKTTAPLTEKRlKLSDElvGLKEKVNT 499
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEikVNKLELELASAKQKfEEIIDNYQKEIEDK-KISEE--KLLEEVEK 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 500 AKGEV-QVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEK-------VTRVDELKESIPRMKTEIASKSAEVDKMV 571
Cdd:pfam05483 680 AKAIAdEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERdselglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
|
410 420
....*....|....*....|....*...
gi 24584683 572 KEERNLSMQCNKLRTEINERSSVMQAQR 599
Cdd:pfam05483 760 KQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
277-594 |
7.57e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 277 QRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEqYTQEHEACAEELKTH 356
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEE-YIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 357 DEGTAALKQSRAEKETIIR--KEIEEYEA----LVKKREQIKKRLVTVES---AYTEIQSTMENTNKQRKKDKA-QIEKN 426
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEEriKELEEKEErleeLKKKLKELEKRLEELEErheLYEEAKAKKEELERLKKRLTGlTPEKL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 427 EKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLN---EELEKQQAELTKTTAPLTEK-RLKLSDElvgLKEKVNTAKG 502
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGKCPVCGRELTEEhRKELLEE---YTAELKRIEK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 503 EVQVFESQLKILKQAET------TESRKYETLKSSYEQsQKSLEEKVTRVDelKESIPRMKTEIASKSAEVDKMVKEERN 576
Cdd:PRK03918 467 ELKEIEEKERKLRKELRelekvlKKESELIKLKELAEQ-LKELEEKLKKYN--LEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
330
....*....|....*...
gi 24584683 577 LSMQCNKLRTEINERSSV 594
Cdd:PRK03918 544 LKKELEKLEELKKKLAEL 561
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
808-1021 |
9.27e-07 |
|
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: 52.84 E-value: 9.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 808 QEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKTTDERAVKEREEQIEAAKQELeQA 887
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ-KE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 888 QFAEQAVSSQIEEIQNQYDTL-RNESVKPVEAKIKKVNSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAE 966
Cdd:COG4942 105 ELAELLRALYRLGRQPPLALLlSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24584683 967 EKLKSLNEDRNKAKEKKEELEKEIEESEASIEGAKSQSSDIKKEIDEITKEENKR 1021
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
330-594 |
1.03e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.09 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 330 KIISIKKSKLEQYTQEHEACAEELKthdegtAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTM 409
Cdd:PHA02562 184 QTLDMKIDHIQQQIKTYNKNIEEQR------KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 410 ENTNKQRKKDKAQIEKNEKEledlHKLPEKNQ------REIEDCNKKLESLEVSKVTLNEELEKqqaeltkttapltekr 483
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKV----IKMYEKGGvcptctQQISEGPDRITKIKDKLKELQHSLEK---------------- 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 484 lklsdelvglkekVNTAKGEVQVFESQLkilkqaeTTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASK 563
Cdd:PHA02562 318 -------------LDTAIDELEEIMDEF-------NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN 377
|
250 260 270
....*....|....*....|....*....|.
gi 24584683 564 SAEVDKMVKEERNLSMQCNKLRTEINERSSV 594
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYHRGIV 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
336-507 |
1.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 336 KSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIiRKEIEEYEALV------KKREQIKKRLVTVESAYTEIQSTM 409
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-REELEKLEKLLqllplyQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 410 ENTN---KQRKKDKAQIEKNEKELEDLHK-LPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLteKRLK 485
Cdd:COG4717 156 EELReleEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL--EQLE 233
|
170 180
....*....|....*....|..
gi 24584683 486 LSDELVGLKEKVNTAKGEVQVF 507
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-537 |
1.37e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 328 IQKIISIKKSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQS 407
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 408 TMENTNKQRK-------KDKAQIEKNekeLEDLHKLPEKNQREIEDCNKKLESLEvskvTLNEELEKQQAELTKTTAPLT 480
Cdd:COG4942 112 ALYRLGRQPPlalllspEDFLDAVRR---LQYLKYLAPARREQAEELRADLAELA----ALRAELEAERAELEALLAELE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24584683 481 EKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQK 537
Cdd:COG4942 185 EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
771-948 |
1.47e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 771 QVRTKTAESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQ--MAS 848
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQppLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 849 NLKQCEAQ----RQRMLKKTTDER-----AVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRNES---VKPV 916
Cdd:COG4942 125 LLSPEDFLdavrRLQYLKYLAPARreqaeELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERqklLARL 204
|
170 180 190
....*....|....*....|....*....|..
gi 24584683 917 EAKIKKVNSQIEKLAANVRSLNVGLATADRNI 948
Cdd:COG4942 205 EKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
305-1149 |
1.89e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 305 QPFNEAVDYLKKENElVRTKSFHIQKIISIKKSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKEtiIRKEIEEYEAL 384
Cdd:PTZ00121 1073 KPSYKDFDFDAKEDN-RADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAED--ARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 385 VKKREQIKKRlvTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKEL---EDLHKLPE----KNQREIEDCNKKLESLEVS 457
Cdd:PTZ00121 1150 DAKRVEIARK--AEDARKAEEARKAEDAKKAEAARKAEEVRKAEELrkaEDARKAEAarkaEEERKAEEARKAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 458 KVTLNEELEKQQAELTKTtapltekrlklsdELVGLKEKVNTAKGEVQVFESQLKILKQAEttESRKYETLKSSyeqsqk 537
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKA-------------EEERNNEEIRKFEEARMAHFARRQAAIKAE--EARKADELKKA------ 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 538 sleEKVTRVDELKESIPRMKTEIASKSAEVDKMVKEERnlsmqcnKLRTEINERSSVMQAQRSNNKVLDFLMRMKMEGKi 617
Cdd:PTZ00121 1287 ---EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAK-------KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA- 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 618 pgilgrlgdlggidaKYDIAISTACGRLDNIVTDnyETASAAIGALKEYNVGRATFITLDKIEHHRREANsRINTPENVP 697
Cdd:PTZ00121 1356 ---------------ADEAEAAEEKAEAAEKKKE--EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAK 1417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 698 RLYDLVKVEDDRVRTAfyfalrntlvcddlEQGTRIAYGRERYRVVTLRGEmiemtgtmsgggsrpiRGKMGTQVRTKTA 777
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKA--------------DEAKKKAEEAKKADEAKKKAE----------------EAKKAEEAKKKAE 1467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 778 ESADSSQISQKALEdmQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQ-QMASNLKQCEAQ 856
Cdd:PTZ00121 1468 EAKKADEAKKKAEE--AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEaKKADEAKKAEEK 1545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 857 RQ-------RMLKKTTDERAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDT----------------LRNESV 913
Cdd:PTZ00121 1546 KKadelkkaEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkmkaeeakkaeeakIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 914 KPVEAKIKKVNSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSLNEDRNKAKEKKEELEKEIEES 993
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 994 EasiegAKSQSSDIKKEIDEITKEENKRNIERIEIDTKLQAAAGKMNKVKNDipgwqaQLAPLKLNEIPGETEPQAPLKE 1073
Cdd:PTZ00121 1706 E-----LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD------EEEKKKIAHLKKEEEKKAEEIR 1774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1074 LNEEELEAETLEALQYKQTM-LEEDLKTKKPNLSCIKEFNEKRLVYLDRVRVLEDITSK-----RNEMRDKYEEVRKRRY 1147
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMeVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKevadsKNMQLEEADAFEKHKF 1854
|
..
gi 24584683 1148 KE 1149
Cdd:PTZ00121 1855 NK 1856
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
784-888 |
1.95e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 51.59 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 784 QISQKALEDMQIQAEELQARVNYcQEQQGSLEREIQTLKNGLQRDEAEYKRL-------AVSITSLEQ------QMASNL 850
Cdd:COG1566 86 AQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYqalykkgAVSQQELDEaraaldAAQAQL 164
|
90 100 110
....*....|....*....|....*....|....*...
gi 24584683 851 KQCEAQRQRMLKKTTDERAVKEREEQIEAAKQELEQAQ 888
Cdd:COG1566 165 EAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAE 202
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
89-141 |
2.50e-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: 51.54 E-value: 2.50e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 24584683 89 ISKIVNRNFKSYaGEVELgPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANR 141
Cdd:COG3593 3 LEKIKIKNFRSI-KDLSI-ELSDDLTVLVGENNSGKSSILEALRLLLGPSSSR 53
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
352-504 |
2.93e-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: 49.92 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 352 ELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIE--KNEKE 429
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 430 LEDLHKLPEKNQREIEDCNK-------KLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKG 502
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDeilelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
..
gi 24584683 503 EV 504
Cdd:COG1579 171 KI 172
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
419-584 |
3.16e-06 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 51.98 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 419 DKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLevsKVTLnEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVN 498
Cdd:pfam05911 679 KTEENKRLKEEFEQLKSEKENLEVELASCTENLEST---KSQL-QESEQLIAELRSELASLKESNSLAETQLKCMAESYE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 499 TAKGEVQVFESQLKILKQaettesrKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKS--AEVDKMVKEERN 576
Cdd:pfam05911 755 DLETRLTELEAELNELRQ-------KFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCdaDQEDKKLQQEKE 827
|
....*...
gi 24584683 577 LSMQCNKL 584
Cdd:pfam05911 828 ITAASEKL 835
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
308-977 |
3.31e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.76 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 308 NEAVDYLKKENELVRTKSFHIqKIISIKKSKLEQYTQEheacAEELKTHDEGTAALKQSRAEKetiiRKEIEEyealvkK 387
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAEL-RLSHLHFGYKSDETLI----ASRQEERQETSAELNQLLRTL----DDQWKE------K 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 388 REQIKKRLVTVESAYTEIQSTMENTNKQRKK-DKAQIEKNEKELEDLHKLpeknQREIEDCNKKLESLEVSKVTLNEELE 466
Cdd:pfam12128 303 RDELNGELSAADAAVAKDRSELEALEDQHGAfLDADIETAAADQEQLPSW----QSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 467 KQQA----ELTKTTAPLTEKRLKLSDELVGLKEkvnTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEK 542
Cdd:pfam12128 379 RRRSkikeQNNRDIAGIKDKLAKIREARDRQLA---VAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQ 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 543 VTRVDELK-------ESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQRSNnkvLDFLMRMKMEG 615
Cdd:pfam12128 456 ATATPELLlqlenfdERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA---LDELELQLFPQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 616 kiPGILGRLGDLGGIDAKYDIA--ISTA-CGRLDnivTDNYETASAAIGALKEYNVGratfITLDKIEHhrreansrint 692
Cdd:pfam12128 533 --AGTLLHFLRKEAPDWEQSIGkvISPElLHRTD---LDPEVWDGSVGGELNLYGVK----LDLKRIDV----------- 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 693 PENVpRLYDLVKVEDDRVRTAFyfalrntlvcddleQGTRIAYGRERYRVVTLRGEMIEMTGTMSGGgSRPIRGKMGTQV 772
Cdd:pfam12128 593 PEWA-ASEEELRERLDKAEEAL--------------QSAREKQAAAEEQLVQANGELEKASREETFA-RTALKNARLDLR 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 773 RTKTAESADSSQIsQKALEDMQIQAEElqaRVNYCQEQQGSLEREIQTLKNGLQRDEAEYK------------------- 833
Cdd:pfam12128 657 RLFDEKQSEKDKK-NKALAERKDSANE---RLNSLEAQLKQLDKKHQAWLEEQKEQKREARtekqaywqvvegaldaqla 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 834 RLAVSITSLEQQMASNLKQCEAQRQRMLKKT-TDERAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRN-- 910
Cdd:pfam12128 733 LLKAAIAARRSGAKAELKALETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPrl 812
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584683 911 -ESVKPVEAKIKKVNSQIEKLAANVR----SLNVGLATADRNITKITGNNNNLRENIkaaeEKLKSLNEDRN 977
Cdd:pfam12128 813 aTQLSNIERAISELQQQLARLIADTKlrraKLEMERKASEKQQVRLSENLRGLRCEM----SKLATLKEDAN 880
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
776-966 |
4.38e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 776 TAESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEA 855
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 856 Q----------------------------RQRMLKKTTDE-----RAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQ 902
Cdd:COG3883 91 RaralyrsggsvsyldvllgsesfsdfldRLSALSKIADAdadllEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24584683 903 NQYDTLRNEsvkpVEAKIKKVNSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAE 966
Cdd:COG3883 171 AELEAQQAE----QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
787-934 |
5.77e-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: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 787 QKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASN---------LKQCEAQR 857
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyealQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584683 858 QRMLKKttdERAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRNEsvkpVEAKIKKVNSQIEKLAANV 934
Cdd:COG1579 103 RRISDL---EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE----LEAELEELEAEREELAAKI 172
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
844-952 |
8.19e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 844 QQMASNLKQCEAQRQRMLKKTTDERAVKEREEQIEAAKQELEQAQ---------FAEQAVS-SQIEEIQNQYDTLRNEsV 913
Cdd:COG1566 86 AQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQreleryqalYKKGAVSqQELDEARAALDAAQAQ-L 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24584683 914 KPVEAKIKKVN------SQIEKLAANVRSLNVGLATADRNITKIT 952
Cdd:COG1566 165 EAAQAQLAQAQaglreeEELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
396-604 |
1.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 396 VTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTK- 474
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 475 ---------TTAPLTEkrLKLSDELVGLKEKVNTAKgevQVFESQLKILKQAETTEsRKYETLKSSYEQSQKSLEEKVTR 545
Cdd:COG3883 92 aralyrsggSVSYLDV--LLGSESFSDFLDRLSALS---KIADADADLLEELKADK-AELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24584683 546 VDELKESiprMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQAQRSNNKV 604
Cdd:COG3883 166 LEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
273-482 |
1.37e-05 |
|
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: 49.74 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 273 QQINQRVDQltddRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENELVRTKSFHI---QKIISIKKSKLEQYTQEHEAc 349
Cdd:pfam17380 388 QQKNERVRQ----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRleeERAREMERVRLEEQERQQQV- 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 350 aeELKTHDEGTAALKQSRAEKETIIRKEIEEYEALV--KKREQIKKRLVTVESAYTEIQSTMENTNK-----QRKKDKAQ 422
Cdd:pfam17380 463 --ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIleKELEERKQAMIEEERKRKLLEKEMEERQKaiyeeERRREAEE 540
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584683 423 IEKNEKELEDLHKLPEKNQREIEDcNKKLESLEVSKVTLNE--ELEKQQAELTKTTAPLTEK 482
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREMMRQivESEKARAEYEATTPITTIK 601
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
266-601 |
2.33e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.02 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 266 QRYIRPLQqiNQRVDQLTDDRTEKHNRCKlAEREMKDLEQPFN----EAVDYLKKENELVRTKSFHIQKIISIKKSkLEQ 341
Cdd:pfam01576 263 LKKIRELE--AQISELQEDLESERAARNK-AEKQRRDLGEELEalktELEDTLDTTAAQQELRSKREQEVTELKKA-LEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 342 YTQEHEACAEELK-----THDEGTAALKQSRAEKETIIRKEieeyEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQR 416
Cdd:pfam01576 339 ETRSHEAQLQEMRqkhtqALEELTEQLEQAKRNKANLEKAK----QALESENAELQAELRTLQQAKQDSEHKRKKLEGQL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 417 KKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPL---TEKRLKLSDELVGL 493
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLqeeTRQKLNLSTRLRQL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 494 KEKVNTakgevqvFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEVDKMVKE 573
Cdd:pfam01576 495 EDERNS-------LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
330 340
....*....|....*....|....*...
gi 24584683 574 ERNLSMQCNKLRTEINERSSVMQAQRSN 601
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDLDHQRQL 595
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
771-944 |
2.37e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 771 QVRTKTAESADSSQISQKALEDMQIQAE-------ELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVS----- 838
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEelneeynELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrsg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 839 ---------------------ITSLEQQMASNLKQCEAQRQRMLKKTTDERAVKEREEQIEAAKQELEQAQfaeQAVSSQ 897
Cdd:COG3883 100 gsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK---AELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 24584683 898 IEEIQNQYDTLRNEsVKPVEAKIKKVNSQIEKLAANVRSLNVGLATA 944
Cdd:COG3883 177 QAEQEALLAQLSAE-EAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
337-490 |
2.81e-05 |
|
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: 47.23 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 337 SKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETII---RKEIEEYEALVK----KREQIKKRLVTVESA--YTEIQS 407
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELedlEKEIKRLELEIEeveaRIKKYEEQLGNVRNNkeYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 408 TMENtnkqrkkDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLS 487
Cdd:COG1579 97 EIES-------LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
...
gi 24584683 488 DEL 490
Cdd:COG1579 170 AKI 172
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
278-590 |
3.15e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 278 RVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEQYTqEHEACAEELKthd 357
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELK--- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 358 egtaalkqsraEKETIIRKEIEEyeaLVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLP 437
Cdd:TIGR04523 225 -----------KQNNQLKDNIEK---KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 438 EKNQREIEDCNKKLESlEVSKvTLNEELEKQQAELTKTTAPLTEKRLKLSDelvgLKEKVNTAKGEVQVFESQLKILKQA 517
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQ-DWNK-ELKSELKNQEKKLEEIQNQISQNNKIISQ----LNEQISQLKKELTNSESENSEKQRE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 518 ETTESRKYETLKS---SYEQSQKSLEEKV----TRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINE 590
Cdd:TIGR04523 365 LEEKQNEIEKLKKenqSYKQEIKNLESQIndleSKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
87-614 |
3.48e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 87 LIISKIVNRNFKSYA-GEVElgpFHQSFTAIIGPNGSGKSNVIDSMMF-VFGCRanriRCKRVSTLIHSSSsypnlRSCS 164
Cdd:PRK01156 1 MIIKRIRLKNFLSHDdSEIE---FDTGINIITGKNGAGKSSIVDAIRFaLFTDK----RTEKIEDMIKKGK-----NNLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 165 VAVHFKQivdkgDGTCEDVPDSsivIERTAMSDNSSYYQINDKRA---QLKDVAKLLKKHHVDLEHNRFL----ILQGEV 237
Cdd:PRK01156 69 VELEFRI-----GGHVYQIRRS---IERRGKGSRREAYIKKDGSIiaeGFDDTTKYIEKNILGISKDVFLnsifVGQGEM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 238 ESIAMMKPKGQTENETGMLE---------YLEDIVGT---------------QRYIRPLQQINQRVDQLTDDRTEKHNRC 293
Cdd:PRK01156 141 DSLISGDPAQRKKILDEILEinslernydKLKDVIDMlraeisnidyleeklKSSNLELENIKKQIADDEKSHSITLKEI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 294 KLAEREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKIISI--KKSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKE 371
Cdd:PRK01156 221 ERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAesDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 372 TIIRKEIEEYEALVK-------KREQIKKRLVTVES---AYTEIQSTMENTNKQR---KKDKAQIEKNEKELEDLHKLPE 438
Cdd:PRK01156 301 FKYKNDIENKKQILSnidaeinKYHAIIKKLSVLQKdynDYIKKKSRYDDLNNQIlelEGYEMDYNSYLKSIESLKKKIE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 439 KNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAE 518
Cdd:PRK01156 381 EYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGT 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 519 TTESRKYETLKSSYEQSQKSLEEK-------VTRVDELKESIPRMKTEIASKsaEVDKMVKEERNLSMQCNKLRTEINER 591
Cdd:PRK01156 461 TLGEEKSNHIINHYNEKKSRLEEKireieieVKDIDEKIVDLKKRKEYLESE--EINKSINEYNKIESARADLEDIKIKI 538
|
570 580
....*....|....*....|...
gi 24584683 592 SSVMQAQRSNNKVLDFLMRMKME 614
Cdd:PRK01156 539 NELKDKHDKYEEIKNRYKSLKLE 561
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
203-601 |
3.54e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 203 QINDKRAQLKDVAKLLKKHH------VDLE--HNRFLILQGEVESIammkpkgqtENETGMLEYLEDivGTQRYIRPLQQ 274
Cdd:PRK01156 306 DIENKKQILSNIDAEINKYHaiikklSVLQkdYNDYIKKKSRYDDL---------NNQILELEGYEM--DYNSYLKSIES 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 275 INQRVdqltddRTEKHNRCKLAEREMKDLEQPFNEAvDYLKKENELVRTKSFHIQKIIS---IKKSKLEQYTQEHEACAE 351
Cdd:PRK01156 375 LKKKI------EEYSKNIERMSAFISEILKIQEIDP-DAIKKELNEINVKLQDISSKVSslnQRIRALRENLDELSRNME 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 352 ELKTH-----------DEGTAALKQSRAEKETIIRKEIEEYEALVK----KREQIKKRLVTVESAYTEIQSTMENTNKQR 416
Cdd:PRK01156 448 MLNGQsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKdideKIVDLKKRKEYLESEEINKSINEYNKIESA 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 417 KKDKAQIEKNEKELEDLHKLPEKNQREIEdcNKKLESLEVSkvtlNEELEKQQAELTKTTAPLTEKRlklSDELvglKEK 496
Cdd:PRK01156 528 RADLEDIKIKINELKDKHDKYEEIKNRYK--SLKLEDLDSK----RTSWLNALAVISLIDIETNRSR---SNEI---KKQ 595
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 497 VNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIasksAEVDKMVKEERN 576
Cdd:PRK01156 596 LNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQI----AEIDSIIPDLKE 671
|
410 420
....*....|....*....|....*
gi 24584683 577 LSMQCNKLRTEINERSSVMQAQRSN 601
Cdd:PRK01156 672 ITSRINDIEDNLKKSRKALDDAKAN 696
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
281-603 |
3.69e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 281 QLTDDRTEKHNRCKLAEREMKDLEqpfNEAVDYLKKENELVRTKSfHIQKIISIKKSKLEQYTQEHEacaeELKTHDEGT 360
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQRE---KEKERYKRDREQWERQRR-ELESRVAELKEELRQSREKHE----ELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 361 AALKQSRAEKETIIRKEIEEYEALVKKREQIKKrlvTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKN 440
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAAHEARIRELEEDIK---TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 441 QREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLK------LSDELVGLKEKVNTAKGEVQVFESQLKIL 514
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeneaLLEELRSLQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 515 ------KQAETTESRkYETLKSSYEQSQKSL---EEKVTRVDE---LKESIPRMKTEIASKSAEV---DKMVKEERnlsM 579
Cdd:pfam07888 264 aaqrdrTQAELHQAR-LQAAQLTLQLADASLalrEGRARWAQEretLQQSAEADKDRIEKLSAELqrlEERLQEER---M 339
|
330 340
....*....|....*....|....
gi 24584683 580 QCNKLRTEINERSSVMQAQRSNNK 603
Cdd:pfam07888 340 EREKLEVELGREKDCNRVQLSESR 363
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
172-936 |
3.83e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.51 E-value: 3.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 172 IVDKGDGTCEDVPDSSIVIertamsdNSSYYQINDkraqlkDVAKLLKKHHVDLEHNRFLILQGEVESIAMMKPKGQTEN 251
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIEIAI-------HTSIYNIID------EIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKHYN 1097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 252 -----ETGMLEYLEDIVGTQRYIRPL-QQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQP-----FNEAVDYLKKENEL 320
Cdd:TIGR01612 1098 fddfgKEENIKYADEINKIKDDIKNLdQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVadkaiSNDDPEEIEKKIEN 1177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 321 VRTKSFHIQKIISIKKSKLEQYT--QEHEACAEELKT------HDEGTAALKQSRAEKETiIRKEIEEYEALVKKREQIK 392
Cdd:TIGR01612 1178 IVTKIDKKKNIYDEIKKLLNEIAeiEKDKTSLEEVKGinlsygKNLGKLFLEKIDEEKKK-SEHMIKAMEAYIEDLDEIK 1256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 393 KRLVTVESAY---TEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKvtlneELEKQQ 469
Cdd:TIGR01612 1257 EKSPEIENEMgieMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDINDIKK-----ELQKNL 1331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 470 AELTKTTAPLTEKRLKLSD-----ELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLK--SSYEQSQKSLEEK 542
Cdd:TIGR01612 1332 LDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKddINLEECKSKIEST 1411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 543 V--TRVDELKESIPRMKTEIASKSAEVDKMVKE----ERNLSMQCNKLRTEINERSSVMQAQRSNnkvldflmrmkmegk 616
Cdd:TIGR01612 1412 LddKDIDECIKKIKELKNHILSEESNIDTYFKNadenNENVLLLFKNIEMADNKSQHILKIKKDN--------------- 1476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 617 ipgilgrlgdlGGIDAKYDiaistacgrldnivtdnyetasaaIGALKEYnvgratfitLDKIEHHRREANSRINTPENV 696
Cdd:TIGR01612 1477 -----------ATNDHDFN------------------------INELKEH---------IDKSKGCKDEADKNAKAIEKN 1512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 697 PRLYDLVKVEDDRVRTAFY-FALRNTLVCDDLEQGTRIAYGRERYRVVTLRGEMIEMtgTMSGGGSRPIRGKMGTQVRTK 775
Cdd:TIGR01612 1513 KELFEQYKKDVTELLNKYSaLAIKNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQ--KIKEIKKEKFRIEDDAAKNDK 1590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 776 TAESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQrdEAEYKRLAVSITSLEQQMASnlkqcea 855
Cdd:TIGR01612 1591 SNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQ--DTELKENGDNLNSLQEFLES------- 1661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 856 qrqrmlkkttderaVKEREEQIEAAKQELEQaqfaeqaVSSQIEEIQNQYDTLR-----------NESVKPVEAKIKKVN 924
Cdd:TIGR01612 1662 --------------LKDQKKNIEDKKKELDE-------LDSEIEKIEIDVDQHKknyeigiiekiKEIAIANKEEIESIK 1720
|
810
....*....|..
gi 24584683 925 SQIEKLAANVRS 936
Cdd:TIGR01612 1721 ELIEPTIENLIS 1732
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
779-977 |
4.76e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 779 SADSSQISQKALEDMQIQAEELQARVNYCQEQQGS-------LEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLK 851
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkqlaaLERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 852 QCEAQRQR------------------MLKKTTD-----------ERAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQ 902
Cdd:COG4942 98 ELEAQKEElaellralyrlgrqpplaLLLSPEDfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584683 903 NQYDTLRNESVKpVEAKIKKVNSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSLNEDRN 977
Cdd:COG4942 178 ALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
1206-1285 |
5.39e-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: 45.67 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 1206 LSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTK---NAQFIIVSLRvNMFELA-NFLVGIY 1281
Cdd:cd03276 110 LSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKkqpGRQFIFITPQ-DISGLAsSDDVKVF 188
|
....
gi 24584683 1282 KVSD 1285
Cdd:cd03276 189 RMKD 192
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
403-610 |
5.44e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 403 TEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEK 482
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 483 RLKLSD---ELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTE 559
Cdd:COG4372 86 NEQLQAaqaELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 24584683 560 IASKSAEVDKMVKEErnLSMQCNKLRTEINERSSVMQAQRSNNKVLDFLMR 610
Cdd:COG4372 166 LAALEQELQALSEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
95-284 |
5.49e-05 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 45.56 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 95 RNFKSYAG-EVElgpFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRCKRVSTLIHSSSSYPNLRS--CSVAVHFKQ 171
Cdd:pfam13476 4 ENFRSFRDqTID---FSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGFVKGDIRIGLEGKgkAYVEITFEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 172 IVDKGDGTCEDVPDSSIVIERTAMSDNSSYYQINDKRAQLKdvakllKKHHVDLEHNRFLILQGEvESIAMMKPKGQTEN 251
Cdd:pfam13476 81 NDGRYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFIS------ELLKSDKIILPLLVFLGQ-EREEEFERKEKKER 153
|
170 180 190
....*....|....*....|....*....|...
gi 24584683 252 ETGMLEYLEDIVGTQRYIRPLQQINQRVDQLTD 284
Cdd:pfam13476 154 LEELEKALEEKEDEKKLLEKLLQLKEKKKELEE 186
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-504 |
7.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 336 KSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIIR--KEIEEYEALVKKREQIKKRLVTVESAYTEIqstmENTN 413
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERL----DASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 414 KQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLE---------------VSKVTLNEELEKQQAELTKTTAP 478
Cdd:COG4913 685 DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelqdrleaaedLARLELRALLEERFAAALGDAVE 764
|
170 180
....*....|....*....|....*.
gi 24584683 479 lTEKRLKLSDELVGLKEKVNTAKGEV 504
Cdd:COG4913 765 -RELRENLEERIDALRARLNRAEEEL 789
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
380-567 |
8.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 380 EYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKL-------- 451
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 452 ---------------ESLE--------VSKVT-----LNEELEKQQAELTKTTAPLTEKRlklsDELVGLKEKVNTAKGE 503
Cdd:COG3883 97 rsggsvsyldvllgsESFSdfldrlsaLSKIAdadadLLEELKADKAELEAKKAELEAKL----AELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24584683 504 VQVFESQLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSAEV 567
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
89-157 |
9.50e-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: 44.90 E-value: 9.50e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24584683 89 ISKIVNRNFKSYA-GEVELGPfhqSFTAIIGPNGSGKSNVIDSMMFVFGCRANRI-RCKRVSTLIHSSSSY 157
Cdd:cd03276 1 IESITLKNFMCHRhLQIEFGP---RVNFIVGNNGSGKSAILTALTIGLGGKASDTnRGSSLKDLIKDGESS 68
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
234-607 |
1.07e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.97 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 234 QGEVESIAMMKPKGQTENETGMLEYLEDIVGTQRYIrpLQQINQRVDQLTDDRTEK---------HNRCKLAEREMKDLE 304
Cdd:TIGR01612 491 QDNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNII--GFDIDQNIKAKLYKEIEAglkesyelaKNWKKLIHEIKKELE 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 305 QpFNEAVDYLKKE-NELVRTKSFHIQKIISIKKSKLEqytqeheaCAEELKTHDEgtaalKQSRAEKETIIRKEIEEYEA 383
Cdd:TIGR01612 569 E-ENEDSIHLEKEiKDLFDKYLEIDDEIIYINKLKLE--------LKEKIKNISD-----KNEYIKKAIDLKKIIENNNA 634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 384 LVKKREQIKKRLVT------------------------VESAYTEIQSTMENTNKQRKKDKAQIE----KNEKELEDLHK 435
Cdd:TIGR01612 635 YIDELAKISPYQVPehlknkdkiystikselskiyeddIDALYNELSSIVKENAIDNTEDKAKLDdlksKIDKEYDKIQN 714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 436 LP----EKNQREIEDCNKKLESLEVS-KVTLNEELEKqqaELTKTTAPLTEKRLKLSDEL---VGLKEKVNTAKGEVQVF 507
Cdd:TIGR01612 715 MEtatvELHLSNIENKKNELLDIIVEiKKHIHGEINK---DLNKILEDFKNKEKELSNKIndyAKEKDELNKYKSKISEI 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 508 ESQLKilkQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPR---MKTEIASKsaeVDKMVKEERNLSMQCNKL 584
Cdd:TIGR01612 792 KNHYN---DQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEmkfMKDDFLNK---VDKFINFENNCKEKIDSE 865
|
410 420
....*....|....*....|...
gi 24584683 585 RTEINERSSVMQAQRSNNKVLDF 607
Cdd:TIGR01612 866 HEQFAELTNKIKAEISDDKLNDY 888
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
782-942 |
1.21e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.11 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 782 SSQIS--QKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMAsnlkqcEAQRQR 859
Cdd:PRK09039 45 SREISgkDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGA------AAEGRA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 860 MLKKttderavkereEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRnESVKPVEAKIKKVNSQIEKLAanvRSLNV 939
Cdd:PRK09039 119 GELA-----------QELDSEKQVSARALAQVELLNQQIAALRRQLAALE-AALDASEKRDRESQAKIADLG---RRLNV 183
|
...
gi 24584683 940 GLA 942
Cdd:PRK09039 184 ALA 186
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
786-1046 |
1.71e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 786 SQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKTT 865
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 866 DERAVKEREEQIEAAKQELEQAQfaeQAVSSQIEEIQNQYDTlRNESVKPVEAKIKKVNSQIEKLAANVRSLNVG----- 940
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQR---KQLEAQIAELQSEIAE-REEELKELEEQLESLQEELAALEQELQALSEAeaeqa 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 941 ----LATADRNITKITGNNNNLRENIKAAEEKLKSLNEDRNKAKEKKEELEKEIEESEASIEGAKSQSSDIKKEIDEITK 1016
Cdd:COG4372 185 ldelLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270
....*....|....*....|....*....|
gi 24584683 1017 EENKRNIERIEIDTKLQAAAGKMNKVKNDI 1046
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALE 294
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
297-553 |
1.96e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 297 EREMKDLEqpfNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIIRK 376
Cdd:PRK01156 489 EIEVKDID---EKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDS 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 377 EIEEY------------EALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREI 444
Cdd:PRK01156 566 KRTSWlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILI 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 445 EDCNKKLESLEvSKVTLNEELEKQQAELTKttaplteKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRK 524
Cdd:PRK01156 646 EKLRGKIDNYK-KQIAEIDSIIPDLKEITS-------RINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDR 717
|
250 260
....*....|....*....|....*....
gi 24584683 525 YETLKSSYEqSQKSLEEKVTRVDELKESI 553
Cdd:PRK01156 718 INDINETLE-SMKKIKKAIGDLKRLREAF 745
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
410-596 |
2.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 410 ENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESL--EVSKVTLN--------EELEKQQAELTKTTAPL 479
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVlrEINEISSElpelreelEKLEKEVKELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 480 TEKRL----------KLSDELVGLKEKVNTAKGEVQVFESQLKILKQAE--TTESRKYETLKSSYEQSQKSLEEKVTRVD 547
Cdd:PRK03918 241 EELEKeleslegskrKLEEKIRELEERIEELKKEIEELEEKVKELKELKekAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 24584683 548 ELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQ 596
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA 369
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
88-130 |
2.83e-04 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 44.76 E-value: 2.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 24584683 88 IISKIVNRNFKSYAgEVELgPFHQSFTAIIGPNGSGKSNVIDS 130
Cdd:COG1195 1 RLKRLSLTNFRNYE-SLEL-EFSPGINVLVGPNGQGKTNLLEA 41
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
814-1023 |
3.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 814 LEREIQTLKnGLQRDEAEYKRLAVSITSLEQQMASnLKQCEAQRQRMLKkttdERAVKEREEQIEAAKQELEQAQFAEQA 893
Cdd:COG4913 247 AREQIELLE-PIRELAERYAAARERLAELEYLRAA-LRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 894 VSSQIEEIQNQYDTLRNESVKPVEAKIKKVNSQIEKLAANVRSLNVGLATADrniTKITGNNNNLRENIKAAEEKLKSLN 973
Cdd:COG4913 321 LREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24584683 974 EDRNKAKEKKEELEKEIEEseasiegAKSQSSDIKKEIDEItkEENKRNI 1023
Cdd:COG4913 398 EELEALEEALAEAEAALRD-------LRRELRELEAEIASL--ERRKSNI 438
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
285-605 |
3.38e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 285 DRTEKHNRCKLAErEMKDLEQPFNEAVD---YLKKENELVRTKSFHIQKIISI----KKSKLEQYTQEHEA--CAEELKT 355
Cdd:PTZ00121 1549 DELKKAEELKKAE-EKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMKLyeeeKKMKAEEAKKAEEAkiKAEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 356 HDEgtaalkqSRAEKETIIRKEIEEyealVKKREQIKKRLVTVE-SAYTEIQSTMENTNKQRKKDKAQIEKNEKE----- 429
Cdd:PTZ00121 1628 AEE-------EKKKVEQLKKKEAEE----KKKAEELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAealkk 1696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 430 -------LEDLHKLPEKNQREIEDCNKKLE--SLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTA 500
Cdd:PTZ00121 1697 eaeeakkAEELKKKEAEEKKKAEELKKAEEenKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 501 KGEVQVFESQLKILKQAETTEsRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKTEIASKSaevdKMVKEERNLSMQ 580
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRMEVD-KKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSK----NMQLEEADAFEK 1851
|
330 340
....*....|....*....|....*
gi 24584683 581 CNKLRTEINERSSVMQAQRSNNKVL 605
Cdd:PTZ00121 1852 HKFNKNNENGEDGNKEADFNKEKDL 1876
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
266-596 |
3.51e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 266 QRYIRPLQQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEQyTQE 345
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL-DQE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 346 HEACAEELKTHDEGTA---------ALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQR 416
Cdd:TIGR00606 480 LRKAERELSKAEKNSLtetlkkevkSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHS 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 417 KKDKAQIE--KNEKELED-LHKLP-EKNQRE--IEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTE--KRLKLSD 488
Cdd:TIGR00606 560 DELTSLLGyfPNKKQLEDwLHSKSkEINQTRdrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcGSQDEES 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 489 ELVGLKEKVNTAK-------GEVQVFESQLKILK----------------QAETTE-SRKYETLKSSYEQSQKSLEEKVT 544
Cdd:TIGR00606 640 DLERLKEEIEKSSkqramlaGATAVYSQFITQLTdenqsccpvcqrvfqtEAELQEfISDLQSKLRLAPDKLKSTESELK 719
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 24584683 545 ----RVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINERSSVMQ 596
Cdd:TIGR00606 720 kkekRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
336-590 |
4.32e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 336 KSKLEQYTQEHEACAEELKTHDEGTAALKQSRAEKETIIRKEIEEYEALVKKREQIKKRLvtvesayTEIQSTMENTNKQ 415
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV-------KELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 416 RKKDKAQIEKNEKELEDLhklpEKNQREIEDCNKKLESLEvskvtlneelEKQQaeltktTAPLT-EKRLKLSDELVGLK 494
Cdd:COG1340 87 LNELREELDELRKELAEL----NKAGGSIDKLRKEIERLE----------WRQQ------TEVLSpEEEKELVEKIKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 495 EKVNTAKGEVQVFESQLKILKQAET--TESRKY-ETLKSSYEQSQK---SLEEKVTRVDELKESIPRMKTEIASKSAEVD 568
Cdd:COG1340 147 KELEKAKKALEKNEKLKELRAELKElrKEAEEIhKKIKELAEEAQElheEMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260
....*....|....*....|..
gi 24584683 569 KMVKEERNLSMQCNKLRTEINE 590
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKK 248
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
272-576 |
4.40e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 272 LQQINQRVDQLTDDRTEKHNRCKLAEREMKDLE---------QPFNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEQY 342
Cdd:TIGR00606 593 LAKLNKELASLEQNKNHINNELESKEEQLSSYEdklfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQL 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 343 TQEHEACAEELKTHDEGTAALKQSRAEKETIIR---KEIEEYEALVKKREQIKKRLVT-----------VESAYTEIQST 408
Cdd:TIGR00606 673 TDENQSCCPVCQRVFQTEAELQEFISDLQSKLRlapDKLKSTESELKKKEKRRDEMLGlapgrqsiidlKEKEIPELRNK 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 409 MENTNKQRKKDKAQIEKNEKELEDLHK-------------LPEKNQREIEDCNKKLES---------LEVSKVTLNEELE 466
Cdd:TIGR00606 753 LQKVNRDIQRLKNDIEEQETLLGTIMPeeesakvcltdvtIMERFQMELKDVERKIAQqaaklqgsdLDRTVQQVNQEKQ 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 467 KQQAELTKTTAPLTEKRlKLSDE----LVGLKEKVNTAKGE-VQVFESQLKILKQAETTESRKYETLKSSYEQSQKslEE 541
Cdd:TIGR00606 833 EKQHELDTVVSKIELNR-KLIQDqqeqIQHLKSKTNELKSEkLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDA--KE 909
|
330 340 350
....*....|....*....|....*....|....*
gi 24584683 542 KVTRVDELKESIPRMKTEIASKSAEVDKMVKEERN 576
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
363-541 |
4.57e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 363 LKQSRAEKETI---IRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEK 439
Cdd:COG4372 54 LEQAREELEQLeeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 440 NQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVG--LKEKVNTAKGEVQVFESQLKILKQA 517
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDelLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180
....*....|....*....|....
gi 24584683 518 ETTESRKYETLKSSYEQSQKSLEE 541
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSA 237
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
299-574 |
4.67e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 299 EMKDLEQPFNE---AVDYLKKENELVRTKSFHIQKIISIKKSKleQYTQEHEACAEELKthDEGTAALKQSRAEKETIIR 375
Cdd:TIGR00606 167 EGKALKQKFDEifsATRYIKALETLRQVRQTQGQKVQEHQMEL--KYLKQYKEKACEIR--DQITSKEAQLESSREIVKS 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 376 KEiEEYEALVKKREQIKKRLVTVESAYTEIQStMENTNKQRKKDKAQIE--------------------------KNEKE 429
Cdd:TIGR00606 243 YE-NELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRKKQMEKDNSELElkmekvfqgtdeqlndlyhnhqrtvrEKERE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 430 LEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLsdELVGLKEKvntAKGEVQVfES 509
Cdd:TIGR00606 321 LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL--ELDGFERG---PFSERQI-KN 394
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584683 510 QLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPR---MKTEIASKSAEVDKMVKEE 574
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtieLKKEILEKKQEELKFVIKE 462
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
113-160 |
5.88e-04 |
|
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: 43.53 E-value: 5.88e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 24584683 113 FTAIIGPNGSGKSNVIDSMMFVFGCRANRIRCKRVSTLIHSSSSYPNL 160
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSL 48
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
422-1045 |
6.91e-04 |
|
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: 44.44 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 422 QIEKNEKELEDLHKLPEKNQREIEDcnkKLESLEVSKVTLNEELEKQQAELTkttapltEKRLKLSDELVGLKEKVNTAK 501
Cdd:pfam12128 252 TLESAELRLSHLHFGYKSDETLIAS---RQEERQETSAELNQLLRTLDDQWK-------EKRDELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 502 GEVQVFESQLKILKQAETtESRKYE-----TLKSSYEQSQKSLE------EKVTR---------VDELKESIPRMKTEIA 561
Cdd:pfam12128 322 SELEALEDQHGAFLDADI-ETAAADqeqlpSWQSELENLEERLKaltgkhQDVTAkynrrrskiKEQNNRDIAGIKDKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 562 SKSAEVDKMVKEERN-LSMQCNKLRTEINerssvmQAQRSNNkvldflmrmkmEGKIpGILGRLGDLGGI--------DA 632
Cdd:pfam12128 401 KIREARDRQLAVAEDdLQALESELREQLE------AGKLEFN-----------EEEY-RLKSRLGELKLRlnqatatpEL 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 633 KYDIAIS-TACGRLDNIVTDNYETASAAIGALKEYNVGRatfitlDKIEHHRREANSRINTPENvpRLYDLVKVEDDRVR 711
Cdd:pfam12128 463 LLQLENFdERIERAREEQEAANAEVERLQSELRQARKRR------DQASEALRQASRRLEERQS--ALDELELQLFPQAG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 712 TAFYFaLRNTLvcddleQGTRIAYGRERYRVVTLRGEMIEMTGTMSGGGSRPIRG--------------KMGTQVRTKTA 777
Cdd:pfam12128 535 TLLHF-LRKEA------PDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvkldlkridvpewaASEEELRERLD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 778 ---ESADSSQISQKALEDMQIQA---------EELQARVNYCQ--EQQGSLEREIQTLKNGLQRDEAEYKRLAV-SITSL 842
Cdd:pfam12128 608 kaeEALQSAREKQAAAEEQLVQAngelekasrEETFARTALKNarLDLRRLFDEKQSEKDKKNKALAERKDSANeRLNSL 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 843 EQQMASNLKQ----CEAQRQRMLKKTTDERA-----VKEREEQIEAAKQELEQAQFAEQAvssQIEEIQNQYDTlrnesv 913
Cdd:pfam12128 688 EAQLKQLDKKhqawLEEQKEQKREARTEKQAywqvvEGALDAQLALLKAAIAARRSGAKA---ELKALETWYKR------ 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 914 kpvEAKIKKVNSQ-IEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSlnedrnkakekkeelekeiee 992
Cdd:pfam12128 759 ---DLASLGVDPDvIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT--------------------- 814
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 24584683 993 seasiegaksQSSDIKKEIDEItkeenKRNIERIEIDTKLQAAAGKMNKVKND 1045
Cdd:pfam12128 815 ----------QLSNIERAISEL-----QQQLARLIADTKLRRAKLEMERKASE 852
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
328-613 |
6.94e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.30 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 328 IQKIISIKKSKLEQYTQEHEACAEELKtHDEGTAALKQSRAE---KETII----------RKEIEEYEALVKKREQIKKR 394
Cdd:COG5022 822 LQKTIKREKKLRETEEVEFSLKAEVLI-QKFGRSLKAKKRFSllkKETIYlqsaqrvelaERQLQELKIDVKSISSLKLV 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 395 LVTVESAYTEIQSTMEN-------------TNKQRKKDKAQIE----KNEKELEDLHKLPEKN------QREIEDCNKKL 451
Cdd:COG5022 901 NLELESEIIELKKSLSSdlienlefkteliARLKKLLNNIDLEegpsIEYVKLPELNKLHEVEsklketSEEYEDLLKKS 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 452 ESLEVSKVTLNEELEKQQAELTKttapLTEKRLKLSDELVGLKEKvntaKGEVQVFESQLKILKQAETTESR--KYETLK 529
Cdd:COG5022 981 TILVREGNKANSELKNFKKELAE----LSKQYGALQESTKQLKEL----PVEVAELQSASKIISSESTELSIlkPLQKLK 1052
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 530 SSYEQSQKSLEEKVTRVDELKESIPRMKTEIA--------SKSAEVDKMVKEERNLSMQCNKLRTEINERSS---VMQAQ 598
Cdd:COG5022 1053 GLLLLENNQLQARYKALKLRRENSLLDDKQLYqlestenlLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKlnlLQEIS 1132
|
330
....*....|....*
gi 24584683 599 RSNNKVLDFLMRMKM 613
Cdd:COG5022 1133 KFLSQLVNTLEPVFQ 1147
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
103-490 |
7.97e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.91 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 103 EVELgPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRAN--RIR--CKR-VSTLIHSSSSYPNLRscsvavhfkQIVDKGD 177
Cdd:COG0497 15 ELEL-EFGPGLTVLTGETGAGKSILLDALGLLLGGRADasLVRhgADKaEVEAVFDLSDDPPLA---------AWLEENG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 178 GtceDVPDSSIVIERTAMSDNSSYYQINDK---RAQLKDVAKLLkkhhVDlehnrfliLQGEVESIAMMKPKGQtenetg 254
Cdd:COG0497 85 L---DLDDGELILRREISADGRSRAFINGRpvtLSQLRELGELL----VD--------IHGQHEHQSLLDPDAQ------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 255 mLEYLEDIVGTQryirplqqinqrvdQLTDDRTEKHNRCKLAEREMKDLEQpfneAVDYLKKENELVRtksFHIQKI--I 332
Cdd:COG0497 144 -RELLDAFAGLE--------------ELLEEYREAYRAWRALKKELEELRA----DEAERARELDLLR---FQLEELeaA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 333 SIKKSKLEQYTQEHE--ACAEELKT---------HDEGTAALKQ-SRAeketiiRKEIEEYEALVKKREQIKKRLvtvES 400
Cdd:COG0497 202 ALQPGEEEELEEERRrlSNAEKLREalqealealSGGEGGALDLlGQA------LRALERLAEYDPSLAELAERL---ES 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 401 AYTEIQSTMENTNKQRkkdkAQIEKNEKELED-------LHKLPEKNQREIED-------CNKKLESLEVS---KVTLNE 463
Cdd:COG0497 273 ALIELEEAASELRRYL----DSLEFDPERLEEveerlalLRRLARKYGVTVEEllayaeeLRAELAELENSderLEELEA 348
|
410 420
....*....|....*....|....*..
gi 24584683 464 ELEKQQAELTKTTAPLTEKRLKLSDEL 490
Cdd:COG0497 349 ELAEAEAELLEAAEKLSAARKKAAKKL 375
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
89-133 |
8.04e-04 |
|
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases with a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213209 [Multi-domain] Cd Length: 270 Bit Score: 43.05 E-value: 8.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 24584683 89 ISKIVNRNFKSYAgEVELgPFHQSFTAIIGPNGSGKSNVIDSMMF 133
Cdd:cd03242 1 LKSLELRNFRNYA-ELEL-EFEPGVTVLVGENAQGKTNLLEAISL 43
|
|
| recf |
TIGR00611 |
recF protein; All proteins in this family for which functions are known are DNA binding ... |
95-157 |
8.15e-04 |
|
recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273173 [Multi-domain] Cd Length: 365 Bit Score: 43.50 E-value: 8.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24584683 95 RNFKSYAgEVELgPFHQSFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRckRVSTLIHSSSSY 157
Cdd:TIGR00611 9 TDFRNYD-AVDL-ELSPGVNVIVGPNGQGKTNLLEAIYYLALGRSHRTS--RDKPLIRFGAEA 67
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
823-932 |
8.57e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 823 NGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMLKKTTDER--AVKEREEQIEAAKQELEQAQFAEQAVSSQIEE 900
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERlaAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAA 144
|
90 100 110
....*....|....*....|....*....|..
gi 24584683 901 IQNQYDtlrnESVKPVEAKIKKVNSQIEKLAA 932
Cdd:PRK09510 145 AKAKAE----AEAKRAAAAAKKAAAEAKKKAE 172
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
280-640 |
8.83e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 280 DQLTDDRTEKHNRCKLAEREMKDLeqpFNEAVDYLKKENELVRTKSFHIQKIISIKkSKLEQYTQEHEAcAEELKTHDEG 359
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDL---VSSKDDVGKNVHELERSKRALEQQVEEMK-TQLEELEDELQA-TEDAKLRLEV 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 360 TAALKQSRAEKETIIRKEIEEyealvKKREQIKKRLvtvesayTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEK 439
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGE-----EKRRQLVKQV-------RELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDA 788
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 440 NQREIEDCNKKLESLEVSKVTLNEELEKQQA--ELTKTTAPLTEKRLK-LSDELVGLKEKVNTAKgevqvfesqlKILKQ 516
Cdd:pfam01576 789 ANKGREEAVKQLKKLQAQMKDLQRELEEARAsrDEILAQSKESEKKLKnLEAELLQLQEDLAASE----------RARRQ 858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 517 AETTESRKYETLKSSYEQSQKSLEEKvtrvDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEIN-ERSSvm 595
Cdd:pfam01576 859 AQQERDELADEIASGASGKSALQDEK----RRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAaERST-- 932
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 24584683 596 qAQRSNNKvldflmRMKMEGKIPGILGRLGDL-GGIDAKYDIAIST 640
Cdd:pfam01576 933 -SQKSESA------RQQLERQNKELKAKLQEMeGTVKSKFKSSIAA 971
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
338-591 |
1.01e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.32 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 338 KLEQYTQEHEACAEE-LKTHDEGTAALKQSRAEKETiiRKEIEEYEAlVKKREQIKKRLVTVESAYTEIQSTMENTNKQR 416
Cdd:pfam02029 70 KREERRQKRLQEALErQKEFDPTIADEKESVAERKE--NNEEEENSS-WEKEEKRDSRLGRYKEEETEIREKEYQENKWS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 417 KKDKAQIEKNEKE---LEDLHKLPEKN----QREIEDCNKKLESLEVSKVTLNE-----ELEKQQAELTKTTAPLTEKRL 484
Cdd:pfam02029 147 TEVRQAEEEGEEEedkSEEAEEVPTENfakeEVKDEKIKKEKKVKYESKVFLDQkrghpEVKSQNGEEEVTKLKVTTKRR 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 485 KLSDELVGLKEKVNTAKGEV-QVFEsqlKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRVDE----LKESIPRMKTE 559
Cdd:pfam02029 227 QGGLSQSQEREEEAEVFLEAeQKLE---ELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREErrklLEEEEQRRKQE 303
|
250 260 270
....*....|....*....|....*....|....*
gi 24584683 560 iasksaEVDKMVKEE---RNLSMQCNKLRTEINER 591
Cdd:pfam02029 304 ------EAERKLREEeekRRMKEEIERRRAEAAEK 332
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
95-137 |
1.13e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.72 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 24584683 95 RNFKSYAGEVEL-----GPFHQSFTAIIGPNGSGKSNVIDSMMFVFGC 137
Cdd:COG1106 8 ENFRSFKDELTLsmvasGLRLLRVNLIYGANASGKSNLLEALYFLRNL 55
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
386-586 |
1.15e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 386 KKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVT---LN 462
Cdd:pfam05483 251 EKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTicqLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 463 EELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKIL------KQAETTESRKYETLKS-SYEQS 535
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIItmelqkKSSELEEMTKFKNNKEvELEEL 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 24584683 536 QKSLEEKVTRVDElKESIPRMKTEIASKSAEVDKMV----KEERNLSMQCNKLRT 586
Cdd:pfam05483 411 KKILAEDEKLLDE-KKQFEKIAEELKGKEQELIFLLqareKEIHDLEIQLTAIKT 464
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
790-887 |
1.33e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 790 LEDMQIQAEELQARVNYCQEQQGSLEREIQTLK---NGLQRDEAEYKRLAVSITSLEQQMA---SNLKQCEAQRQRMLKK 863
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRariKELAARAPAWLAAQDALERLREQSGealADSQEVTAAMQQLLER 638
|
90 100
....*....|....*....|....
gi 24584683 864 ttdERAVKEREEQIEAAKQELEQA 887
Cdd:COG3096 639 ---EREATVERDELAARKQALESQ 659
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
272-612 |
1.46e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.50 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 272 LQQINQRVDQLTDDRTEKHNRCKLAEREmKDLEQPFNEAVDyLKKENELVRTKSFhiQKIISIKKsklEQYTQEHEACae 351
Cdd:TIGR01612 1516 FEQYKKDVTELLNKYSALAIKNKFAKTK-KDSEIIIKEIKD-AHKKFILEAEKSE--QKIKEIKK---EKFRIEDDAA-- 1586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 352 elKTHDEGTAALK--------QSRAEKETIIRKEIEEyeaLVKKREQIKKRLVT--VESAYTEIQSTMENTN------KQ 415
Cdd:TIGR01612 1587 --KNDKSNKAAIDiqlslenfENKFLKISDIKKKIND---CLKETESIEKKISSfsIDSQDTELKENGDNLNslqeflES 1661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 416 RKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLS---DELVG 492
Cdd:TIGR01612 1662 LKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSfntNDLEG 1741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 493 LK-----EKVNTAKGEV--QVFESQLKILKQAETT--ESRKYETLKSSYEQSQKSLEEKV-------TRVDELK-ESIPR 555
Cdd:TIGR01612 1742 IDpneklEEYNTEIGDIyeEFIELYNIIAGCLETVskEPITYDEIKNTRINAQNEFLKIIeiekkskSYLDDIEaKEFDR 1821
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 24584683 556 MKTEIASKSAEV-DKMVKEERNLSMQCNKLRTEINErssvMQAQRSNNKVLDFLMRMK 612
Cdd:TIGR01612 1822 IINHFKKKLDHVnDKFTKEYSKINEGFDDISKSIEN----VKNSTDENLLFDILNKTK 1875
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
273-574 |
1.58e-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: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 273 QQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNE-----AVDYLKKENELVRTKSFHIQKIISIKKSKLEQYTQEHE 347
Cdd:pfam12128 671 KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkreaRTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 348 ACAEELKTH------DEGT-AALKQSRAEKETII------RKEIEEY-----EALVKKREQIKKRLVTVESAYTEIQSTM 409
Cdd:pfam12128 751 ALETWYKRDlaslgvDPDViAKLKREIRTLERKIeriavrRQEVLRYfdwyqETWLQRRPRLATQLSNIERAISELQQQL 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 410 ENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEvskvtLNEELEKQQAELTKTTAPLTEKRLKLSDE 489
Cdd:pfam12128 831 ARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLK-----EDANSEQAQGSIGERLAQLEDLKLKRDYL 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 490 LVGLKEKVN---------TAKGEVQVFES-----------QLKILKQAETTESRKyETLKSSYEQSQKSLEEKVT----R 545
Cdd:pfam12128 906 SESVKKYVEhfknviadhSGSGLAETWESlreedhyqndkGIRLLDYRKLVPYLE-QWFDVRVPQSIMVLREQVSilgvD 984
|
330 340
....*....|....*....|....*....
gi 24584683 546 VDELKESIPRMKTEIASKSAEVDKMVKEE 574
Cdd:pfam12128 985 LTEFYDVLADFDRRIASFSRELQREVGEE 1013
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
188-516 |
1.63e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 188 IVIERTA--MSDNSSYYQINDKRAQLKDVAKLLK---------KHHVDLEHNRFLILQGEVESIAMMkpkgQTENETGML 256
Cdd:pfam15921 480 VVEELTAkkMTLESSERTVSDLTASLQEKERAIEatnaeitklRSRVDLKLQELQHLKNEGDHLRNV----QTECEALKL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 257 EyledIVGTQRYIRPLQQINQRVDQLTDdrteKHNRCKLA-EREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKI---- 331
Cdd:pfam15921 556 Q----MAEKDKVIEILRQQIENMTQLVG----QHGRTAGAmQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELearv 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 332 --ISIKKSKLEQYTQEHEACAEELKTH-DEGTAALKQSRAEKETIIrkeiEEYEALvkKREQIKKRlvtvesayTEIQST 408
Cdd:pfam15921 628 sdLELEKVKLVNAGSERLRAVKDIKQErDQLLNEVKTSRNELNSLS----EDYEVL--KRNFRNKS--------EEMETT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 409 MENTNKQRKKDKAQIEKNEKELEDLH-------KLPEKNQREIEDCNKKLESLEvSKVTLneeLEKQQAELTKTTAPLTE 481
Cdd:pfam15921 694 TNKLKMQLKSAQSELEQTRNTLKSMEgsdghamKVAMGMQKQITAKRGQIDALQ-SKIQF---LEEAMTNANKEKHFLKE 769
|
330 340 350
....*....|....*....|....*....|....*
gi 24584683 482 KRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQ 516
Cdd:pfam15921 770 EKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
114-143 |
1.79e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.96 E-value: 1.79e-03
10 20 30
....*....|....*....|....*....|
gi 24584683 114 TAIIGPNGSGKSNVIDSMMFVFgCRANRIR 143
Cdd:pfam13555 25 TLLTGPSGSGKSTLLDAIQTLL-VPAKRAR 53
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
95-128 |
1.87e-03 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 42.07 E-value: 1.87e-03
10 20 30
....*....|....*....|....*....|....
gi 24584683 95 RNFKSYAgEVELgPFHQSFTAIIGPNGSGKSNVI 128
Cdd:PRK00064 9 TDFRNYE-ELDL-ELSPGVNVLVGENGQGKTNLL 40
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
361-558 |
1.99e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 361 AALKQSRAEKETIIRkeIEEYEALVKKREQIKKRLV---TVESAYTEiqstMENTNKQRKKDKAQIEKNEKELEdlhklP 437
Cdd:COG2433 340 AALKAYDAYKNKFER--VEKKVPPDVDRDEVKARVIrglSIEEALEE----LIEKELPEEEPEAEREKEHEERE-----L 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 438 EKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKttapltekrlklsdelvgLKEKVNTAKGEvqvfesqlkilKQA 517
Cdd:COG2433 409 TEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER------------------LERELSEARSE-----------ERR 459
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 24584683 518 ETTESRKYETLKSSYEQSQKSLEEKVTRVDELKESIPRMKT 558
Cdd:COG2433 460 EIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
415-541 |
2.03e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 39.97 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 415 QRKKD--KAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELtkttAPLTEKRLKLSDELVG 492
Cdd:pfam10473 16 ERKADslKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDL----VTLRSEKENLTKELQK 91
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 24584683 493 LKEKVNTAKGEVQVFESQLKILKQAettESRKYETLKSSYEQSQKSLEE 541
Cdd:pfam10473 92 KQERVSELESLNSSLENLLEEKEQE---KVQMKEESKTAVEMLQTQLKE 137
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
777-887 |
2.24e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 777 AESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQ 856
Cdd:COG4942 132 LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
90 100 110
....*....|....*....|....*....|.
gi 24584683 857 RQRMLKKTTDERAVKEREEQIEAAKQELEQA 887
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
799-1045 |
2.26e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 799 ELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRMlkkTTDERAVKEREEQIE 878
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL---EQNNKKIKELEKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 879 AAKQEL-----EQAQFAEQAVSSQIEEIQNQYDTLRNESVKpVEAKIKKVNSQIEKLAANVRSLNVGLATADR------- 946
Cdd:TIGR04523 292 QLKSEIsdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQ-NNKIISQLNEQISQLKKELTNSESENSEKQReleekqn 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 947 --------------NITKITGNNNNLRENIKAAEEKLKSLNEDRNKAKEKKEELEKEIEESEASIEGAKSQSSDIKKEID 1012
Cdd:TIGR04523 371 eieklkkenqsykqEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270
....*....|....*....|....*....|...
gi 24584683 1013 EITKEENKRNIERIEIDTKLQAAAGKMNKVKND 1045
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-496 |
2.26e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 272 LQQINQRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKenelvrtksfhIQKIISIKKSKLEQYTQEHEACAE 351
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-----------LEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 352 ELKTHDEGTAALKQsraekeTIIRKEIEEYEALVKKREQIkKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELE 431
Cdd:COG4942 98 ELEAQKEELAELLR------ALYRLGRQPPLALLLSPEDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584683 432 DLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEK 496
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
89-133 |
2.44e-03 |
|
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: 40.67 E-value: 2.44e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 24584683 89 ISKIVNRNFKSYA--GEVElgpFHQSFTAIIGPNGSGKSNVIDSMMF 133
Cdd:cd03240 1 IDKLSIRNIRSFHerSEIE---FFSPLTLIVGQNGAGKTTIIEALKY 44
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
277-474 |
2.51e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.48 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 277 QRVDQLTDDRTEKHNRCKLAEREMKDLEQPFNEAVDYLKKENELVRTK--SF---------HIQKIIsiKKSKLEQytQE 345
Cdd:pfam09728 92 KLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKlkSLieqyelrelHFEKLL--KTKELEV--QL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 346 HEACAEELKTHDEgtaalkQSRAEKE-TIIRKEIEEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIE 424
Cdd:pfam09728 168 AEAKLQQATEEEE------KKAQEKEvAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTTFKKEME 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 24584683 425 KNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAELTK 474
Cdd:pfam09728 242 KMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEK 291
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
218-590 |
2.55e-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: 42.34 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 218 LKKHHVDLEHNRFLILQGEVESIAMMKPKGQTENETGMLEYLEDIV--GTQRYIRPLQQINQRVDQltdDRTEKHNRCKl 295
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqGTDEQLNDLYHNHQRTVR---EKERELVDCQ- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 296 aeremKDLEQPFNEAVDYLKKENELVRTksfhiQKIISIKKSKLEQYTQEHEACAEELKTHDEgtaalkQSRAEKETIIR 375
Cdd:TIGR00606 326 -----RELEKLNKERRLLNQEKTELLVE-----QGRLQLQADRHQEHIRARDSLIQSLATRLE------LDGFERGPFSE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 376 KEIEEYEALVKKREQIKKRlvTVESAYTEIQSTMenTNKQRKKDKAQIEKN--EKELEDLHKLPEKNQREIEDCNKKLES 453
Cdd:TIGR00606 390 RQIKNFHTLVIERQEDEAK--TAAQLCADLQSKE--RLKQEQADEIRDEKKglGRTIELKKEILEKKQEELKFVIKELQQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 454 LEVSK---VTLNEELEKQQAELTK-----TTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKY 525
Cdd:TIGR00606 466 LEGSSdriLELDQELRKAERELSKaeknsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKM 545
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584683 526 ETLKSSYEQSQKSLEEKVTRVDELKESiPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEINE 590
Cdd:TIGR00606 546 DKDEQIRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNH 609
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
389-603 |
2.62e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 389 EQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDcnkkleslevskvtLNEELEKQ 468
Cdd:PHA02562 181 QQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEE--------------LTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 469 QAELTKTTAPLTekrlKLSDELVGLKEKVNTAKGEVQVFES--QLKILKQAETTESRKYETLKSSYEQSQKSLEEKVTRV 546
Cdd:PHA02562 247 VMDIEDPSAALN----KLNTAAAKIKSKIEQFQKVIKMYEKggVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 24584683 547 DELKEsiprmkteiasksaevdkMVKEERNLSMQCNKLRTEINERSSVMQAQRSNNK 603
Cdd:PHA02562 323 DELEE------------------IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAK 361
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
788-974 |
2.82e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 788 KALEDMQIQAEELQarvnycqEQQGSLEREIQTLKNGLQR----------------DEAEYKRLAVSITSLE-------- 843
Cdd:PRK04863 786 KRIEQLRAEREELA-------ERYATLSFDVQKLQRLHQAfsrfigshlavafeadPEAELRQLNRRRVELEraladhes 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 844 --QQMASNLKQCEAQRQrMLKKTTDERAVKERE---EQIEAAKQELEQAQFAEQAVSSQ---IEEIQNQYDTLRNE---- 911
Cdd:PRK04863 859 qeQQQRSQLEQAKEGLS-ALNRLLPRLNLLADEtlaDRVEEIREQLDEAEEAKRFVQQHgnaLAQLEPIVSVLQSDpeqf 937
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24584683 912 -----SVKPVEAKIKKVNSQIEKLAANV-RSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSLNE 974
Cdd:PRK04863 938 eqlkqDYQQAQQTQRDAKQQAFALTEVVqRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRARE 1006
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
359-472 |
2.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 359 GTAALKQSRAEKETII---RKEIEEY--EALVKKREQIKKRlvtvesayteiQSTMENTNKQRKKDKAQIEKN------- 426
Cdd:PRK12704 29 AEAKIKEAEEEAKRILeeaKKEAEAIkkEALLEAKEEIHKL-----------RNEFEKELRERRNELQKLEKRllqkeen 97
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 24584683 427 -EKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKQQAEL 472
Cdd:PRK12704 98 lDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
89-151 |
3.01e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 41.14 E-value: 3.01e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24584683 89 ISKIVNRNFKSYAgEVELgPFHQ--SFTAIIGPNGSGKSNVIDSMMFVFGCRANRIRCKRVSTLI 151
Cdd:COG3950 3 IKSLTIENFRGFE-DLEI-DFDNppRLTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLL 65
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
778-1044 |
3.09e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 42.08 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 778 ESADSSQiSQKALEDMQIQAEELQ-------ARVNYCQEQQGSLEREIQTLKNGLQ--------RDEAEYKRLAvSITSL 842
Cdd:pfam01576 255 ETAQKNN-ALKKIRELEAQISELQedleserAARNKAEKQRRDLGEELEALKTELEdtldttaaQQELRSKREQ-EVTEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 843 EQQMASNLKQCEAQRQRMLKKTTdeRAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLrNESVKPVEAKIKK 922
Cdd:pfam01576 333 KKALEEETRSHEAQLQEMRQKHT--QALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL-QQAKQDSEHKRKK 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 923 VNSQIE---------------------KLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEE-------------- 967
Cdd:pfam01576 410 LEGQLQelqarlseserqraelaeklsKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQEllqeetrqklnlst 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 968 KLKSLNEDRNKAKEKKEELEKEIEESEASIEGAKSQSSDIKKEIDEITK-----EENKRNIERiEIDTKLQ------AAA 1036
Cdd:pfam01576 490 RLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGtlealEEGKKRLQR-ELEALTQqleekaAAY 568
|
....*...
gi 24584683 1037 GKMNKVKN 1044
Cdd:pfam01576 569 DKLEKTKN 576
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
89-147 |
3.09e-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: 40.66 E-value: 3.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYaGEVELGPFHqSFTAIIGPNGSGKSNVIDSMMFVFGCRANRI-RCKRV 147
Cdd:cd03277 3 IVRIKLENFVTY-DETEFRPGP-SLNMIIGPNGSGKSSIVCAICLGLGGKPKLLgRAKKV 60
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
332-532 |
3.78e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 332 ISIKKSKLEQYTQEHEACAEELKT-----------HDEGTAALKQSRAEKETIiRKEIEEYEA-LVKKREQIKKRLVTVE 399
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDAlqaeleelneeYNELQAELEALQAEIDKL-QAEIAEAEAeIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 400 -------------------------SAYTEIQSTMENTNKQRKKDKAQIEKNEKELEdlhklpeKNQREIEDCNKKLESL 454
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELE-------AKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24584683 455 EVSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQAETTESRKYETLKSSY 532
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
292-588 |
3.81e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 292 RCKLAEREmKDLEQPFNEAVDYLKKENElvRTKSFHIQKiisiKKSK-----LEQYTQEHEACAEELKThDEGTAALKQS 366
Cdd:pfam01576 63 RARLAARK-QELEEILHELESRLEEEEE--RSQQLQNEK----KKMQqhiqdLEEQLDEEEAARQKLQL-EKVTTEAKIK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 367 RAEKETIIRKEieEYEALVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEknekELEDLHKLPEKNQREIED 446
Cdd:pfam01576 135 KLEEDILLLED--QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMIS----DLEERLKKEEKGRQELEK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 447 CNKKLESlevSKVTLNEELEKQQAELTKTTAPLTEKRLKLSDELVGLKEkvntakgevqvfesqlkilkqaettesrkye 526
Cdd:pfam01576 209 AKRKLEG---ESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEE------------------------------- 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584683 527 tlkssyEQSQKSLEEKVTRvdELKESIPRMKTEIASKSAEVDKMVKEERNLSMQCNKLRTEI 588
Cdd:pfam01576 255 ------ETAQKNNALKKIR--ELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL 308
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1201-1264 |
3.87e-03 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 39.73 E-value: 3.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24584683 1201 KYISNLSGGEKTLSSLALVFAlhyyKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIV 1264
Cdd:cd03214 93 RPFNELSGGERQRVLLARALA----QEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVV 152
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
817-976 |
4.19e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 817 EIQTLKNGLQRDEAEYKRLAVSITSLEQQMASNLKQCEAQRQRmLKKTtdERAVKEREEQIEAAKQELEQAQFAEQAVSS 896
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDL--EKEIKRLELEIEEVEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 897 --QIEEIQNQYDTLRNEsVKPVEAKIKKVNSQIEKLAANVRSLNVGLATADRNITKITgnnNNLRENIKAAEEKLKSLNE 974
Cdd:COG1579 88 nkEYEALQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEA 163
|
..
gi 24584683 975 DR 976
Cdd:COG1579 164 ER 165
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
770-1053 |
4.24e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 770 TQVRTKTAESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQmASN 849
Cdd:COG4372 62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQ-IAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 850 LKQCEAQRQRMLKKTTDERAVKERE-EQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRNESVKPVEAKIKKVNSQIE 928
Cdd:COG4372 141 LQSEIAEREEELKELEEQLESLQEElAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEEL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 929 KLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSLNEDRNKAKEKKEELEKEIEESEASIEGAKSQSSDIK 1008
Cdd:COG4372 221 LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 24584683 1009 KEIDEITKEENKRNIERIEIDTKLQAAAGKMNKVKNDIPGWQAQL 1053
Cdd:COG4372 301 LLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| DUF4515 |
pfam14988 |
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ... |
384-468 |
4.42e-03 |
|
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.
Pssm-ID: 405647 [Multi-domain] Cd Length: 206 Bit Score: 40.14 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 384 LVKKREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQIEKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNE 463
Cdd:pfam14988 27 YVQECEEIERRRQELASRYTQQTAELQTQLLQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEKVRAETAEKDR 106
|
....*
gi 24584683 464 ELEKQ 468
Cdd:pfam14988 107 EAHLQ 111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
347-593 |
4.76e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 347 EACAEELKTHDEGTAALKQSRAEKEtiirKEIEEYEALVK---KREQIKKRLVTVESAYTEIQSTMENTNKQRKKDKAQI 423
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVE----ERLERAEDLVEaedRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 424 EKNEKELEDLHKLPEKNQREIEDCNKKLESLEVSKVTLNEELEKqqaelTKTTAPLTEKRLKLSDELVGLKEKVNTakge 503
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-----LERIRTLLAAIADAEDEIERLREKREA---- 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 504 vqvfesqlkilkQAETTESRKyETLKSSYEQsQKSLEEKV--TRVDELKESIPRMKTEIASKSAEVDKMVKEERNLSMQC 581
Cdd:PRK02224 618 ------------LAELNDERR-ERLAEKRER-KRELEAEFdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
250
....*....|..
gi 24584683 582 NKLRTEINERSS 593
Cdd:PRK02224 684 GAVENELEELEE 695
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
297-505 |
6.13e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 40.99 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 297 EREMKDLEQPFNEAVDYLKKENELVRTKSFHIQKIISIKKSKLEQYTQEHEACAEELKTHDEGTA---ALK----QSRAE 369
Cdd:PLN03229 514 EKLKDEFNKRLSRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEkmeALKaevaSSGAS 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 370 KETIIRKEIEeyEALVKKREQIKKRLVTV-ESAYTEIQSTmentnKQRKKDKAQIEKNEKELEDLHKLPEKNQREIE--- 445
Cdd:PLN03229 594 SGDELDDDLK--EKVEKMKKEIELELAGVlKSMGLEVIGV-----TKKNKDTAEQTPPPNLQEKIESLNEEINKKIErvi 666
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24584683 446 ---DCNKKLESL--EVSK------VTLNEELEKQQAELTKT------TAPLTEKRLKLSDELVGLKEKVNTAKGEVQ 505
Cdd:PLN03229 667 rssDLKSKIELLklEVAKasktpdVTEKEKIEALEQQIKQKiaealnSSELKEKFEELEAELAAARETAAESNGSLK 743
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
89-179 |
6.27e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 40.34 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 89 ISKIVNRNFKSYA-GEVELGPFhqsfTAIIGPNGSGKSNVIDSmmfVFGCRANRIRCkrvstlIHSSSSYPNLRSCSVAV 167
Cdd:COG4938 1 IKSISIKNFGPFKeAELELKPL----TLLIGPNGSGKSTLIQA---LLLLLQSNFIY------LPAERSGPARLYPSLVR 67
|
90
....*....|..
gi 24584683 168 HFKQIVDKGDGT 179
Cdd:COG4938 68 ELSDLGSRGEYT 79
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
757-1033 |
6.68e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.78 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 757 SGGGSRPIRGKMGTQVRTKTAESADSSQISQKALEDMQIQAEELQARVnycQEQQGSLEREIQTLKNGLQRDEAEYKRLA 836
Cdd:pfam05667 286 GSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQR---EEELEELQEQLEDLESSIQELEKEIKKLE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 837 VSItsleQQMASNLKQCEAQRQRmlkkTTDERAVKER--------EEQIEAAKQELEQAQFAEQAVSSQIEEIQ----NQ 904
Cdd:pfam05667 363 SSI----KQVEEELEELKEQNEE----LEKQYKVKKKtldllpdaEENIAKLQALVDASAQRLVELAGQWEKHRvpliEE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 905 YDTLRNESVKPvEAKIKKVNSQIEKLAANVRSLNVGLATADrnitkitgnnnnlrENIKAAEEKLKSLNEDrnkakekke 984
Cdd:pfam05667 435 YRALKEAKSNK-EDESQRKLEEIKELREKIKEVAEEAKQKE--------------ELYKQLVAEYERLPKD--------- 490
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 24584683 985 elekeieeseasiegaKSQSSDIKKeIDEITK--EENKRNIERIEIDTKLQ 1033
Cdd:pfam05667 491 ----------------VSRSAYTRR-ILEIVKniKKQKEEITKILSDTKSL 524
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
773-973 |
7.07e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.09 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 773 RTKTAESADSSQISQKALEDMQIQAEELQARVNYCQEQQGSLEREIQTLKNGLQRDEAEYKRLAVSITSLEQQMA----- 847
Cdd:pfam06008 32 LSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVAtlgen 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 848 ------SNLKQCEAQRQRMLKkttdERAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRN---ESVKPVEA 918
Cdd:pfam06008 112 dfalpsSDLSRMLAEAQRMLG----EIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANalrDSLAEYEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584683 919 KIKKVNSQIEKLAANVRSLNVGLATADRNIT-------KITGNNNNLRENIKAAEEKLKSLN 973
Cdd:pfam06008 188 KLSDLRELLREAAAKTRDANRLNLANQANLRefqrkkeEVSEQKNQLEETLKTARDSLDAAN 249
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
836-972 |
8.60e-03 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 38.41 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 836 AVSITSLEQQMASNLKQCEAQrQRMLKKTTDE--RAVKEREEQIEAAKQE---LEQAQFAEQAVSSQIEEIQNQYDTLRN 910
Cdd:pfam16535 17 EVSLSQLESRIAAWKAMQEAQ-QQKGLELSDEfqTALSEAEEATDAYEKAinkLKNAKSKAKAAEKKIDQAQTRLQSLAP 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24584683 911 ESVKPVEAKIKKVNSQIEKLAanvrslnvglATADRNITKITGNNNNLRENIKAAEEKLKSL 972
Cdd:pfam16535 96 DSPGKAKLEAAEQQAGIKKDA----------LQADRTLDKALDAASKLTTKAMAKEKEADDF 147
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
327-614 |
8.86e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.97 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 327 HIQKIISIKKSKLEQYTQEHEACAEELKT-----HDEGTAALKQSRAEKETIIRKEiEEYEALVKKREQIKKRLVTVESA 401
Cdd:PTZ00440 1028 LIDKLIKEKGKEIEEKVDQYISLLEKMKTklssfHFNIDIKKYKNPKIKEEIKLLE-EKVEALLKKIDENKNKLIEIKNK 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 402 YTEiqsTMENTNKQRKKDKAQIEKNEKELEDLHKlpeknqrEIEDCNKKLESLEVSKVTLNEELEKQqaeltkttapLTE 481
Cdd:PTZ00440 1107 SHE---HVVNADKEKNKQTEHYNKKKKSLEKIYK-------QMEKTLKELENMNLEDITLNEVNEIE----------IEY 1166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24584683 482 KRLKLSDELVGLKEKVNTAKGEVQVFESQLKILKQA-----ETTESRKYETLKSSYEQSQKSLEEKVTRVDelKESIPRM 556
Cdd:PTZ00440 1167 ERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVkknmsKERNDHLTTFEYNAYYDKATASYENIEELT--TEAKGLK 1244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 24584683 557 KTEIASKSAEVDKMVKEERNlsmqcNKLRTEINERSSVMQAQRSNNKVLDFLMRMKME 614
Cdd:PTZ00440 1245 GEANRSTNVDELKEIKLQVF-----SYLQQVIKENNKMENALHEIKNMYEFLISIDSE 1297
|
|
| |
