|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
951-1049 |
1.15e-49 |
|
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: 174.32 E-value: 1.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 951 NKAAFNDMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDLILKMADSQRFRQFILLTPQSMSSL 1030
Cdd:cd03276 100 NKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGL 179
|
90
....*....|....*....
gi 966979913 1031 PSSKLIRILRMSDPERGQT 1049
Cdd:cd03276 180 ASSDDVKVFRMKDPRGPRR 198
|
|
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
49-168 |
3.03e-45 |
|
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: 161.61 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMCHsMLGPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSLKGFVKDGQNSADISITLRNRG 128
Cdd:cd03276 1 IESITLKNFMCH-RHLQIEFGPRVNFIVGNNGSGKSAILTALTIGLGGKASDTNRGSSLKDLIKDGESSAKITVTLKNQG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 966979913 129 DDAfkasvygNSILIQqhiSIDGSRSYkLKSATGSVVSTK 168
Cdd:cd03276 80 LDA-------NPLCVL---SQDMARSF-LTSNKAAVRDVK 108
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
961-1046 |
1.20e-31 |
|
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: 122.03 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 961 LSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDLILKMADSqrFRQFILLTPQSMSSLPSSKLIRILR 1040
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKH--TSQFIVITLKKEMFENADKLIGVLF 172
|
....*.
gi 966979913 1041 MSDPER 1046
Cdd:cd03239 173 VHGVST 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
189-874 |
8.80e-27 |
|
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: 118.62 E-value: 8.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 189 QLEQMKEDYSYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSIaglstmKTNLESLKHEmawavVNEIEKQLNAIR 268
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL------QKELYALANE-----ISRLEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 269 DNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVAKKRAYNEAEVLYNRSLNEY 348
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 349 KALKKDDEQLCKRIEEL---KKSTDQSLEPERLERQKKISWLKE-RVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIKR 424
Cdd:TIGR02168 389 AQLELQIASLNNEIERLearLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 425 EESDVKHALSYNQRQLKELKdSKTDRLKRfgpnvpaLLEAIDDAYRQGLFTYKP-------VGPLGACIHLrDPELALAI 497
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQ-ARLDSLER-------LQENLEGFSEGVKALLKNqsglsgiLGVLSELISV-DEGYEAAI 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 498 ESCLKGLLQAYCCHNHADERVLQALMKR-------FYLPGTSRPQIIVSEFRNeiydvrhRAAYHPEFPTVLTALEIDNA 570
Cdd:TIGR02168 540 EAALGGRLQAVVVENLNAAKKAIAFLKQnelgrvtFLPLDSIKGTEIQGNDRE-------ILKNIEGFLGVAKDLVKFDP 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 571 VVANSLIDMRGieTVLLIKNnsVARAVMQSQKPPKNCReAFTAEGDQVFAG--RYYSSENTRPKFLSRDvdSEISDLENE 648
Cdd:TIGR02168 613 KLRKALSYLLG--GVLVVDD--LDNALELAKKLRPGYR-IVTLDGDLVRPGgvITGGSAKTNSSILERR--REIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 649 VENKMAQILNLQQHLSDLEK---------------------DIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEH 707
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKeleeleeeleqlrkeleelsrQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 708 QSVDIATLEDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKR 787
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 788 GKRHYEEKQKEHLDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKIQAEHASHGDREEIMR 867
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
....*..
gi 966979913 868 QYQEARE 874
Cdd:TIGR02168 926 QLELRLE 932
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
49-127 |
5.02e-22 |
|
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: 94.30 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMCHsMLGPFKFGSN-VNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSL---KGFVKDGQNSADISITL 124
Cdd:cd03239 1 IKQITLKNFKSY-RDETVVGGSNsFNAIVGPNGSGKSNIVDAICFVLGGKAAKLRRGSLLflaGGGVKAGINSASVEITF 79
|
...
gi 966979913 125 RNR 127
Cdd:cd03239 80 DKS 82
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
204-1023 |
9.72e-21 |
|
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: 98.99 E-value: 9.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 204 KERTKEQIHQGEERLTELKRQCVEKEERFQSIAG-LSTMKTNLESLKHEMAWAV---VNEIEKQLNAIRDNIKIGEDRAA 279
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQlLEELNKKIKDLGEEEQLRVkekIGELEAEIASLERSIAEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 280 RLDRKMEEQQVRLN----EAEQKYKDIQD---KLEKISEETNARAPECMALKADVvakkrayNEAEVLYNRSLNEYKALK 352
Cdd:TIGR02169 319 DAEERLAKLEAEIDkllaEIEELEREIEEerkRRDKLTEEYAELKEELEDLRAEL-------EEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 353 KDDEQLCKRIEELKKSTDQSLEPERLERQK-------------KISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEY 419
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEEladlnaaiagieaKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 420 GKIKREESDVKHALSYNQRQLKELKDSKTDRLKRFGPNVPAllEAIDDAYRQGLftYKPVGPLGACihlrDPELALAIES 499
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV--EEVLKASIQGV--HGTVAQLGSV----GERYATAIEV 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 500 CLKGLLQAYCCHNHAD-ERVLQALMKRFYLPGTSRPQIIVSEFRNEI-----------------YDVRHRAAYHPEFPTV 561
Cdd:TIGR02169 544 AAGNRLNNVVVEDDAVaKEAIELLKRRKAGRATFLPLNKMRDERRDLsilsedgvigfavdlveFDPKYEPAFKYVFGDT 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 562 LTALEIDNA---------------------------------------------VVANSLIDMRGIETVLLIKNNSVARA 596
Cdd:TIGR02169 624 LVVEDIEAArrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepaelqRLRERLEGLKRELSSLQSELRRIENR 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 597 VMQSQKPPKNC-REAFTAEGDQVFAGRYYSSENTRPKFLSRD----------VDSEISDLENEVENKMAQILNLQQHLSD 665
Cdd:TIGR02169 704 LDELSQELSDAsRKIGEIEKEIEQLEQEEEKLKERLEELEEDlssleqeienVKSELKELEARIEELEEDLHKLEEALND 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 666 LEKDIkrNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLEDEAQENKSKMKMVEKHMEQQKENMEHLKS 745
Cdd:TIGR02169 784 LEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 746 LKIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKRGKRHYE---EKQKEHLDTLNKKKRELDMKEKELEEKMS 822
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqiEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 823 QARQICPERIEVEKsasiLDKEINRLRQKIQAehashgdREEI-MR---QYQEARETYLDLDNKVRTLKKFIKLLGEimd 898
Cdd:TIGR02169 942 EDEEIPEEELSLED----VQAELQRVEEEIRA-------LEPVnMLaiqEYEEVLKRLDELKEKRAKLEEERKAILE--- 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 899 hRFKTYQQFRRCLTLRCklyFDNLLSQRAYC--------GKMNFDHKNETLS----ISVQPGEgnkAAFNDMRALSGGER 966
Cdd:TIGR02169 1008 -RIEEYEKKKREVFMEA---FEAINENFNEIfaelsggtGELILENPDDPFAggleLSAKPKG---KPVQRLEAMSGGEK 1080
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 966979913 967 SFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDLILKMADSQrfrQFILLT 1023
Cdd:TIGR02169 1081 SLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEA---QFIVVS 1134
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
961-1043 |
2.35e-19 |
|
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: 86.26 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 961 LSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDLILKMADSQrfRQFILLTPQSMSSLPSSKLIRILR 1040
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG--AQVIVITHLPELAELADKLIHIKK 155
|
...
gi 966979913 1041 MSD 1043
Cdd:cd03227 156 VIT 158
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
66-897 |
1.34e-15 |
|
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: 82.03 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 66 FKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSLKGFVKDG------QNSADISITLRNrgDDAFKASVYGN 139
Cdd:TIGR02168 19 INFDKGITGIVGPNGCGKSNIVDAIRWVLGEQSAKALRGGKMEDVIFNGsetrkpLSLAEVELVFDN--SDGLLPGADYS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 140 SILIQQHISIDGSRSY-------KLK--------SATGS-------------VVSTKKEELIAILdhfniqffmkatqle 191
Cdd:TIGR02168 97 EISITRRLYRDGESEYfingqpcRLKdiqdlfldTGLGKrsysiieqgkiseIIEAKPEERRAIF--------------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 192 qmkEDYSYIMETKERTKEqihqgeerlTELKrqcvekeerfqsiagLSTMKTNLESLKhemawAVVNEIEKQLNAIRDNI 271
Cdd:TIGR02168 162 ---EEAAGISKYKERRKE---------TERK---------------LERTRENLDRLE-----DILNELERQLKSLERQA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 272 KIGEdRAARLDRKMEEQQV-----RLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVAKKRAYNEAEVLYNRSLN 346
Cdd:TIGR02168 210 EKAE-RYKELKAELRELELallvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 347 EYKALKKDDEQLCKRIEELKKSTDQSL-EPERLERQ-------------------KKISWLKERVKALRNQENSVNQEIE 406
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLErQLEELEAQleeleskldelaeelaeleEKLEELKEELESLEAELEELEAELE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 407 QFQQAIEKDKEEYGKIKREESDVKHALSYNQRQLKELKDSKTD---RLKRFGPNVPALL--------------------- 462
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERledRRERLQQEIEELLkkleeaelkelqaeleeleee 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 463 --------------------------EAIDDAYRQ-------------------GLFTYK------------PVGPLGAC 485
Cdd:TIGR02168 449 leelqeelerleealeelreeleeaeQALDAAERElaqlqarldslerlqenleGFSEGVkallknqsglsgILGVLSEL 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 486 IHLrDPELALAIESCLKGLLQAYCCHNHADERVLQALMKR-------FYLPGTSRPQIIVSEFRNeiydvrhRAAYHPEF 558
Cdd:TIGR02168 529 ISV-DEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQnelgrvtFLPLDSIKGTEIQGNDRE-------ILKNIEGF 600
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 559 PTVLTALEIDNAVVANSLIDMRGieTVLLIKNnsVARAVMQSQKPPKNCReAFTAEGDQVFAG--RYYSSENTRPKFLSR 636
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALSYLLG--GVLVVDD--LDNALELAKKLRPGYR-IVTLDGDLVRPGgvITGGSAKTNSSILER 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 637 dvDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLE 716
Cdd:TIGR02168 676 --RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 717 DEAQEnkskmkmVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKRGKRHYEEKQ 796
Cdd:TIGR02168 754 KELTE-------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 797 KEHLDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLrQKIQAEHASHgdREEIMRQYQEARETY 876
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL-LNERASLEEA--LALLRSELEELSEEL 903
|
970 980
....*....|....*....|.
gi 966979913 877 LDLDNKVRTLKKFIKLLGEIM 897
Cdd:TIGR02168 904 RELESKRSELRRELEELREKL 924
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
962-1039 |
2.60e-14 |
|
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: 73.01 E-value: 2.60e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966979913 962 SGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDLILKMADSQRFRQFILLTPQSMSSLPSSKLIRIL 1039
Cdd:cd03277 128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITPKLLPGLNYHEKMTVL 205
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
47-130 |
1.22e-13 |
|
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: 71.09 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 47 GIIESIHLKNFMCHSMLgPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSLKGFVKDGQNSADISITLRN 126
Cdd:cd03277 1 GSIVRIKLENFVTYDET-EFRPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPKLLGRAKKVGEFVKRGCDEGTIEIELYG 79
|
....
gi 966979913 127 RGDD 130
Cdd:cd03277 80 NPGN 83
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
49-891 |
3.69e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMCHSmLGPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSLKGFVKDGQNSADISITLRNRG 128
Cdd:PRK03918 3 IEELKIKNFRSHK-SSVVEFDDGINLIIGQNGSGKSSILEAILVGLYWGHGSKPKGLKKDDFTRIGGSGTEIELKFEKNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 129 DD--AFKASVYGNSILIQQHISidgsrsykLKSATGSVVSTKKEELIAILDHFNIQFFMKATQLEQMKEDysyiMETKER 206
Cdd:PRK03918 82 RKyrIVRSFNRGESYLKYLDGS--------EVLEEGDSSVREWVERLIPYHVFLNAIYIRQGEIDAILES----DESREK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 207 TKEQIhqgeerltelkrqcvekeerfqsiaglstmkTNLEslKHEMAWAVVNEIEKQLNAIRDNIKIGEDRAARLDRKME 286
Cdd:PRK03918 150 VVRQI-------------------------------LGLD--DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 287 EQQVRLNEAEQKYKDIQDKLEKISEEtnarapecmalkadVVAKKRAYNEAEVLYNRsLNEYKALKKDDEQLCKRIEELK 366
Cdd:PRK03918 197 EKEKELEEVLREINEISSELPELREE--------------LEKLEKEVKELEELKEE-IEELEKELESLEGSKRKLEEKI 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 367 KSTDQSLEperlERQKKISWLKERVKALRNQENSVnQEIEQFQQAIEKDKEEYGKIKREESDVKHALSYNQRQLKELkDS 446
Cdd:PRK03918 262 RELEERIE----ELKKEIEELEEKVKELKELKEKA-EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL-EE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 447 KTDRLKRfgpnVPALLEAIDDAYRQglftykpvgplgacihlrdpelalaiescLKGLLQAYcchnhADERVLQALMKRF 526
Cdd:PRK03918 336 KEERLEE----LKKKLKELEKRLEE-----------------------------LEERHELY-----EEAKAKKEELERL 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 527 YLPGTSRPqiiVSEFRNEIYDVRHRaayhpefptvltALEIDNAVvaNSLIDMRGietVLLIKNNSVARAVMQSQKppkn 606
Cdd:PRK03918 378 KKRLTGLT---PEKLEKELEELEKA------------KEEIEEEI--SKITARIG---ELKKEIKELKKAIEELKK---- 433
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 607 creaftAEGDQVFAGRYYSSENTrpKFLSRDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQL--HY 684
Cdd:PRK03918 434 ------AKGKCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQL 505
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 685 KELEMKIRKSNSEirELENIEEhqsvDIATLEDEAQENKSKMKMVEKHMEQQKEnmehLKSLKIEAENKYDAIKlkinql 764
Cdd:PRK03918 506 KELEEKLKKYNLE--ELEKKAE----EYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELE------ 569
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 765 SELADPLKDELNLADSEVDNQKRGKRHYEEKQKEHLdTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKE 844
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 966979913 845 INRLRQKIQAEhashgDREEIMRQYQEARETYLDLDNKVRTLKKFIK 891
Cdd:PRK03918 649 LEELEKKYSEE-----EYEELREEYLELSRELAGLRAELEELEKRRE 690
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
68-1007 |
1.49e-12 |
|
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: 72.31 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 68 FGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSLKGFV----KDGQNSADISITLRNRGDDAFkasVYGNSILI 143
Cdd:pfam02463 21 FSPGFTAIVGPNGSGKSNILDAILFVLGERSAKSLRSERLSDLIhsksGAFVNSAEVEITFDNEDHELP---IDKEEVSI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 144 QQHISIDGSRSYKL--KSATGSVVSTKKEELIAILDHFNIQFFMKA-TQLEQMKEDYSYIMET-----------KERTKE 209
Cdd:pfam02463 98 RRRVYRGGDSEYYIngKNVTKKEVAELLESQGISPEAYNFLVQGGKiEIIAMMKPERRLEIEEeaagsrlkrkkKEALKK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 210 QIH-----------------------------------QGEERLTELKRQCVEKEERFQSIAGLSTMKTNLESLKHEMAW 254
Cdd:pfam02463 178 LIEetenlaeliidleelklqelklkeqakkaleyyqlKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 255 A---VVNEIEKQLNAIRDN----IKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADV 327
Cdd:pfam02463 258 QeieKEEEKLAQVLKENKEeekeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 328 VAKKRAYNEAEVLYNRSLNEYKALKKDDEQLCKRIEELKKStdQSLEPERLERQKKISWLKERVKALRNQENSVNQEIEQ 407
Cdd:pfam02463 338 EELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAK--KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 408 FQQAIEKDKEEYGKIKREEsdVKHALSYNQRQLKELKDSKTDRLKRFGPNVPALLEAIDDAYR----------------- 470
Cdd:pfam02463 416 QLEDLLKEEKKEELEILEE--EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKEtqlvklqeqlelllsrq 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 471 -------------------QGLFTYKPVGPLGACIHLR-DPELALAIESCLKGLLQAYCCHNHADERVLQALMKRFYLP- 529
Cdd:pfam02463 494 kleersqkeskarsglkvlLALIKDGVGGRIISAHGRLgDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEl 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 530 -------GTSRPQIIVSEFRNEIYDVRHRAAYHPEFPTVLTALEIDNAVVANSLIDMRGIETVL----------LIKNNS 592
Cdd:pfam02463 574 plgarklRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLkesakakesgLRKGVS 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 593 VARAVMQSQKPPKNCREAFTAEGDQVFAGRYYSSENTRPKFLSRDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKR 672
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 673 NEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLEDEAQENKSKMKMVEKH-------------MEQQKEN 739
Cdd:pfam02463 734 INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEeklkaqeeelralEEELKEE 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 740 MEHLKSL---------KIEAENKYDAIKLKINQLSELADPLKDELNLADSEVD---NQKRGKRHYEEKQKEHLDTLNK-- 805
Cdd:pfam02463 814 AELLEEEqllieqeekIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEellQELLLKEEELEEQKLKDELESKee 893
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 806 -KKRELDMKEKELEEKMSQARQICPERIEVEKSASILDK--------------------------EINRLRQKIQAEHAS 858
Cdd:pfam02463 894 kEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKyeeepeellleeadekekeennkeeeEERNKRLLLAKEELG 973
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 859 HGDREEIMRQYQEARETYLDLDNKVRTLKKFIKLLGEIMD----HRFKTYQQFRRCLTLRCKLYFDNLLSQRAYCGKMNF 934
Cdd:pfam02463 974 KVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEetcqRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDP 1053
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966979913 935 DHK-NETLSISVQPGegnKAAFNDMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDLI 1007
Cdd:pfam02463 1054 DDPfSGGIEISARPP---GKGVKNLDLLSGGEKTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLL 1124
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
636-902 |
3.79e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 636 RDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATL 715
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 716 EDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQ-------LSELADPLKDELNLADSEVDNQKRG 788
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaeealleAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 789 KRHYEEKQKEHLDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKIQAEHASHGDREEIMRQ 868
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270
....*....|....*....|....*....|....
gi 966979913 869 YQEARETYLDLDNKVRTLKKFIKLLGEIMDHRFK 902
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
634-854 |
1.06e-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: 69.28 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 634 LSRDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIA 713
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 714 TLEDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKRGKRHYE 793
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966979913 794 EKQKEHLDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKIQA 854
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
636-888 |
1.68e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 636 RDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATL 715
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 716 EDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKI-NQLSELADPLKDELNLADSEVDNQKRGKRHyEE 794
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELlEALRAAAELAAQLEELEEAEEALLERLERL-EE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 795 KQKEHLDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKIQAEHASHGDREEIMRQYQEARE 874
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
250
....*....|....
gi 966979913 875 TYLDLDNKVRTLKK 888
Cdd:COG1196 502 DYEGFLEGVKAALL 515
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
51-124 |
3.64e-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: 62.76 E-value: 3.64e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966979913 51 SIHLKNFMCHsMLGPFKFGS--NVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSslkgFVKDGQNSADISITL 124
Cdd:cd03227 1 KIVLGRFPSY-FVPNDVTFGegSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRS----GVKAGCIVAAVSAEL 71
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
636-855 |
4.25e-10 |
|
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: 62.86 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 636 RDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATL 715
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 716 EDEAQENKS----KMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKRGKRH 791
Cdd:COG4942 110 LRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966979913 792 YEEKQKEHLDTLNKKKRELDMKEKELEEKMSQARQicperieveksasiLDKEINRLRQKIQAE 855
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEE--------------LEALIARLEAEAAAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-750 |
4.90e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 189 QLEQMKEDYSYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSiaglstMKTNLESLKHEMAwavvnEIEKQLNAIR 268
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE------AQAEEYELLAELA-----RLEQDIARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 269 DNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNarapecmALKADVVAKKRAYNEAEVLYNRSLNEY 348
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 349 KALKKDDEQLCKRIEELKKSTdQSLEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIKREESD 428
Cdd:COG1196 382 EELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 429 VKHALSYNQRQLKELKDSKTDRLKRFGPNVP---ALLEAIDDA--------YRQGLFTYKPVGPLGACIHLRDPELALAI 497
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAArllLLLEAEADYegflegvkAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 498 ESCLKGLLQAYCCHNHADERVLQALMKRFYLPGTSRPQIIVSEFRNEIYDVRHRAAYHPEFPTVLTALEIDNAVVANSLI 577
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 578 DMRGIETVLLIKNNSVARAVmqsqkppkncreafTAEGDQVFAGRYYSSENTRPKFLSRDVDSEISDLENEVENKMAQIL 657
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAV--------------TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 658 NLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLEDEAQENKSKMKMVEKHMEQQK 737
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE 766
|
570
....*....|...
gi 966979913 738 ENMEHLKSlKIEA 750
Cdd:COG1196 767 RELERLER-EIEA 778
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
52-224 |
1.10e-09 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 59.05 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 52 IHLKNFMCHSmLGPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSlKGFVKD-------GQNSADISITL 124
Cdd:pfam13476 1 LTIENFRSFR-DQTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSG-GGFVKGdirigleGKGKAYVEITF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 125 RNRGDdafkasVYGNSILIQQHISIDGSRSYKLKSATGSVVSTKKEELIAILDHFNIQF-------------FMKATQLE 191
Cdd:pfam13476 79 ENNDG------RYTYAIERSRELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILpllvflgqereeeFERKEKKE 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 966979913 192 QMKEDYSYIMETKE-----RTKEQIHQGEERLTELKRQ 224
Cdd:pfam13476 153 RLEELEKALEEKEDekkllEKLLQLKEKKKELEELKEE 190
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
641-898 |
2.31e-09 |
|
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: 61.61 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 641 EISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLEDEAQ 720
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 721 ENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKRGkrhyEEKQKEHL 800
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR----LEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 801 DTLNKKKRELDMKEKELEEKMSQARqicpERIE-VEKSASILDKEINRLRQKIQ--AEHASHGDREEIMRQYQEARETYL 877
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLE----ARLErLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELEELQEELE 457
|
250 260
....*....|....*....|.
gi 966979913 878 DLDNKVRTLKKFIKLLGEIMD 898
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALD 478
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
636-826 |
2.41e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 636 RDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLkrcqlhyKELEMKIRKSNSEIRELENIEEHQSVDIATL 715
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-------EALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 716 EDEAQENK-------------------SKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELN 776
Cdd:COG3883 92 ARALYRSGgsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 966979913 777 LADSEVDNQKRGKRHYEEKQKEHLDTLNKKKRELDMKEKELEEKMSQARQ 826
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
189-417 |
7.39e-09 |
|
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: 60.07 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 189 QLEQMKEDYSYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSIAG-LSTMKTNLESLKHEMA--WAVVNEIEKQLN 265
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEqIEELSEDIESLAAEIEelEELIEELESELE 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 266 AIRDNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVA-KKRAYNEAEVLYNRS 344
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEA 956
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966979913 345 LNEYKALKKDDEQLCKRIEELKKSTDQsLEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEK-DKE 417
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKE-LGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEiDRE 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-467 |
7.52e-09 |
|
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: 60.07 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 147 ISIDGSRSYKLKSATGSVVSTKKE---------ELIAILDHFNIQFFMKATQLEQMKEDYSYIMETKERTKEQIHQGEER 217
Cdd:TIGR02168 655 VRPGGVITGGSAKTNSSILERRREieeleekieELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 218 LTELKRQC-----------VEKEERFQSIAGLSTMKTNLESLKHEMAW------AVVNEIEKQLNAIRDNIKIGEDRAAR 280
Cdd:TIGR02168 735 LARLEAEVeqleeriaqlsKELTELEAEIEELEERLEEAEEELAEAEAeieeleAQIEQLKEELKALREALDELRAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 281 LDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVAKKRAYNEAEVLYNRSLNEYKALKKDDEQLCK 360
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 361 RIEELKKsTDQSLEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAI-EKDKEEYGKIKREESDVKHALSYNQRQ 439
Cdd:TIGR02168 895 ELEELSE-ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEEARRR 973
|
330 340
....*....|....*....|....*....
gi 966979913 440 LKELKDSktdrLKRFGP-NvpalLEAIDD 467
Cdd:TIGR02168 974 LKRLENK----IKELGPvN----LAAIEE 994
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
667-875 |
1.31e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 667 EKDIKRNEELLkrcqLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLEDEAQENKSKMKMVEKHMEQQKENMEHLKSL 746
Cdd:COG1196 221 ELKELEAELLL----LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 747 KIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKRGKRHYEEKQKEHLDTLNKKKRELDMKEKELEEKMSQARQ 826
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 966979913 827 ICPERIEVEKSASILDKEINRLRQKIQAEHASHGDREEIMRQYQEARET 875
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
636-888 |
2.07e-08 |
|
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: 58.49 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 636 RDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATL 715
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 716 EDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKRGKrhyeEK 795
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL----NK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 796 QKEHLDTLNKKKrELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKIQAEHAShgdREEIMRQYQEARET 875
Cdd:TIGR04523 550 DDFELKKENLEK-EIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKK---ISSLEKELEKAKKE 625
|
250
....*....|...
gi 966979913 876 YLDLDNKVRTLKK 888
Cdd:TIGR04523 626 NEKLSSIIKNIKS 638
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
48-243 |
3.41e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 55.02 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 48 IIESIHLKNFMCHSMLGPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSlkGFVKDGQNSADISITLRNR 127
Cdd:COG0419 1 KLLRLRLENFRSYRDTETIDFDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRS--DLINVGSEEASVELEFEHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 128 GddafkasvygnsiliqqhisidgsRSYKLK---SATGSVVSTKKEELIAILDH-FNIQFFMKAtqleqmkedysyimet 203
Cdd:COG0419 79 G------------------------KRYRIErrqGEFAEFLEAKPSERKEALKRlLGLEIYEEL---------------- 118
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 966979913 204 KERTKEQIHQGEERLTELKRQCVEKEERFQSIAGLSTMKT 243
Cdd:COG0419 119 KERLKELEEALESALEELAELQKLKQEILAQLSGLDPIET 158
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
647-891 |
1.03e-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: 55.54 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 647 NEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENieehqsvDIATLEDEAQENKSKM 726
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-------ELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 727 KMVEKHMEQQKENMEHLkslkieaenkydaikLKINQLSELADPLKDELNlADSEVDNQKRGK--RHYEEKQKEHLDTLN 804
Cdd:COG4942 93 AELRAELEAQKEELAEL---------------LRALYRLGRQPPLALLLS-PEDFLDAVRRLQylKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 805 KKKRELDMKEKELEEKMSQARQIcpeRIEVEKSASILDKEINRlRQKIQAEHAShgDREEIMRQYQEARETYLDLDNKVR 884
Cdd:COG4942 157 ADLAELAALRAELEAERAELEAL---LAELEEERAALEALKAE-RQKLLARLEK--ELAELAAELAELQQEAEELEALIA 230
|
....*..
gi 966979913 885 TLKKFIK 891
Cdd:COG4942 231 RLEAEAA 237
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
632-888 |
1.33e-07 |
|
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: 55.84 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 632 KFLSRDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQ--- 708
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvke 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 709 -----SVDIATLEDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELNLADS--- 780
Cdd:TIGR02169 295 kigelEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAele 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 781 EVDNQKRGKRHYEEKQKEHLDTLNKK----KRELDMKEKELEEKMSQARQICPE--RIEVEKSASI-----LDKEINRLR 849
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREinelKRELDRLQEELQRLSEELADLNAAiaGIEAKINELEeekedKALEIKKQE 454
|
250 260 270
....*....|....*....|....*....|....*....
gi 966979913 850 QKIQAEHAshgDREEIMRQYQEARETYLDLDNKVRTLKK 888
Cdd:TIGR02169 455 WKLEQLAA---DLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
49-452 |
2.44e-07 |
|
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: 55.07 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMCHSMLGPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSL-----KGFVKDGQNSADISIT 123
Cdd:TIGR02169 2 IERIELENFKSFGKKKVIPFSKGFTVISGPNGSGKSNIGDAILFALGLSSSKAMRAERLsdlisNGKNGQSGNEAYVTVT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 124 LRNrgddafKASVYGNSILIQQHISIDGSRSYKLKSATGSVVStkKEELIAILDHFNIQFfmkatqleqmkEDYSYIMet 203
Cdd:TIGR02169 82 FKN------DDGKFPDELEVVRRLKVTDDGKYSYYYLNGQRVR--LSEIHDFLAAAGIYP-----------EGYNVVL-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 204 kertkeqihQGEerLTE-LKRQCVEKEERFQSIAGLSTMKTNLESLKHEMAwavvnEIEKQLNAIRDNIKIGEDRAARLD 282
Cdd:TIGR02169 141 ---------QGD--VTDfISMSPVERRKIIDEIAGVAEFDRKKEKALEELE-----EVEENIERLDLIIDEKRQQLERLR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 283 RKMEEQQvrlneaeqKYKDIQDKLEKIseETNARAPECMALKADVVAKKRAYNEAEVLYNRSLNEYKALKKDDEQLCKRI 362
Cdd:TIGR02169 205 REREKAE--------RYQALLKEKREY--EGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 363 EELKKSTDQSLEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIKREesdvKHALSYNQRQLKE 442
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE----IEELEREIEEERK 350
|
410
....*....|
gi 966979913 443 LKDSKTDRLK 452
Cdd:TIGR02169 351 RRDKLTEEYA 360
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
632-893 |
5.63e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 632 KFLSR--DVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRcqlhYKELEMKIRKSNSEIRELENieehqs 709
Cdd:PRK03918 183 KFIKRteNIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEELEKELESLEG------ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 710 vDIATLEDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADpLKDELNLADSEVDNQKRGK 789
Cdd:PRK03918 253 -SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 790 RHYEEKqKEHLDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEK-SASILDKEINRLRQKIQ-AEHAshgdREEIMR 867
Cdd:PRK03918 331 KELEEK-EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEeLEKA----KEEIEE 405
|
250 260
....*....|....*....|....*.
gi 966979913 868 QYQEARETYLDLDNKVRTLKKFIKLL 893
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEEL 431
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
637-819 |
5.90e-07 |
|
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: 53.87 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 637 DVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLE 716
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 717 DEAQENKSKMKMVEKhmeqqKENMEHLKSLKIEAEN-KYDAIKLKINQLSELADPLKDELNLADSEVDNQKRGKRHYEEK 795
Cdd:TIGR04523 180 KEKLNIQKNIDKIKN-----KLLKLELLLSNLKKKIqKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
170 180
....*....|....*....|....
gi 966979913 796 QKEHLDTLNKKKRELDMKEKELEE 819
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQ 278
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
249-444 |
7.26e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 249 KHEMAWAVVNEIEKQLNAIRDNikigEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAP--ECMALKAD 326
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 327 VVAKKRAYNEAEvlynRSLNEYKALKKDDEQLCKRIEELKKSTDQSLEPERLERQKKISWLKERVKALRNQENSVNQEIE 406
Cdd:COG4717 141 LAELPERLEELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190
....*....|....*....|....*....|....*...
gi 966979913 407 QFQQAIEKDKEEYGKIKREesdvkHALSYNQRQLKELK 444
Cdd:COG4717 217 EAQEELEELEEELEQLENE-----LEAAALEERLKEAR 249
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
48-433 |
1.09e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 48 IIESIHLKNFMCHSMLGPFkFGSNVNFVVGNNGSGKSAVLTALIVGLGGravaTNRGSSLKGFVKDGQNSADISITLRNR 127
Cdd:PRK01156 2 IIKRIRLKNFLSHDDSEIE-FDTGINIITGKNGAGKSSIVDAIRFALFT----DKRTEKIEDMIKKGKNNLEVELEFRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 128 GDDAFKASVY---GNSILIQQHISIDGSRSYKLKSATGSVVstKKEELIAILDHFNIQFFMKATQLE--------QMKED 196
Cdd:PRK01156 77 GHVYQIRRSIerrGKGSRREAYIKKDGSIIAEGFDDTTKYI--EKNILGISKDVFLNSIFVGQGEMDslisgdpaQRKKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 197 YSYIMETK--ERTKEQIHQGEERLT-----------ELKRQCVEKEERFQSIAGLSTMKTNLESLKHEMAwAVVNEIEKQ 263
Cdd:PRK01156 155 LDEILEINslERNYDKLKDVIDMLRaeisnidyleeKLKSSNLELENIKKQIADDEKSHSITLKEIERLS-IEYNNAMDD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 264 ---LNAIRDNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARapecmalkadVVAKKRAYNEAEVL 340
Cdd:PRK01156 234 ynnLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDP----------VYKNRNYINDYFKY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 341 YNRSLNEYKALKKDDEQLCKRIEELKKSTD-QSLEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEY 419
Cdd:PRK01156 304 KNDIENKKQILSNIDAEINKYHAIIKKLSVlQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYS 383
|
410
....*....|....
gi 966979913 420 GKIKREESDVKHAL 433
Cdd:PRK01156 384 KNIERMSAFISEIL 397
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
49-145 |
2.62e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.53 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMCHSMLGPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNR-GSSLKGFVKDGQNSADISITLRNR 127
Cdd:cd03240 1 IDKLSIRNIRSFHERSEIEFFSPLTLIVGQNGAGKTTIIEALKYALTGELPPNSKgGAHDPKLIREGEVRAQVKLAFENA 80
|
90 100
....*....|....*....|..
gi 966979913 128 GDDAFKA----SVYGNSILIQQ 145
Cdd:cd03240 81 NGKKYTItrslAILENVIFCHQ 102
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
257-425 |
2.96e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 257 VNEIEKQLNAIR---------DNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNA--RAPECMALKA 325
Cdd:COG3206 191 LEEAEAALEEFRqknglvdlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 326 DVVAKKRAYNEAEVLYNRSLNEYKALKKddeqlckRIEELKKSTDQSLEPERLERQKKISWLKERVKALRNQENSVNQEI 405
Cdd:COG3206 271 QLAELEAELAELSARYTPNHPDVIALRA-------QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL 343
|
170 180
....*....|....*....|
gi 966979913 406 EQFQQAiekdKEEYGKIKRE 425
Cdd:COG3206 344 AELPEL----EAELRRLERE 359
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
640-888 |
5.18e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 640 SEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRC---QLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLE 716
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIselKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 717 DEAQENKS----KMKMVEKHMEQQKENMEHLKSLKIE----------------------AENKYDAIKLKINQLSELADP 770
Cdd:TIGR04523 260 DEQNKIKKqlseKQKELEQNNKKIKELEKQLNQLKSEisdlnnqkeqdwnkelkselknQEKKLEEIQNQISQNNKIISQ 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 771 LKDELN-----LADSEVDNQKRgKRHYEEKQKEhldtLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEI 845
Cdd:TIGR04523 340 LNEQISqlkkeLTNSESENSEK-QRELEEKQNE----IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 966979913 846 NRLRQkiqaehashgDREEIMRQYQEARETYLDLDNKVRTLKK 888
Cdd:TIGR04523 415 KKLQQ----------EKELLEKEIERLKETIIKNNSEIKDLTN 447
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-897 |
5.26e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 685 KELEMKIRKSNSEIRELENIEEHqsvdIATLEDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEaenkYDAIKLKINQL 764
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEEL----IKEKEKELEEVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 765 SELADPLKDELnladSEVDNQKRGKRHYEEKQKEHLDTLNKKKRELdmkeKELEEKMSQARQICPERIEVEKSASILDKE 844
Cdd:PRK03918 244 EKELESLEGSK----RKLEEKIRELEERIEELKKEIEELEEKVKEL----KELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 966979913 845 INRLRQKIQAEHASHGDREEIMRQYQEARETYLDLDNKVRTLKKFIKLLGEIM 897
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK 368
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
625-820 |
5.98e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 625 SSENTRPKFLSRDVDSEISDLENEVENKMAQILNLQQHLSDLEkdiKRNEELLKRCQLHY-------KELEMKIRKSNSE 697
Cdd:PHA02562 166 SEMDKLNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR---KKNGENIARKQNKYdelveeaKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 698 IRELENIEEHQSVDIATLEDEAQENKSKM-------KMVEKH---------MEQQKENMEHLKSLKIEAENKYDAIKLKI 761
Cdd:PHA02562 243 LLNLVMDIEDPSAALNKLNTAAAKIKSKIeqfqkviKMYEKGgvcptctqqISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966979913 762 NQLSELAD----------PLKDELNLAD----SEVDNQKRGKRHYEEKQKEH------LDTLNKKKRELDMKEKELEEK 820
Cdd:PHA02562 323 DELEEIMDefneqskkllELKNKISTNKqsliTLVDKAKKVKAAIEELQAEFvdnaeeLAKLQDELDKIVKTKSELVKE 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
636-763 |
1.01e-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: 48.00 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 636 RDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIR--KSNSEIRELENIEEHQSVDIA 713
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNKEYEALQKEIESLKRRIS 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 966979913 714 TLEDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQ 763
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
636-893 |
1.29e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 636 RDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATL 715
Cdd:TIGR00606 839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 716 EDEAQENKSKMKmvEKHMEQQKENMEhLKSLKIEAENKYDAIKLKINQLSELADPLK----DELN-LADSEVDNQKRGKR 790
Cdd:TIGR00606 919 EKDQQEKEELIS--SKETSNKKAQDK-VNDIKEKVKNIHGYMKDIENKIQDGKDDYLkqkeTELNtVNAQLEECEKHQEK 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 791 HYEE-----------KQKEHL--DTLNKKKRELDMKEKElEEKMSQARQICPERIEVEKSA-SILDKEINRL-------- 848
Cdd:TIGR00606 996 INEDmrlmrqdidtqKIQERWlqDNLTLRKRENELKEVE-EELKQHLKEMGQMQVLQMKQEhQKLEENIDLIkrnhvlal 1074
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 966979913 849 -RQKIQAEHASHGDREEIMRQYQEARETYLDLDNKVRTLKKFIKLL 893
Cdd:TIGR00606 1075 gRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
188-909 |
2.09e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 188 TQLEQMKEDYSYIMETK---ERTKEQIhqgeERLTELKRQCVEKEERFQSIAGLSTMKTNLESLKHEMAwavVNEIEKQL 264
Cdd:COG4913 225 EAADALVEHFDDLERAHealEDAREQI----ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR---LELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 265 NAIRDNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQ-DKLEkiseetnarapecmALKADVVAKKRAYNEAEvlynR 343
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLE--------------QLEREIERLERELEERE----R 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 344 SLNEYkalkkddEQLCKRIEElkkstDQSLEPERLERQKKIswLKERVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIK 423
Cdd:COG4913 360 RRARL-------EALLAALGL-----PLPASAEEFAALRAE--AAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 424 REesdvkhalsynqrqLKELKDSKTdrlkrfgpNVPALLEAIDDAYRQGL-FTYKPVGPLGACIHLRDPELA--LAIESC 500
Cdd:COG4913 426 AE--------------IASLERRKS--------NIPARLLALRDALAEALgLDEAELPFVGELIEVRPEEERwrGAIERV 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 501 LkgllqayccHNHA-----DERVLQAlmkrfylpgtsrpqiiVSEFRNEiYDVRHRAAYHpEFPTVLTALEIDnAVVANS 575
Cdd:COG4913 484 L---------GGFAltllvPPEHYAA----------------ALRWVNR-LHLRGRLVYE-RVRTGLPDPERP-RLDPDS 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 576 LIDmrgietVLLIKNNSVARAVMQ------------SQKPPKNCREAFTAEGdQVFAGRYYSSENTRPKFLSR-----DV 638
Cdd:COG4913 536 LAG------KLDFKPHPFRAWLEAelgrrfdyvcvdSPEELRRHPRAITRAG-QVKGNGTRHEKDDRRRIRSRyvlgfDN 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 639 DSEISDLEnevenkmAQILNLQQHLSDLEKDIKRNEELLKRCQLHyKELEMKIRKSNSEIRELENIEEHqsvdIATLEDE 718
Cdd:COG4913 609 RAKLAALE-------AELAELEEELAEAEERLEALEAELDALQER-REALQRLAEYSWDEIDVASAERE----IAELEAE 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 719 ---AQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELNLADsevdnqKRGKRHYEEK 795
Cdd:COG4913 677 lerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE------DLARLELRAL 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 796 QKEHLDTLNKKKRELDMKEkELEEKMSQARqicperieveksasildKEINRLRQKIqaehashgdrEEIMRQYQEA-RE 874
Cdd:COG4913 751 LEERFAAALGDAVERELRE-NLEERIDALR-----------------ARLNRAEEEL----------ERAMRAFNREwPA 802
|
730 740 750
....*....|....*....|....*....|....*...
gi 966979913 875 TYLDLDNKVRTLKKFIKLLGEIMD---HRFKtyQQFRR 909
Cdd:COG4913 803 ETADLDADLESLPEYLALLDRLEEdglPEYE--ERFKE 838
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
640-895 |
2.09e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 640 SEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEhqsvDIATLEDEA 719
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED----MKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 720 QENKSKMKMVEKHMEQQKENMEHLKSL-------KIEAENKYDAIKLKINQLSELADPLKDELNLADS---EVDNQKRGK 789
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIindpvykNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAiikKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 790 RHYEEKQKEHlDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKIQAehashgDREEIMRQY 869
Cdd:PRK01156 339 NDYIKKKSRY-DDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEI------DPDAIKKEL 411
|
250 260
....*....|....*....|....*.
gi 966979913 870 QEARETYLDLDNKVRTLKKFIKLLGE 895
Cdd:PRK01156 412 NEINVKLQDISSKVSSLNQRIRALRE 437
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
48-130 |
2.33e-05 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 47.84 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 48 IIESIHLKNFMCHSMLGpFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVatnRGSSLKGFVKDGQNSADISITLRNR 127
Cdd:COG1195 1 RLKRLSLTNFRNYESLE-LEFSPGINVLVGPNGQGKTNLLEAIYLLATGRSF---RTARDAELIRFGADGFRVRAEVERD 76
|
...
gi 966979913 128 GDD 130
Cdd:COG1195 77 GRE 79
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
168-467 |
2.40e-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: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 168 KKEELIAILDHFNIQFFMKATQLEQMKEDYSYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSI--------AGLS 239
Cdd:TIGR04523 212 KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkikeleKQLN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 240 TMKTNLESLKHEMAWAVVNE-------IEKQLNAIRDNIKIGEDRAARLDRKME--EQQVRLNEAEQKYKDIQ-----DK 305
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDWNKElkselknQEKKLEEIQNQISQNNKIISQLNEQISqlKKELTNSESENSEKQREleekqNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 306 LEKISEETNARAPECMALKADVVAKKRAYNEAEVLYNRSLNEYKALKKDDEQLCKRIEELKKstdqslepERLERQKKIS 385
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE--------TIIKNNSEIK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 386 WLKERVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIKREESDVKHALSYNQRQLKELKDSKTD---RLKRFGPNVPALL 462
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEleeKVKDLTKKISSLK 523
|
....*
gi 966979913 463 EAIDD 467
Cdd:TIGR04523 524 EKIEK 528
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
209-442 |
2.68e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 209 EQIHQGEERLTELKRQCVEKEERFQSIAglstmktnleslkhemawAVVNEIEKQLNAIRDNIKIGEDRAARLDRKMEEQ 288
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK------------------KEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 289 QVRLNEAEQKYKDIQDKLEKISEEtnarapecMALKADVVAKKRAYNEAEVLYN--------RSLNEYKALKKDDEQlck 360
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEE--------LAELLRALYRLGRQPPLALLLSpedfldavRRLQYLKYLAPARRE--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 361 RIEELKKSTD------QSLEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIKREESDVKHALS 434
Cdd:COG4942 151 QAEELRADLAelaalrAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
....*...
gi 966979913 435 YNQRQLKE 442
Cdd:COG4942 231 RLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
636-853 |
5.16e-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: 47.32 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 636 RDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENieehQSVDIATL 715
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS----DLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 716 EDEAQENKSKMKMVEKHMEQQ-KENMEHLKSLKIEAENKYDAIKL---KINQLSELADPLKDELNLADSEVDN--QKRGK 789
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQkKENKKNIDKFLTEIKKKEKELEKlnnKYNDLKKQKEELENELNLLEKEKLNiqKNIDK 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966979913 790 RHYEEKQKEH----LDTLNKKKRELDMKEKELEEKMSQarqicperieVEKSASILDKEINRLRQKIQ 853
Cdd:TIGR04523 192 IKNKLLKLELllsnLKKKIQKNKSLESQISELKKQNNQ----------LKDNIEKKQQEINEKTTEIS 249
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
932-1023 |
5.41e-05 |
|
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: 45.15 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 932 MNFDHKNETLSISVQ---------PGEGNKaafnDMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVN-RR 1001
Cdd:cd03278 80 LTFDNSDGRYSIISQgdvseiieaPGKKVQ----RLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANvER 155
|
90 100
....*....|....*....|..
gi 966979913 1002 IAmDLILKMADSQrfrQFILLT 1023
Cdd:cd03278 156 FA-RLLKEFSKET---QFIVIT 173
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
49-96 |
6.30e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 46.14 E-value: 6.30e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 966979913 49 IESIHLKNFMCHSMLG-PFKFGSNVNFVVGNNGSGKSAVLTALIVGLGG 96
Cdd:COG3950 3 IKSLTIENFRGFEDLEiDFDNPPRLTVLVGENGSGKTTLLEAIALALSG 51
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
205-448 |
6.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 205 ERTKEQIHQGEERLTELKRQCVEKEERFQSIAGLSTMKTNLESLKH-------------EMAWAVVNEIEKQLNAIRDNI 271
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEleeklkkynleelEKKAEEYEKLKEKLIKLKGEI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 272 KIGEDRAAR---LDRKMEEQQVRLNEAEQKYKDIQDKLEKIS----EETNARAPECMALKADVVAKKRAYNEAEVLYNR- 343
Cdd:PRK03918 542 KSLKKELEKleeLKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYLELKDAEKELEREEKEl 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 344 ---------SLNEYKALKKDDEQLCKRIEELKKSTDQ----SLEPERLERQKKISWLKERVKALRNQENSVNQEIEQfqq 410
Cdd:PRK03918 622 kkleeeldkAFEELAETEKRLEELRKELEELEKKYSEeeyeELREEYLELSRELAGLRAELEELEKRREEIKKTLEK--- 698
|
250 260 270
....*....|....*....|....*....|....*...
gi 966979913 411 aIEKDKEEYGKIKREESDVKHALSYNQRQLKELKDSKT 448
Cdd:PRK03918 699 -LKEELEEREKAKKELEKLEKALERVEELREKVKKYKA 735
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
634-895 |
7.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 634 LSRDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRcqlhYKELEMKIRKSNSEIRELEnieehqsvDIA 713
Cdd:PRK03918 301 FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK----LKELEKRLEELEERHELYE--------EAK 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 714 TLEDEAQENKSKMKMVEKhmEQQKENMEHLKSLKIEAENKYDAIKLKINQLselaDPLKDELNLADSEVDNQKRG----K 789
Cdd:PRK03918 369 AKKEELERLKKRLTGLTP--EKLEKELEELEKAKEEIEEEISKITARIGEL----KKEIKELKKAIEELKKAKGKcpvcG 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 790 RHYEEKQKEHLdtLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASiLDKEINRLRQ------KIQAEHASHG--D 861
Cdd:PRK03918 443 RELTEEHRKEL--LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeqlkELEEKLKKYNleE 519
|
250 260 270
....*....|....*....|....*....|....
gi 966979913 862 REEIMRQYQEARETYLDLDNKVRTLKKFIKLLGE 895
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
49-181 |
8.00e-05 |
|
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: 45.26 E-value: 8.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMC---HSMLGPFK-FGSnvnfVVGNNGSGKSAVLTALIVGLGGRAvATNRGSSLKGFVKDGqnsadisITL 124
Cdd:cd03275 1 LKRLELENFKSykgRHVIGPFDrFTC----IIGPNGSGKSNLMDAISFVLGEKS-SHLRSKNLKDLIYRA-------RVG 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 125 RNRGDDAFKASVY---GNSILIQQHISIDGSRSYKLKsatGSVVStkKEELIAILDHFNI 181
Cdd:cd03275 69 KPDSNSAYVTAVYeddDGEEKTFRRIITGGSSSYRIN---GKVVS--LKEYNEELEKINI 123
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
49-126 |
1.15e-04 |
|
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: 44.38 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFmcHSMLGP--FKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSLKGFV------KDGQNSADI 120
Cdd:cd03278 1 LKKLELKGF--KSFADKttIPFPPGLTAIVGPNGSGKSNIIDAIRWVLGEQSAKSLRGEKMSDVIfagsetRKPANFAEV 78
|
....*.
gi 966979913 121 SITLRN 126
Cdd:cd03278 79 TLTFDN 84
|
|
| ABC_RecF |
cd03242 |
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ... |
49-130 |
1.51e-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: 44.98 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMCHSMLgPFKFGSNVNFVVGNNGSGKSAVLTALIVGLGGRavaTNRGSSLKGFVKDGQNSADISITLRNRG 128
Cdd:cd03242 1 LKSLELRNFRNYAEL-ELEFEPGVTVLVGENAQGKTNLLEAISLLATGK---SHRTSRDKELIRWGAEEAKISAVLERQG 76
|
..
gi 966979913 129 DD 130
Cdd:cd03242 77 GE 78
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
637-891 |
1.79e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.62 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 637 DVDSEISDLENEVENKM-----AQILNLQQHLSDLEKDIKRNEELLKRCQlhyKELEMKIRKSNSEIRELENIE---EHQ 708
Cdd:pfam06160 157 EIEEEFSQFEELTESGDylearEVLEKLEEETDALEELMEDIPPLYEELK---TELPDQLEELKEGYREMEEEGyalEHL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 709 SVDiatledeaqenkSKMKMVEKHMEqqkENMEHLKSLKI-EAENKYDAIKLKINQLSELadpLKDELNlADSEVDNQKR 787
Cdd:pfam06160 234 NVD------------KEIQQLEEQLE---ENLALLENLELdEAEEALEEIEERIDQLYDL---LEKEVD-AKKYVEKNLP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 788 GKRHYEEKQKEHLDTLNKKKRELDMK--------------EKELEEKMSQARQICPERIEVEKSASILDKEINRLRQ--- 850
Cdd:pfam06160 295 EIEDYLEHAEEQNKELKEELERVQQSytlnenelervrglEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEqle 374
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 966979913 851 KIQAEHASHGDR-EEIMRQYQEARETYLDLDNKVRTLKKFIK 891
Cdd:pfam06160 375 EIEEEQEEFKESlQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
49-128 |
1.87e-04 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 45.15 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMCHSMLGpFKFGSNVNFVVGNNGSGKSAVLTALIVgLG-GRAVatnRGSSLKGFVKDGQNSADISITLRNR 127
Cdd:PRK00064 3 LTRLSLTDFRNYEELD-LELSPGVNVLVGENGQGKTNLLEAIYL-LApGRSH---RTARDKELIRFGAEAAVIHGRVEKG 77
|
.
gi 966979913 128 G 128
Cdd:PRK00064 78 G 78
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
251-453 |
2.25e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 251 EMAWAVVNEIEKQLNAIRDNIKIGEDRAAR--LDRKMEEQQVRLNEAEQKYKDIQDK--LEKISEETNARAPECMALKAD 326
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKALefLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 327 VVAKKRAYNEAEVLYNrslneykALKKDDEQLCKRIEELKKSTD-QSLEPERLERQKKISWLKER-------VKALRNQE 398
Cdd:COG3206 228 LAEARAELAEAEARLA-------ALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARytpnhpdVIALRAQI 300
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 966979913 399 NSVNQEIEQFQQAIEKDKE-EYGKIKREESDVKHALSYNQRQLKEL--KDSKTDRLKR 453
Cdd:COG3206 301 AALRAQLQQEAQRILASLEaELEALQAREASLQAQLAQLEARLAELpeLEAELRRLER 358
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
208-452 |
2.60e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 208 KEQIHQGEERLTELKRQCVEKEERF----QSIAGLSTMKTNLESLKHEMAwavvNEIEKQLNAIR----------DNIKI 273
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIIsqlnEQISQLKKELTNSESENSEKQ----RELEEKQNEIEklkkenqsykQEIKN 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 274 GEDRAARLDRKMEEQ-------QVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVAKKRAYNEAEVLYNRS-- 344
Cdd:TIGR04523 389 LESQINDLESKIQNQeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLet 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 345 -----LNEYKALKKDDEQLCKRIE----ELKKSTDQS--LEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIE 413
Cdd:TIGR04523 469 qlkvlSRSINKIKQNLEQKQKELKskekELKKLNEEKkeLEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
250 260 270
....*....|....*....|....*....|....*....
gi 966979913 414 KDKEEYGKIKREESdvkhaLSYNQRQLKELKDSKTDRLK 452
Cdd:TIGR04523 549 KDDFELKKENLEKE-----IDEKNKEIEELKQTQKSLKK 582
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
641-781 |
2.75e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 641 EISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQL---------HYKELEMKIRksnsEIRELENIEEHQSVD 711
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaelaelpeRLEELEERLE----ELRELEEELEELEAE 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966979913 712 IATLEDEAQENKSKMK-MVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELNLADSE 781
Cdd:COG4717 172 LAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
48-455 |
2.79e-04 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 45.11 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 48 IIESIH-LKNFMCHSMLGPFKFGSNVNFVVGNNGSGKSAVLTALivglggRAVATNRGSSL---KGFVKDGQNSADISIT 123
Cdd:COG4694 1 MITKIKkLKNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRIL------RSLELGDTSSEviaEFEIEAGGSAPNPSVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 124 LRNRG--DDAFKASVYGNSIL--------IQQHISIDGSRSYKLKSATGSVVSTKKEELIAILDHFNIQFFMKATQLEQM 193
Cdd:COG4694 75 VFNRDfvEENLRSGEEIKGIFtlgeenieLEEEIEELEKEIEDLKKELDKLEKELKEAKKALEKLLEDLAKSIKDDLKKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 194 KEDySYIMETKERTKEQI----HQGEERLTELKRQCVEKE-ERFQSIAGLSTMKTNLESLKHEMAWAVVNEIEKQLNAIR 268
Cdd:COG4694 155 FAS-SGRNYRKANLEKKLsalkSSSEDELKEKLKLLKEEEpEPIAPITPLPDLKALLSEAETLLEKSAVSSAIEELAALI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 269 DNI--------------------------KIGEDRAARLDRKMEEqqvrlnEAEQKYKDIQDKLEKISEETNA-RAPECM 321
Cdd:COG4694 234 QNPgnsdwveqglayhkeeeddtcpfcqqELAAERIEALEAYFDD------EYEKLLAALKDLLEELESAINAlSALLLE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 322 ALKADVVAKKRAYNEAEVLYNRSLNEYKAL---KKDDEQLCKRIEELKKSTDQSLEPERLERQ-----KKISWLK----E 389
Cdd:COG4694 308 ILRTLLPSAKEDLKAALEALNALLETLLAAleeKIANPSTSIDLDDQELLDELNDLIAALNALieehnAKIANLKaekeE 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966979913 390 RVKALRNQE-NSVNQEIEQFQQAIEKDKEEYGKIKREESDVKH------ALSYNQRQLKELKDSKTDRLKRFG 455
Cdd:COG4694 388 ARKKLEAHElAELKEDLSRYKAEVEELIEELKTIKALKKALEDlkteisELEAELSSVDEAADEINEELKALG 460
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
685-895 |
2.80e-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: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 685 KELEMKIRKSNSEIRELENIEEHQSVDIATLEDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQL 764
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 765 SELADPLKDELNLADSEVDNQKRGKRHYEEK---QKEHLDTLNKKKREL-----DMKEKELEEKMSQARQICPERIEVEK 836
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKvndIKEKVKNIHGYMKDIenkiqDGKDDYLKQKETELNTVNAQLEECEK 991
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 966979913 837 SASILDKEINRLRQKIQAEHAshgdREEIMRQYQEARETYLDLDNKVRTLKKFIKLLGE 895
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKI----QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQ 1046
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
198-461 |
3.02e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 198 SYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSiaglstmktnLESLKhemawavvnEIEKQLNAIRDNIKIGE-- 275
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLER----------AEDLV---------EAEDRIERLEERREDLEel 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 276 --DRAARLDRKmEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECmALKADVVAKKRAYNEAEVlynRSLNEYKALKK 353
Cdd:PRK02224 525 iaERRETIEEK-RERAEELRERAAELEAEAEEKREAAAEAEEEAEEA-REEVAELNSKLAELKERI---ESLERIRTLLA 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 354 DDEQLCKRIEELKKSTDQSLEPERlERQKKISWLKERVKALRN--QENSVN---QEIEQFQQAIEKDKEEYGKIKREESD 428
Cdd:PRK02224 600 AIADAEDEIERLREKREALAELND-ERRERLAEKRERKRELEAefDEARIEearEDKERAEEYLEQVEEKLDELREERDD 678
|
250 260 270
....*....|....*....|....*....|...
gi 966979913 429 VKHALSYNQRQLKELKDSKtDRLKRFGPNVPAL 461
Cdd:PRK02224 679 LQAEIGAVENELEELEELR-ERREALENRVEAL 710
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
192-445 |
3.58e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 192 QMKEDYSYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSIAGLstmktnLESLKHEmawavVNEIEKQLNAIRDNI 271
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFL------LEESRDK-----ANQLEEKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 272 KIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEkISEETNARAPEcmalkaDVVAKKRAYNEAEVLYNRSLNEYKAL 351
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ-IATKTICQLTE------EKEAQMEELNKAKAAHSFVVTEFEAT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 352 KKDDEQLCKRIEELKKSTDQSLEPERLERQKKISWLKERVKALRNQENSVNQ--EIEQFQQAIEKDKEEYGKIKREESDV 429
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElkKILAEDEKLLDEKKQFEKIAEELKGK 437
|
250
....*....|....*..
gi 966979913 430 KHALSY-NQRQLKELKD 445
Cdd:pfam05483 438 EQELIFlLQAREKEIHD 454
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
202-444 |
3.96e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 202 ETKERTKEQIHQGEERLTElkRQCVEKEErfQSIAGLSTMKTNLESLKHEMAWAVVNEIEKQLNAIRDNIkigEDRAARL 281
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHL--QQCSQELA--LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLA---LQKMQSE 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 282 DRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVvakkrayNEAEVLYNRSLNEYKALKkdDEQLCKR 361
Cdd:TIGR00618 689 KEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDL-------AAREDALNQSLKELMHQA--RTVLKAR 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 362 IEELKKS---------TDQSLEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEeygKIKREESDVKHA 432
Cdd:TIGR00618 760 TEAHFNNneevtaalqTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE---TLVQEEEQFLSR 836
|
250
....*....|..
gi 966979913 433 LSYNQRQLKELK 444
Cdd:TIGR00618 837 LEEKSATLGEIT 848
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
299-454 |
4.91e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 4.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 299 YKDIQDKLEKISeetnARAPECM---ALKADVVAKKrayneaevlynrSLNEykALKKDDEQLCKRIEELKKSTDQSLEP 375
Cdd:COG2433 345 YDAYKNKFERVE----KKVPPDVdrdEVKARVIRGL------------SIEE--ALEELIEKELPEEEPEAEREKEHEER 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 376 ERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIKREE-----------------SDVKHALSYNQR 438
Cdd:COG2433 407 ELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEErreirkdreisrldreiERLERELEEERE 486
|
170
....*....|....*.
gi 966979913 439 QLKELKdSKTDRLKRF 454
Cdd:COG2433 487 RIEELK-RKLERLKEL 501
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
636-883 |
5.38e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 636 RDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATL 715
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 716 EDEAQENK-SKMKMVEKhmeqQKENMEHLKSLKIEAENKYDAIKLKINQLSELADplkdelnlaDSEVDnqkrgKRHYEE 794
Cdd:pfam15921 624 EARVSDLElEKVKLVNA----GSERLRAVKDIKQERDQLLNEVKTSRNELNSLSE---------DYEVL-----KRNFRN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 795 KQKEHLDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKIQAEHASHGDREEIMRQYQEARE 874
Cdd:pfam15921 686 KSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKH 765
|
....*....
gi 966979913 875 TYLDLDNKV 883
Cdd:pfam15921 766 FLKEEKNKL 774
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
49-886 |
5.65e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFmchsmlGPFKFGSNVNF--------VVGNNGSGKSAVLTALIVGLGGRAVATNRGSSLKGFVKDGQNSADI 120
Cdd:TIGR00618 3 PLRLTLKNF------GSYKGTHTIDFtalgpiflICGKTGAGKTTLLDAITYALYGKLPRRSEVIRSLNSLYAAPSEAAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 121 SITLRNRGDDAFKASVYGNSILIQQHISIDGSRSYKLKSATGSVVSTK---KEELIAILDHFNIQFFMKATQLEQMKEDY 197
Cdd:TIGR00618 77 AELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKkseTEEVIHDLLKLDYKTFTRVVLLPQGEFAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 198 SYIMETKERTK--------EQIHQGEERLTELKRQCVEKEERFQSIAGLSTMKTNLESLKHEMAWAVVNEIEKQLNAIRD 269
Cdd:TIGR00618 157 FLKAKSKEKKEllmnlfplDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 270 NIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADvvakkrayneaevlynRSLNEYK 349
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA----------------PLAAHIK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 350 ALKKDDEQLCKRIEELkKSTDQSLEPERLERQKKISWLKErVKALRNQENSVNQEIEQFQQAIEKDkeeygKIKREESDV 429
Cdd:TIGR00618 301 AVTQIEQQAQRIHTEL-QSKMRSRAKLLMKRAAHVKQQSS-IEEQRRLLQTLHSQEIHIRDAHEVA-----TSIREISCQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 430 KHALSYNQRQLKELKDSKTDRLKrfgpNVPALLEAIDDAYRQGLFTYKPVGPL-GACIHLRDPE---------LALAIES 499
Cdd:TIGR00618 374 QHTLTQHIHTLQQQKTTLTQKLQ----SLCKELDILQREQATIDTRTSAFRDLqGQLAHAKKQQelqqryaelCAAAITC 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 500 CLKGLLQAycchNHADERVLQALMKRFYLPGTSrpQIIVSEFRNEIYDVRHRAAYHPEFPTVLTALEIDNAvVANSLIDM 579
Cdd:TIGR00618 450 TAQCEKLE----KIHLQESAQSLKEREQQLQTK--EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN-PARQDIDN 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 580 RGIETVLLIKnnsVARAVMQSQKPPKNCREAFTAEGDQVfagRYYSSENTRpkflSRDVDSEISDLENEVENKMAQILNL 659
Cdd:TIGR00618 523 PGPLTRRMQR---GEQTYAQLETSEEDVYHQLTSERKQR---ASLKEQMQE----IQQSFSILTQCDNRSKEDIPNLQNI 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 660 QQHLSDlEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIR-ELENIEEHQSVDIATLEDEaQENKSKMKMVEKHMEQQKE 738
Cdd:TIGR00618 593 TVRLQD-LTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRlHLQQCSQELALKLTALHAL-QLTLTQERVREHALSIRVL 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 739 NMEHLKSlkieAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKRGKRHYEEKQKEHLDTLNKKKRELDMKEKELE 818
Cdd:TIGR00618 671 PKELLAS----RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966979913 819 EKMSQARQICPERIEVEKSAS-------ILDKEINRLRQKIQAEHASHGDREEIMRQYQEARETYLDLDNKVRTL 886
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNeevtaalQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNL 821
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
627-782 |
5.78e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 627 ENTRPKFLSRDVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRcqlhykeLEMKIRKSNSEIRELENIEE 706
Cdd:COG2433 393 EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER-------LERELSEARSEERREIRKDR 465
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966979913 707 HqsvdIATLEDEAQENKSKMKMVEKHMEQQKENMEHLKSL-KIEAENKYDAIKlKINQLSeladplKDELNLADSEV 782
Cdd:COG2433 466 E----ISRLDREIERLERELEEERERIEELKRKLERLKELwKLEHSGELVPVK-VVEKFT------KEAIRRLEEEY 531
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
49-90 |
5.92e-04 |
|
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: 43.45 E-value: 5.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 966979913 49 IESIHLKNFMCHSMLGpFKFGSNVNFVVGNNGSGKSAVLTAL 90
Cdd:COG3593 3 LEKIKIKNFRSIKDLS-IELSDDLTVLVGENNSGKSSILEAL 43
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
189-425 |
6.42e-04 |
|
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: 43.02 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 189 QLEQMKEDYSYIMETKERTKEQIHQGEERLTELKRqcvEKEERFQSIAGLSTMKTNLESLkhemawavVNEIEKQLNAIR 268
Cdd:pfam09728 19 KLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQK---EKDQLQSELSKAILAKSKLEKL--------CRELQKQNKKLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 269 DNIKigedraarldRKMEEQQVRLNEAEQKY----KDIQDKLEKISEETNARAPECMALKA---DVVAKkrayNEAEVLY 341
Cdd:pfam09728 88 EESK----------KLAKEEEEKRKELSEKFqstlKDIQDKMEEKSEKNNKLREENEELREklkSLIEQ----YELRELH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 342 NRSLNEYKAL--KKDDEQLCKRIEELKKSTDQSLEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEY 419
Cdd:pfam09728 154 FEKLLKTKELevQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVF 233
|
....*.
gi 966979913 420 GKIKRE 425
Cdd:pfam09728 234 TTFKKE 239
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
63-95 |
6.91e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 42.45 E-value: 6.91e-04
10 20 30
....*....|....*....|....*....|...
gi 966979913 63 LGPFKFGSNVNFVVGNNGSGKSAVLTALIVGLG 95
Cdd:COG3910 30 LEGLEFHPPVTFFVGENGSGKSTLLEAIAVAAG 62
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
723-875 |
7.11e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 723 KSKMKMVEKHMEQQKENMehLKSLKIEAENKYDAIKLKINQ-LSELADPLKDELNLADSEVDNQKRGKRHYEEKQKEHLD 801
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRI--LEEAKKEAEAIKKEALLEAKEeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 802 TLNKKKRELDM-------KEKELEEKMSQARQICPERIEVEKSASILDKE------INRLRQKIQAEHAShgdreeIMRQ 868
Cdd:PRK12704 104 LLEKREEELEKkekeleqKQQELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAV------LIKE 177
|
....*...
gi 966979913 869 Y-QEARET 875
Cdd:PRK12704 178 IeEEAKEE 185
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
957-1023 |
7.21e-04 |
|
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: 42.63 E-value: 7.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966979913 957 DMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDLILKMADSQrfrQFILLT 1023
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGA---QFITTT 218
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
192-427 |
7.53e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 192 QMKEDYSYIMETKERTKEQIHQGEERLTEL-KRQCVEKEERFqsiaGLSTMKTNLESLKHEMAW------AVVNEIEKQL 264
Cdd:PLN02939 153 QALEDLEKILTEKEALQGKINILEMRLSETdARIKLAAQEKI----HVEILEEQLEKLRNELLIrgategLCVHSLSKEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 265 NAIR-----------------DNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISeetnARAPECMALKADV 327
Cdd:PLN02939 229 DVLKeenmllkddiqflkaelIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLS----PLQYDCWWEKVEN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 328 VAK--KRAYNEAEvlynrslnEYKALKKDDEQLCKRIEELKKSTDQS----LEPERLE-RQKKISWLKERVKALRNQENS 400
Cdd:PLN02939 305 LQDllDRATNQVE--------KAALVLDQNQDLRDKVDKLEASLKEAnvskFSSYKVElLQQKLKLLEERLQASDHEIHS 376
|
250 260 270
....*....|....*....|....*....|.
gi 966979913 401 ----VNQEIEQFQQAIEKDKEEYGKIKREES 427
Cdd:PLN02939 377 yiqlYQESIKEFQDTLSKLKEESKKRSLEHP 407
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
635-852 |
9.01e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 635 SRDVDSEISDLENEVENKMAQILnlqQHLSDLEKDIKRNEELLKRCQLHYK----ELEMKIRKSNSEIRELENIEEHQSV 710
Cdd:pfam15921 294 ANSIQSQLEIIQEQARNQNSMYM---RQLSDLESTVSQLRSELREAKRMYEdkieELEKQLVLANSELTEARTERDQFSQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 711 DIATLEDEAQENKSKMKMVEKHMEQQKENMEHL------KSLKIE-AENKYDAIKLKINQLSELADPLKDELNLADSEVD 783
Cdd:pfam15921 371 ESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgNSITIDhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQM 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966979913 784 NQKRGKRHYEEK------QKEHL-DTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKI 852
Cdd:pfam15921 451 AAIQGKNESLEKvssltaQLESTkEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV 526
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
649-876 |
1.07e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 649 VENKMAQILNLQQhlsdLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENieehqsvDIATLEDEAQENKSKMKM 728
Cdd:COG1579 2 MPEDLRALLDLQE----LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKT-------ELEDLEKEIKRLELEIEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 729 VEKHMEQQKENMEHLKSLKieaenkydaiklkinqlseladplkdELNLADSEVDNQKRGKRHYEEKQKEHLDtlnkkkr 808
Cdd:COG1579 71 VEARIKKYEEQLGNVRNNK--------------------------EYEALQKEIESLKRRISDLEDEILELME------- 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966979913 809 ELDMKEKELEEKMSQARQICPE----RIEVEKSASILDKEINRLRQKIqAEHASHGDrEEIMRQYQEARETY 876
Cdd:COG1579 118 RIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEELEAER-EELAAKIP-PELLALYERIRKRK 187
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
755-893 |
1.10e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 755 DAIKLKINQLSELADPLKDELNLADSEVDNQKRGK-RHYEEKQKE---HLDTLNKKKRELDMKEKELEEKMSQARQICPE 830
Cdd:COG2433 380 EALEELIEKELPEEEPEAEREKEHEERELTEEEEEiRRLEEQVERleaEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966979913 831 RIEVEKSASILDKEINRLRQKIqaehashgdreeimrqyQEARETYLDLDNKVRTLKKFIKLL 893
Cdd:COG2433 460 EIRKDREISRLDREIERLEREL-----------------EEERERIEELKRKLERLKELWKLE 505
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
189-382 |
1.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 189 QLEQMKEDYSYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSIAGLstmktnlesLKHEMAWAVVNEIEKQLNAIR 268
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL---------LQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 269 DNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECmalkadvvakKRAYNEAEVLYNRSLNEY 348
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL----------AEELEELQQRLAELEEEL 215
|
170 180 190
....*....|....*....|....*....|....
gi 966979913 349 KALKKDDEQLCKRIEELKKSTDQSLEPERLERQK 382
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
646-906 |
1.20e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 646 ENEVENKMAQILNLQQHLSDLEKDIK--RNEELLKRCQLHYKELEMKIRKSNSEIRELENIE-EHQSVDIATLEDEAQEN 722
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEmDRQAAIYAEQERMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 723 KSKMKMVEkhMEQQKENMEHLKSLKIEAEnkydaiklkINQLSELaDPLKDELNLADSEVDNQKRGKRHYEEKQKEHLDT 802
Cdd:pfam17380 347 ERELERIR--QEERKRELERIRQEEIAME---------ISRMREL-ERLQMERQQKNERVRQELEAARKVKILEEERQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 803 LNKKKRELDMKEKELEEkmsqARQICPERIEVEKSasildKEINRLRQkiqaEHASHGDREEIMRQYQEARE-TYLDLDN 881
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEE----ARQREVRRLEEERA-----REMERVRL----EEQERQQQVERLRQQEEERKrKKLELEK 481
|
250 260
....*....|....*....|....*
gi 966979913 882 KVRTLKKFIKLLGEIMDHRFKTYQQ 906
Cdd:pfam17380 482 EKRDRKRAEEQRRKILEKELEERKQ 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-839 |
1.63e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 186 KATQLEQMKEDYSYimETKERTKEQIHQGEERLTELKRQCVEKEERFQSIAGLSTMKTNLESLKHEMAWAVVNEIEKQLN 265
Cdd:PTZ00121 1195 KAEDARKAEAARKA--EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAI 1272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 266 AIRDNIKIGEDRAARLDRKMEE-----QQVRLNEAEQKYKDIQ--DKLEKISEETNARAPECM-----ALKADVVAKKRA 333
Cdd:PTZ00121 1273 KAEEARKADELKKAEEKKKADEakkaeEKKKADEAKKKAEEAKkaDEAKKKAEEAKKKADAAKkkaeeAKKAAEAAKAEA 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 334 YNEAEVLyNRSLNEYKALKKDDEQLCKRIEELKKSTDQSLEPErlERQKKISWLKERVKALRNQENSVNQEIEQFQQAIE 413
Cdd:PTZ00121 1353 EAAADEA-EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD--EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 414 KDKEEYGKIKREESdvkhalsynqRQLKELKdsKTDRLKRFGPNVPALLEAIDDAyrqglftykpvgplgacihlrdPEL 493
Cdd:PTZ00121 1430 KKKADEAKKKAEEA----------KKADEAK--KKAEEAKKAEEAKKKAEEAKKA----------------------DEA 1475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 494 ALAIESCLKGllqaycchNHADERVLQALMKrfylpgtsrpqiivSEFRNEIYDVRHRAAYHPEFPTVLTALEIDNAVVA 573
Cdd:PTZ00121 1476 KKKAEEAKKA--------DEAKKKAEEAKKK--------------ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 574 NSLIDMRGIETVLLIKNNSVARAVMQSQKPpKNCREAFTAEGDQVFAGRyySSENTRPKFLSRDvdSEISDLENEVENKM 653
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEK-KKAEEAKKAEEDKNMALR--KAEEAKKAEEARI--EEVMKLYEEEKKMK 1608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 654 AQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSnseiRELENIEEHQSVDIATLEDEAQENKSKMKMVEKHM 733
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA----EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 734 EQQKENMEHLKSlKIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKR----GKRHYEEKQKE--------HLD 801
Cdd:PTZ00121 1685 EDEKKAAEALKK-EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKeaeeDKKKAEEAKKDeeekkkiaHLK 1763
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 966979913 802 TLNKKKRELDMKEKE------LEEKMSQARQICPERIEVEKSAS 839
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEavieeeLDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
654-887 |
1.75e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 654 AQILN------LQQHLSDLEKDIKRNEELLKRcQLhyKELEMKIRKSNSEIRELEniEEHQSVDiatLEDEAQENKSKMK 727
Cdd:COG3206 151 AAVANalaeayLEQNLELRREEARKALEFLEE-QL--PELRKELEEAEAALEEFR--QKNGLVD---LSEEAKLLLQQLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 728 MVEKHMEQqkenmehLKSLKIEAENKYDAIKLKINQLSE-----LADP----LKDELNLADSEVDNQKRgkrHYEEKQKE 798
Cdd:COG3206 223 ELESQLAE-------ARAELAEAEARLAALRAQLGSGPDalpelLQSPviqqLRAQLAELEAELAELSA---RYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 799 HLDTLNKKKRELDMKEKELEEKMSQARQicpERIEVEKSASILDKEINRLRQKIQAEHASHGDREEIMRQYQEARETYLD 878
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
....*....
gi 966979913 879 LDNKVRTLK 887
Cdd:COG3206 370 LLQRLEEAR 378
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
168-451 |
2.33e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 168 KKEELIAILDHFNIqffmkaTQLEQMKEDYSYimetkertkEQIHQGEERLTELKRqCVEKEERFQSIAGLStmKTNLES 247
Cdd:PRK05771 17 YKDEVLEALHELGV------VHIEDLKEELSN---------ERLRKLRSLLTKLSE-ALDKLRSYLPKLNPL--REEKKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 248 LKHEMAWAVVNEIEKQLNAIRDNIKIGEDRAARLDRKMEEQQVRLNEAEqKYKDIQDKLEKISEETNARAPECMALKADV 327
Cdd:PRK05771 79 VSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLE-PWGNFDLDLSLLLGFKYVSVFVGTVPEDKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 328 VAKKRAYNEAEVLYNRSLNEYKAL----KKDDEQlcKRIEELKKStdqSLEPERLERQKKISwlkERVKALRNQENSVNQ 403
Cdd:PRK05771 158 EELKLESDVENVEYISTDKGYVYVvvvvLKELSD--EVEEELKKL---GFERLELEEEGTPS---ELIREIKEELEEIEK 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 966979913 404 EIEQfqqaIEKDKEEYGKIKREESDVKHALSYNQRQLKE--LKDSKTDRL 451
Cdd:PRK05771 230 ERES----LLEELKELAKKYLEELLALYEYLEIELERAEalSKFLKTDKT 275
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
49-211 |
2.36e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 41.57 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMCH------SMLGPFKFGSNVNFVVGNNGSGKSAVLTAL-IVGLGGRAVATNRGSSLKGFVKDGQNSADIS 121
Cdd:COG1106 2 LISFSIENFRSFkdeltlSMVASGLRLLRVNLIYGANASGKSNLLEALyFLRNLVLNSSQPGDKLVEPFLLDSESKNEPS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 122 ItlrnrgddaFKASVYGNSILIQQHISIDGSR--SYKLksatgSVVSTKKEELIAILDHFnIQFFMKATQLEQMKEDYSY 199
Cdd:COG1106 82 E---------FEILFLLDGVRYEYGFELDKERiiSEWL-----YFLSTAAQLNVPLLSPL-YDWFDNNISLDTSSDGLTL 146
|
170
....*....|..
gi 966979913 200 IMETKERTKEQI 211
Cdd:COG1106 147 LLKEDESLKEEL 158
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
637-871 |
2.40e-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: 42.35 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 637 DVDSEISDLENEVEN-KMAQILNLQQHLSDLEKDIKRNEELLKRCQLhyKELEMKIRKSNsEIRE---LENIEEHQSVDI 712
Cdd:TIGR01612 1030 DIEQKIEDANKNIPNiEIAIHTSIYNIIDEIEKEIGKNIELLNKEIL--EEAEINITNFN-EIKEklkHYNFDDFGKEEN 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 713 ATLEDEAQENKSKMKMVEKHMEQqkeNMEHLKSLKIEAENKYDAIKLKINQLSELADplKDELNLADSEVDNQKRGKRHY 792
Cdd:TIGR01612 1107 IKYADEINKIKDDIKNLDQKIDH---HIKALEEIKKKSENYIDEIKAQINDLEDVAD--KAISNDDPEEIEKKIENIVTK 1181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 793 EEKQKEHLDTLNKKKRELDMKEKE---LEE----KMSQARQIcpERIEVEKsasiLDKEINRLRQKIQAEHASHGDREEI 865
Cdd:TIGR01612 1182 IDKKKNIYDEIKKLLNEIAEIEKDktsLEEvkgiNLSYGKNL--GKLFLEK----IDEEKKKSEHMIKAMEAYIEDLDEI 1255
|
....*.
gi 966979913 866 MRQYQE 871
Cdd:TIGR01612 1256 KEKSPE 1261
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
258-447 |
2.61e-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: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 258 NEIEKQLNAIRDNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNarapecmALKADVVAKKRAYNE- 336
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREELGEr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 337 AEVLYNRS------------------LNEYKALKKDDEQLCKRIEELKKSTDQsLEPERLERQKKISWLKERVKALRNQE 398
Cdd:COG3883 92 ARALYRSGgsvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAE-LEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 966979913 399 NSVNQEIEQFQQAIEKDKEEYGKIKREESDVKHALSYNQRQLKELKDSK 447
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
259-853 |
2.80e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 259 EIEKQLNAIR--DNIKIGEDRAARLDRKMEEQQVRLNEaEQKYKDIQDKLEKISEETNARAPECMAL----KADVVAKKR 332
Cdd:PTZ00121 1221 EDAKKAEAVKkaEEAKKDAEEAKKAEEERNNEEIRKFE-EARMAHFARRQAAIKAEEARKADELKKAeekkKADEAKKAE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 333 AYNEAEVLYNRSLNEYKA--LKKDDEQLCKRIEELKKST------DQSLEPERLERQKKISWLKERVKALRNQENSVNQE 404
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKAdeAKKKAEEAKKKADAAKKKAeeakkaAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 405 IEQFQQAIEKDKEEYGKIKREESDVKHAlsyNQRQLKELKDSKTDRLKRFGPNVPALLEAIDDAYRQglftyKPVGPLGa 484
Cdd:PTZ00121 1380 ADAAKKKAEEKKKADEAKKKAEEDKKKA---DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA-----KKADEAK- 1450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 485 cihlRDPELALAIESCLKGLLQAycchNHADERVLQALMKRfylpGTSRPQIIVSEFRNEIYDVRHRAAYHPEFPTVLTA 564
Cdd:PTZ00121 1451 ----KKAEEAKKAEEAKKKAEEA----KKADEAKKKAEEAK----KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 565 LEIDNAVVANSLIDMRGIETVLLIKNNSVARAVMQSQ-----KPPKNCREAFTAEGDQVFAGRyySSENTRPKFLSRdvD 639
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEelkkaEEKKKAEEAKKAEEDKNMALR--KAEEAKKAEEAR--I 1594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 640 SEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSnseiRELENIEEHQSVDIATLEDEA 719
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA----EELKKAEEENKIKAAEEAKKA 1670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 720 QENKSKMKMVEKHMEQQKENMEHLKSlKIEAENKYDAIKLKINQLSELADPLKDELNLADSEVDNQKRgKRHYEEKQKEH 799
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKK-EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK-EAEEDKKKAEE 1748
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 966979913 800 LDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEksasiLDKEINRLRQKIQ 853
Cdd:PTZ00121 1749 AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE-----LDEEDEKRRMEVD 1797
|
|
| ABC_SMC4_euk |
cd03274 |
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ... |
48-98 |
3.03e-03 |
|
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: 40.36 E-value: 3.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 966979913 48 IIESIHLKNFMCHS---MLGPF--KFGSnvnfVVGNNGSGKSAVLTALIVGLGGRA 98
Cdd:cd03274 2 IITKLVLENFKSYAgeqVIGPFhkSFSA----IVGPNGSGKSNVIDSMLFVFGFRA 53
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
347-442 |
3.04e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 347 EYKALKKDDEQLCKRIEELKKSTDQSLEpERLER-QKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIKRE 425
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASF-ERLAElRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|
gi 966979913 426 ESDVKHA---LSYNQRQLKE 442
Cdd:COG0542 491 EKELAELeeeLAELAPLLRE 510
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
238-426 |
3.28e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 238 LSTMKTNLESLKHEMAwavvnEIEKQLNAIRDNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNAra 317
Cdd:COG1579 12 LQELDSELDRLEHRLK-----ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 318 pecmalkadvvakkrayneaevlyNRSLNEYKALKKDDEQLCKRIEELKKSTDQSLEpERLERQKKISWLKERVKALRNQ 397
Cdd:COG1579 85 ------------------------VRNNKEYEALQKEIESLKRRISDLEDEILELME-RIEELEEELAELEAELAELEAE 139
|
170 180
....*....|....*....|....*....
gi 966979913 398 ENSVNQEIEQFQQAIEKDKEEYGKiKREE 426
Cdd:COG1579 140 LEEKKAELDEELAELEAELEELEA-EREE 167
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
282-471 |
3.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 282 DRKMEEQQVRLNEAEQKYKDIQDKLEKISEEtnarapecmalkadVVAKKRAYNEAEVlynrslnEYKALKKDDEQLCKR 361
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAE--------------LEELNEEYNELQA-------ELEALQAEIDKLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 362 IEELKkstdqslepERLERQKKIswLKERVKALRNQENSVN--------------------------------QEIEQFQ 409
Cdd:COG3883 74 IAEAE---------AEIEERREE--LGERARALYRSGGSVSyldvllgsesfsdfldrlsalskiadadadllEELKADK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966979913 410 QAIEKDKEEYGKIKREESDVKHALSYNQRQLKELKDSKTDRLKRFGPNVPALLEAIDDAYRQ 471
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
285-453 |
3.46e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 285 MEEQQ---VRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVAKKRAYNEAEvlynrslNEYKALKKDDEQLCKR 361
Cdd:COG1579 2 MPEDLralLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-------KEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 362 IEELKKSTDQSLEPERLER-QKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEygkIKREESDVKHALSYNQRQL 440
Cdd:COG1579 75 IKKYEEQLGNVRNNKEYEAlQKEIESLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEEL 151
|
170
....*....|...
gi 966979913 441 KELKDSKTDRLKR 453
Cdd:COG1579 152 AELEAELEELEAE 164
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
275-471 |
3.63e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 275 EDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVAKKRAYNEAEvlynrslneyKALKKD 354
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAE----------AEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 355 DEQLCKRIEELKKS-----------TDQSLEpERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIK 423
Cdd:COG3883 85 REELGERARALYRSggsvsyldvllGSESFS-DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 966979913 424 REESDVKHALSYNQRQLKELKDSKTDRLKRFGPNVPALLEAIDDAYRQ 471
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
635-899 |
4.22e-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: 41.58 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 635 SRDVDSEISDLENEV-------ENKMAQILNLQQHLSD-LEKDIKRNEELLKrCQLHYKELEMKI-------RKSNSEIR 699
Cdd:TIGR01612 1546 SEIIIKEIKDAHKKFileaeksEQKIKEIKKEKFRIEDdAAKNDKSNKAAID-IQLSLENFENKFlkisdikKKINDCLK 1624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 700 ELENIEEH-QSVDIATLEDEAQENKSKMKMVEKHMEQ---QKENMEHLKSLKIEAENKYDAIKLKINQ------------ 763
Cdd:TIGR01612 1625 ETESIEKKiSSFSIDSQDTELKENGDNLNSLQEFLESlkdQKKNIEDKKKELDELDSEIEKIEIDVDQhkknyeigiiek 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 764 LSELADPLKDELNLADSEVDNQ-KRGKRHYEEKQKEHLDTlNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILD 842
Cdd:TIGR01612 1705 IKEIAIANKEEIESIKELIEPTiENLISSFNTNDLEGIDP-NEKLEEYNTEIGDIYEEFIELYNIIAGCLETVSKEPITY 1783
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 966979913 843 KEINRLRQKIQAEHASHgdrEEIMRQYQeareTYLDlDNKVRTLKKFIKLLGEIMDH 899
Cdd:TIGR01612 1784 DEIKNTRINAQNEFLKI---IEIEKKSK----SYLD-DIEAKEFDRIINHFKKKLDH 1832
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
205-416 |
4.61e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 205 ERTKEQIHQGEERLTELKRQCVEKEERFQSIAGLSTMKTNLESLKHEMAWAVVNeiekQLNAIRDNIKIGEDRAARLDRK 284
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQN----QRGYAQEILATLEDTLKAADRQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 285 MEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPEcmalkADVVAKKRAYNEAEVLYNRSLNEYKALKKDDEQLCKRIEE 364
Cdd:COG5185 422 IEELQRQIEQATSSNEEVSKLLNELISELNKVMRE-----ADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVST 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 966979913 365 LKkstdQSLEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDK 416
Cdd:COG5185 497 LK----ATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENL 544
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
259-450 |
4.91e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 259 EIEKQLNAIRDNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNArapecmaLKADVVAKKRAYNEAE 338
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-------LEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 339 vlynrslneyKALKKDDEQLCKRIEELKKSTDQSlEPERLERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEE 418
Cdd:COG4942 97 ----------AELEAQKEELAELLRALYRLGRQP-PLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190
....*....|....*....|....*....|..
gi 966979913 419 YGKIKREESDVKHALSYNQRQLKELKDSKTDR 450
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAER 197
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
261-471 |
4.98e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 261 EKQLNAIRDNIkigedraARLDRKMEEQQVRLN----EAEQ--KYKDIQDKLEKISEETNARAPEcmALKADVVAKKRAY 334
Cdd:COG1196 178 ERKLEATEENL-------ERLEDILGELERQLEplerQAEKaeRYRELKEELKELEAELLLLKLR--ELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 335 NEAEVLYNRSLNEYKALKKDDEQLCKRIEELKKSTDQSLEPERLERQKKISW------LKERVKALRNQENSVNQEIEQF 408
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLeqdiarLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966979913 409 QQAIEKDKEEYGKIKREESDVKHALSYNQRQLKELKDSKTDRLKRFGpnvpALLEAIDDAYRQ 471
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA----EAEEELEELAEE 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
186-468 |
5.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 186 KATQLEQMKEDYSYImETKERTKEQIHQGEERLTELKRQCVEKEERFQSIAGLS----TMKTNLESLKHEMAWAVVNEIE 261
Cdd:COG4717 117 ELEKLEKLLQLLPLY-QELEALEAELAELPERLEELEERLEELRELEEELEELEaelaELQEELEELLEQLSLATEEELQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 262 KQLNAIRDnikiGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVA---------KKR 332
Cdd:COG4717 196 DLAEELEE----LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallglggslLSL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 333 AYNEAEVLYNRS---LNEYKALKKDDEQLCKRIEELKK-STDQSLEPERLERQKK------------ISWLKERVKALRN 396
Cdd:COG4717 272 ILTIAGVLFLVLgllALLFLLLAREKASLGKEAEELQAlPALEELEEEELEELLAalglppdlspeeLLELLDRIEELQE 351
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966979913 397 QENSVNQ-----EIEQFQQAIEKDKEEYGKIKREESDVKHALSYNQRQLKELKDSKTDRLKRFGPNVPALLEAIDDA 468
Cdd:COG4717 352 LLREAEEleeelQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE 428
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
685-783 |
5.94e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 685 KELEMKIRKSNSEIRELENIEEHQSVD-IATLEDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQ 763
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493
|
90 100
....*....|....*....|
gi 966979913 764 LSELADPLKDELNLADSEVD 783
Cdd:COG0542 494 LAELEEELAELAPLLREEVT 513
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
650-895 |
6.16e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 650 ENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLEDEAQEnkskmkMV 729
Cdd:TIGR00618 672 KELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ------SL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 730 EKHMEQQKENmehLKSLKIEAENKYDAIKLKINQLSELADPLKDelnladsevdnqkrgkrhyeekqkehldtLNKKKRE 809
Cdd:TIGR00618 746 KELMHQARTV---LKARTEAHFNNNEEVTAALQTGAELSHLAAE-----------------------------IQFFNRL 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 810 LDMKEKELEEKMSQARQICPE-RIEVEKSASILDKEINRLRQKIQAEHASHGdreEIMRQYQEARETYLDLDNKVRTLKK 888
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEEEQFLSRLEEKSATLG---EITHQLLKYEECSKQLAQLTQEQAK 870
|
....*..
gi 966979913 889 FIKLLGE 895
Cdd:TIGR00618 871 IIQLSDK 877
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
49-127 |
7.01e-03 |
|
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: 39.59 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 49 IESIHLKNFMC---HSMLGPF--KFgsnvNFVVGNNGSGKSAVLTALIVGLGGRAVATNRGSSLKGFV-KDGQ---NSAD 119
Cdd:cd03273 3 IKEIILDGFKSyatRTVISGFdpQF----NAITGLNGSGKSNILDAICFVLGITNLSTVRASNLQDLIyKRGQagiTKAS 78
|
....*...
gi 966979913 120 ISITLRNR 127
Cdd:cd03273 79 VTIVFDNS 86
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
634-885 |
7.01e-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: 40.48 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 634 LSRDVDSEISDLENEVENKMAQILNLQQHLSDL----EKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQS 709
Cdd:pfam05483 227 LEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtfllEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 710 VDIATLEDEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELadpLKDELNLADSEVDNQKRGK 789
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL---LRTEQQRLEKNEDQLKIIT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 790 RHYEEKQKEhLDTLNKKKRELDMKEKELEEKMSQARQICPERIEVEKSASILDKEINRLRQKIQAEHASHGDREEIMRQY 869
Cdd:pfam05483 384 MELQKKSSE-LEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAI 462
|
250
....*....|....*.
gi 966979913 870 QEARETYLDLDNKVRT 885
Cdd:pfam05483 463 KTSEEHYLKEVEDLKT 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
187-352 |
7.42e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 187 ATQLEQMKEDYSYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSIAglstmKTNLESLKHEmawavvNEIEKQLNA 266
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA-----EELLEALRAA------AELAAQLEE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 267 IRDNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVAKKRAYNEAEVLYNRSLN 346
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
....*.
gi 966979913 347 EYKALK 352
Cdd:COG1196 485 ELAEAA 490
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
637-874 |
8.48e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 39.66 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 637 DVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENieehqsvdiatLE 716
Cdd:pfam15742 45 DLKQHNSLLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKIRELELEVLKQAQSIKSQNS-----------LQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 717 DEAQENKSKMKMVEKHMEQQKENMEHLKSLKIEaenkyDAIKLKINQLSELADPLKdelnladsevDNQKRGKRHY-EEK 795
Cdd:pfam15742 114 EKLAQEKSRVADAEEKILELQQKLEHAHKVCLT-----DTCILEKKQLEERIKEAS----------ENEAKLKQQYqEEQ 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966979913 796 QKEHLdtLNKKKRELDMKEKELEEKMSQArqicpERIEVEKSASILDKEInrLRQKIQAEHAshgDREEIMRQYQEARE 874
Cdd:pfam15742 179 QKRKL--LDQNVNELQQQVRSLQDKEAQL-----EMTNSQQQLRIQQQEA--QLKQLENEKR---KSDEHLKSNQELSE 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
637-875 |
8.95e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 637 DVDSEISDLENEVENKMAQILNLQQHLSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEEHQSVDIATLE 716
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 717 DEAQENKSKMkmvekhmEQQKENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDELN-----LADSEVDNQKRGKRH 791
Cdd:PRK02224 370 SELEEAREAV-------EDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDelrerEAELEATLRTARERV 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 792 YEEKQ----------------KEHLDTLNKKKRELDMKEKELEEKMSQaRQICPERIEVEKSASILDKEINRLRQKIQAE 855
Cdd:PRK02224 443 EEAEAlleagkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDL 521
|
250 260
....*....|....*....|
gi 966979913 856 HASHGDREEIMRQYQEARET 875
Cdd:PRK02224 522 EELIAERRETIEEKRERAEE 541
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
280-928 |
9.11e-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: 40.21 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 280 RLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNArapECMALKADvVAKKRAynEAEVLynrslnEYKALKKDDEQLC 359
Cdd:pfam12128 273 LIASRQEERQETSAELNQLLRTLDDQWKEKRDELNG---ELSAADAA-VAKDRS--ELEAL------EDQHGAFLDADIE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 360 KRIEELKK----STDQSLEPERLE----RQKKISWLKERVKALRNQENsvNQEIEQFQQAIEKDKEEYGKIKREESDVKH 431
Cdd:pfam12128 341 TAAADQEQlpswQSELENLEERLKaltgKHQDVTAKYNRRRSKIKEQN--NRDIAGIKDKLAKIREARDRQLAVAEDDLQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 432 ALSYNQR-QLKELKDSKTDRLKRFGPNVPALLEAIDDA-YRQGLFTYKPVGPLgACIHLRDpelalAIESCLKGLLQAYC 509
Cdd:pfam12128 419 ALESELReQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtATPELLLQLENFDE-RIERARE-----EQEAANAEVERLQS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 510 CHNHADERVLQALMKrfylpgTSRPQIIVSEFRNEIYDVRHRAAyhPEFPTVLTALEIDNAVVANSLidMRGIETVLLIK 589
Cdd:pfam12128 493 ELRQARKRRDQASEA------LRQASRRLEERQSALDELELQLF--PQAGTLLHFLRKEAPDWEQSI--GKVISPELLHR 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 590 NNSVARAVMQSQKPPKNCReAFTAEGDQVFAGRYYSSENT---RPKFLSRDVDSEiSDLENEVENKMAQIL----NLQQH 662
Cdd:pfam12128 563 TDLDPEVWDGSVGGELNLY-GVKLDLKRIDVPEWAASEEElreRLDKAEEALQSA-REKQAAAEEQLVQANgeleKASRE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 663 LSDLEKDIKRNEELLKRCQLHYKELEMKIRKSNSEIRELENIEehqsvdIATLEDEAQENKSKMKMVEKHMEQQK----- 737
Cdd:pfam12128 641 ETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANER------LNSLEAQLKQLDKKHQAWLEEQKEQKreart 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 738 ENMEHLKSLKIEAENKYDAIKLKINQLSELADPLKDEL------NLADSEVDNQKRGKRHYEEKQKEH-LDTLNKKKREL 810
Cdd:pfam12128 715 EKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALetwykrDLASLGVDPDVIAKLKREIRTLERkIERIAVRRQEV 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 811 DMKEKELEEKMSQARQICPERI-EVEKSASILDKEINRLRQKIQAehashgDREEIMRQYQEARETYLDLDNKVRTLKKF 889
Cdd:pfam12128 795 LRYFDWYQETWLQRRPRLATQLsNIERAISELQQQLARLIADTKL------RRAKLEMERKASEKQQVRLSENLRGLRCE 868
|
650 660 670
....*....|....*....|....*....|....*....
gi 966979913 890 IKLLGEIMDHRFKTYQQFRRCLTLRCklyFDNLLSQRAY 928
Cdd:pfam12128 869 MSKLATLKEDANSEQAQGSIGERLAQ---LEDLKLKRDY 904
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
275-456 |
9.81e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 275 EDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISE-----ETNARAPECMalkadvvakkRAYNEAEVLYNRSLNEYK 349
Cdd:PHA02562 240 TDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyEKGGVCPTCT----------QQISEGPDRITKIKDKLK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979913 350 ALKKDDEQLCKRIEELKKSTDQSLEPER--LERQKKISWLKERVKALRNQENSVNQEIEQFQQAIEKDKEEYGKIKREES 427
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFNEQSKklLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD 389
|
170 180 190
....*....|....*....|....*....|....*...
gi 966979913 428 DVKHALSYNQRQLKE-------LKDS--KTDRLKRFGP 456
Cdd:PHA02562 390 KIVKTKSELVKEKYHrgivtdlLKDSgiKASIIKKYIP 427
|
|
| |
