|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
785-883 |
1.74e-50 |
|
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: 176.25 E-value: 1.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 785 NKASFNDMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQRFRQFILLTPQSMSSL 864
Cdd:cd03276 100 NKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGL 179
|
90
....*....|....*....
gi 1958782907 865 PSSKLIRILRMSDPERGQT 883
Cdd:cd03276 180 ASSDDVKVFRMKDPRGPRR 198
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
795-880 |
1.37e-32 |
|
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: 124.34 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 795 LSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSqrFRQFILLTPQSMSSLPSSKLIRILR 874
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKH--TSQFIVITLKKEMFENADKLIGVLF 172
|
....*.
gi 1958782907 875 MSDPER 880
Cdd:cd03239 173 VHGVST 178
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-857 |
5.05e-26 |
|
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: 115.54 E-value: 5.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 23 QLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNI-AGLSTMKTNLEYLKHEMAwavvnEIEKQLNAI 101
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqKELYALANEISRLEQQKQ-----ILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 102 RDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAFNDAEVLYNRSLNE 181
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 182 YKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKRicwLKEKVKALQDQENTVNQEVEQFEQAIEKDKQEHVRIKREDV 261
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKL---EEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 262 EVRHTLSYNQRQLKELKdSKTDRLKRFGPHVPALLEAIDDAYRRRQFTHKPIGPLGACIHLrDPELALAIESCLKGLLQA 341
Cdd:TIGR02168 472 EAEQALDAAERELAQLQ-ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV-DEGYEAAIEAALGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 342 YCCHNHADERVLQSLMKK-------FYPPGTSRPQIIVSEFRNevydvrlRAAYHPEFPTVLTALEIDNAVVANSLIDMR 414
Cdd:TIGR02168 550 VVVENLNAAKKAIAFLKQnelgrvtFLPLDSIKGTEIQGNDRE-------ILKNIEGFLGVAKDLVKFDPKLRKALSYLL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 415 SieTVLLIKNnsVARAVMQSQKPPKNCReAFTADGDQVFAG--RYYSSESTRPKFLSRDvdSEISDLETEIENKKGHIMN 492
Cdd:TIGR02168 623 G--GVLVVDD--LDNALELAKKLRPGYR-IVTLDGDLVRPGgvITGGSAKTNSSILERR--REIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 493 LQHRLSALEKDI--KRNEELLKRCQLHYKEIKM-------------------KIRKNISEIRELENIEEHQSVDIATLED 551
Cdd:TIGR02168 696 LEKALAELRKELeeLEEELEQLRKELEELSRQIsalrkdlarleaeveqleeRIAQLSKELTELEAEIEELEERLEEAEE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 552 EAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLK------------------------------------- 594
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaterrledleeqieelsedie 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 595 -----INQLSELADPLKDELNLADSEVDSQKRG----KQHYEDKQKEhMDTLNKKRRELDMKEKELQEKMSQARQICpER 665
Cdd:TIGR02168 856 slaaeIEELEELIEELESELEALLNERASLEEAlallRSELEELSEE-LRELESKRSELRRELEELREKLAQLELRL-EG 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 666 IEVK---------------------------KSASILDKEINRLRQKIQA----EHASHGDREEIMKQYQEARETYLDLD 714
Cdd:TIGR02168 934 LEVRidnlqerlseeysltleeaealenkieDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYDFLTAQKEDLT 1013
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 715 SKVRTLRRFIKLLEEIMTHRYK-TYQQFRRCLTLRCKLYFDNllsQRAYCGKMNFDHKNET-LSISVQPGEGNKASfndM 792
Cdd:TIGR02168 1014 EAKETLEEAIEEIDREARERFKdTFDQVNENFQRVFPKLFGG---GEAELRLTDPEDLLEAgIEIFAQPPGKKNQN---L 1087
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782907 793 RALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQrfrQFILLT 857
Cdd:TIGR02168 1088 SLLSGGEKALTALALLFAIFKVKPAPFCILDEVDAPLDDANVERFANLLKEFSKNT---QFIVIT 1149
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
795-877 |
5.29e-20 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 87.80 E-value: 5.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 795 LSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQrfRQFILLTPQSMSSLPSSKLIRILR 874
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG--AQVIVITHLPELAELADKLIHIKK 155
|
...
gi 1958782907 875 MSD 877
Cdd:cd03227 156 VIT 158
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
9-857 |
1.19e-17 |
|
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: 88.59 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 9 KNEGDKYKFFMKATQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLSTMKTNLEYL--KHEM 86
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvKEKI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 87 A--WAVVNEIEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDViar 164
Cdd:TIGR02169 297 GelEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL--- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 165 trafNDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKR------ICWLKEKVKALQDQENTVNQE 238
Cdd:TIGR02169 374 ----EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELadlnaaIAGIEAKINELEEEKEDKALE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 239 VEQFEQAIE-------KDKQEHVRIKREDVEVRHTLSYNQRQLKELKDSKtDRLKRFGPHVPALLEAIDDayrRRQFTHK 311
Cdd:TIGR02169 450 IKKQEWKLEqlaadlsKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA-RASEERVRGGRAVEEVLKA---SIQGVHG 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 312 PIGPLGACihlrDPELALAIESCLKGLLQAYCCHNHAD-ERVLQSLMKKFYPPGTSRPQIIVSEFRNEV----------- 379
Cdd:TIGR02169 526 TVAQLGSV----GERYATAIEVAAGNRLNNVVVEDDAVaKEAIELLKRRKAGRATFLPLNKMRDERRDLsilsedgvigf 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 380 ------YDVRLRAAYHPEFPTVLTALEIDNA---------------------------------------------VVAN 408
Cdd:TIGR02169 602 avdlveFDPKYEPAFKYVFGDTLVVEDIEAArrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepaelqRLRE 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 409 SLIDMRSIETVLLIKNNSVARAVMQSQKPPKNC-REAFTADGDQVFAGRYYSSESTRPKFLSRD----------VDSEIS 477
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDAsRKIGEIEKEIEQLEQEEEKLKERLEELEEDlssleqeienVKSELK 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 478 DLETEIENKKGHIMNLQHRLSALEKDIkrNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATLEDEAEENK 557
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 558 IKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKDELnladSEVDSQKRGKQHYEDKQKEHMDTL 637
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER----DELEAQLRELERKIEELEAQIEKK 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 638 NKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKeINRLRQKIQAEHASHGD-REEIMKQYQEARETYLDLDSK 716
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDELKEK 994
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 717 VRTLRR----FIKLLEEIMTHRYKTYQQFRRCLTLRCKLYFDNLLSQRAYCGKMNFDHK-NETLSISVQPgeGNKASfND 791
Cdd:TIGR02169 995 RAKLEEerkaILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGGTGELILENPDDPfAGGLELSAKP--KGKPV-QR 1071
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782907 792 MRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQrfrQFILLT 857
Cdd:TIGR02169 1072 LEAMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEA---QFIVVS 1134
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
796-873 |
7.79e-15 |
|
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: 74.17 E-value: 7.79e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958782907 796 SGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQRFRQFILLTPQSMSSLPSSKLIRIL 873
Cdd:cd03277 128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITPKLLPGLNYHEKMTVL 205
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
470-729 |
4.00e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 470 RDVDSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATL 549
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 550 EDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQ-------LSELADPLKDELNLADSEVDSQKRG 622
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaeealleAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 623 KQHYEDKQKEHMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQ 702
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260
....*....|....*....|....*..
gi 1958782907 703 YQEARETYLDLDSKVRTLRRFIKLLEE 729
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
475-722 |
7.74e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 475 EISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKrcqlhykEIKMKIRKNISEIRELENIEEHQSVDIATLEDEAE 554
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-------ELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 555 ENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKI-NQLSELADPLKDELNLADSEVDSQKRgKQHYEDKQKEH 633
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELlEALRAAAELAAQLEELEEAEEALLER-LERLEEELEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 634 MDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARETYLDL 713
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
....*....
gi 1958782907 714 DSKVRTLRR 722
Cdd:COG1196 507 LEGVKAALL 515
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
5-841 |
4.16e-09 |
|
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: 60.76 E-value: 4.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 5 FLQSKNEGDKYKFFMKATQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLSTMKTNLEYLKH 84
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 85 EMAWAVVNE----IEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNArapecmALKTD 160
Cdd:pfam02463 292 AKEEEELKSellkLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE------LEKLQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 161 VIARTRAFNDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKRICWLKEKVKALQDQENTVNQEVE 240
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 241 QFEQAIEKDKQEHVRIKREDVEVRHTLSYNQRQLKELKDSKTDRLKRF-GPHVPALLEAIDDAY---RRRQFTHKPIGPL 316
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQkLEERSQKESKARSGLkvlLALIKDGVGGRII 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 317 GACIHLRDPELALAIESCLKGLLQAYCCHNHADE-----RVLQSLMKKFYPPGTSRPQIIVSEF---RNEVYDVRLRAAY 388
Cdd:pfam02463 526 SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEveerqKLVRALTELPLGARKLRLLIPKLKLplkSIAVLEIDPILNL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 389 HPEFPTVLTALEIDNAVVANSLIDMRSIETVL----------LIKNNSVARAVMQSQKPPKNCREAFTADGDQVFAGRYY 458
Cdd:pfam02463 606 AQLDKATLEADEDDKRAKVVEGILKDTELTKLkesakakesgLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 459 SSESTRPKFLSRDVDSEISDLETEIENKKGH-------IMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISE 531
Cdd:pfam02463 686 ESELAKEEILRRQLEIKKKEQREKEELKKLKleaeellADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 532 IRELENIEEHQSVDIA-----TLEDEAEENKIKMQMVEKNMEQQK----------ENMENLKTLKIEAENKYDTIKLKIN 596
Cdd:pfam02463 766 KSELSLKEKELAEEREkteklKVEEEKEEKLKAQEEELRALEEELkeeaelleeeQLLIEQEEKIKEEELEELALELKEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 597 QLSELADPLKDELNLADS--EVDSQKRGKQHYEDKQKEHMDTLNKKRRELDMKEKELQEKMSQARQ-------------- 660
Cdd:pfam02463 846 QKLEKLAEEELERLEEEItkEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLleekeneieerike 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 661 ----------------ICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARETYLDLDSKVRTLRRFI 724
Cdd:pfam02463 926 eaeillkyeeepeellLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 725 KLLEEIMTHRYKTYQQFRRCL----TLRCKLYFDNLLSQRAYCGKMNFDHK-NETLSISVQPGegnKASFNDMRALSGGE 799
Cdd:pfam02463 1006 KLIRAIIEETCQRLKEFLELFvsinKGWNKVFFYLELGGSAELRLEDPDDPfSGGIEISARPP---GKGVKNLDLLSGGE 1082
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1958782907 800 RSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMI 841
Cdd:pfam02463 1083 KTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLL 1124
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
470-689 |
4.48e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 470 RDVDSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATL 549
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 550 EDEA----EENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQH 625
Cdd:COG4942 110 LRALyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958782907 626 YEDKQKEHMDTLNKKRRELDMKEKELQEKMSQARQicperievkksasiLDKEINRLRQKIQAE 689
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEE--------------LEALIARLEAEAAAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-584 |
2.05e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 9 KNEGDKYKFFMKATQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLSTMKTNLEYLkhemAW 88
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE----LL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 89 AVVNEIEKQLNAIrdnikigEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAF 168
Cdd:COG1196 295 AELARLEQDIARL-------EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 169 NDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKSTdQSLEPERLERQKRICWLKEKVKALQDQENTVNQEVEQFEQAIEK 248
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 249 DKQEHVRIKREDVEVRHTLSYNQRQLKELKDSKTDRLKRFGPHVP---ALLEAIDDA---YRRRQFTHKPIGPLGACIHL 322
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAArllLLLEAEADYegfLEGVKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 323 R-----DPELALAIESCLKGLLQAYCCHNHADERVLQSLMKK-------FYPPGTSRPQIIVSEF--RNEVYDVRLRAAY 388
Cdd:COG1196 527 AvligvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratFLPLDKIRARAALAAAlaRGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 389 HPEFPTVLTALEIDNAVVANSLIDMRSIETVLLIKNNSVARAVmqsqkppkncreafTADGDQVFAGRYYSSESTRPKFL 468
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV--------------TLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 469 SRDVDSEISDLETEIENKKgHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIAT 548
Cdd:COG1196 673 ALLEAEAELEELAERLAEE-ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580 590
....*....|....*....|....*....|....*.
gi 1958782907 549 LEDEAEEnkikmqmvEKNMEQQKENMENLKTlKIEA 584
Cdd:COG1196 752 ALEELPE--------PPDLEELERELERLER-EIEA 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
468-688 |
2.12e-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: 58.11 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 468 LSRDVDSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIA 547
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 548 TLEDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQHYE 627
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958782907 628 DKQKEHMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQA 688
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
476-721 |
2.57e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 476 ISDLETEIENkkghimnlqhRLSALEKD---------IKRNEELLKRCQ--LHYKEIKMKIRKNISEIRELENIEEHQSV 544
Cdd:COG1196 191 LEDILGELER----------QLEPLERQaekaeryreLKEELKELEAELllLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 545 DIATLEDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQ 624
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 625 HYEDKQKEHMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQ 704
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250
....*....|....*..
gi 1958782907 705 EARETYLDLDSKVRTLR 721
Cdd:COG1196 421 EELEELEEALAELEEEE 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
474-729 |
4.57e-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: 53.23 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 474 SEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKrcqlhykEIKMKIRKNISEIRELENieehqsvDIATLEDEA 553
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-------ALERRIAALARRIRALEQ-------ELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 554 EENKIKMQMVEKNMEQQKENMENLktlkieaenkydtikLKINQLSELADPLKDELNlADSEVDSQKRGK--QHYEDKQK 631
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAEL---------------LRALYRLGRQPPLALLLS-PEDFLDAVRRLQylKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 632 EHMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSasiLDKEINRLRQKIQaehashgdreEIMKQYQEARETYL 711
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAA---LEALKAERQKLLA----------RLEKELAELAAELA 216
|
250
....*....|....*...
gi 1958782907 712 DLDSKVRTLRRFIKLLEE 729
Cdd:COG4942 217 ELQQEAEELEALIARLEA 234
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
491-729 |
5.01e-07 |
|
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: 53.91 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 491 MNLQhRLSALEKDIKRNEELLKR---CQLHYKEIKmkirkniSEIRELEnieehqsVDIATLEDEAEENKIKMQMVEKNM 567
Cdd:TIGR02168 186 ENLD-RLEDILNELERQLKSLERqaeKAERYKELK-------AELRELE-------LALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 568 EQQKenMENLKTLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQHYedkqkehmdtlNKKRRELDMK 647
Cdd:TIGR02168 251 AEEE--LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL-----------RERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 648 EKELQEKMSQARQicpERIEVKKSASILDKEINRLRQKIQAEHASHgdrEEIMKQYQEARETYLDLDSKVRTLRRFIKLL 727
Cdd:TIGR02168 318 LEELEAQLEELES---KLDELAEELAELEEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQLETLRSKVAQL 391
|
..
gi 1958782907 728 EE 729
Cdd:TIGR02168 392 EL 393
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
473-660 |
5.95e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 473 DSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELE-NIEEHQsvdiATLED 551
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEaEIEERR----EELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 552 EAEENKI----------------------KMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKDEL 609
Cdd:COG3883 91 RARALYRsggsvsyldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1958782907 610 NLADSEVDSQKRGKQHYEDKQKEHMDTLNKKRRELDMKEKELQEKMSQARQ 660
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
519-729 |
4.97e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 519 KEIKMKIRKNISEIRELENieehqSVDIAtledeaeENKIKMQmvEKNM-EQQKENMENLKtlkiEAENKYDTIKLKINQ 597
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDM-----KIDHI-------QQQIKTY--NKNIeEQRKKNGENIA----RKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 598 LSELADPLKDELnladSEVDSQKrgkqhyeDKQKEHMDTLNKKRRELDMKEKELQ--EKMSQARQICP----------ER 665
Cdd:PHA02562 232 IKAEIEELTDEL----LNLVMDI-------EDPSAALNKLNTAAAKIKSKIEQFQkvIKMYEKGGVCPtctqqisegpDR 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958782907 666 I-EVKKSASILDKEINRLRQKIQAEhashgdrEEIMKQYQEARETYLDLDSKVRTLRRFIKLLEE 729
Cdd:PHA02562 301 ItKIKDKLKELQHSLEKLDTAIDEL-------EEIMDEFNEQSKKLLELKNKISTNKQSLITLVD 358
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
470-731 |
5.13e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 470 RDVDSEISDLET---EIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDI 546
Cdd:PRK03918 217 PELREELEKLEKevkELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 547 aTLEDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKydtiKLKINQLSELADPLKDELNLADSEVDSQKRGKQhy 626
Cdd:PRK03918 297 -KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHELYEEAKA-- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 627 edkQKEHMDTLNKKR--RELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHG---------- 694
Cdd:PRK03918 370 ---KKEELERLKKRLtgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelt 446
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1958782907 695 --DREEIMKQY----QEARETYLDLDSKVRTLRRFIKLLEEIM 731
Cdd:PRK03918 447 eeHRKELLEEYtaelKRIEKELKEIEEKERKLRKELRELEKVL 489
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
43-276 |
7.92e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 43 EQINQGEERLTELKRQCLEKEERFQNIAglstmktnleylkhemawAVVNEIEKQLNAIRDNIKIGEERAAKLDRKMEEQ 122
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK------------------KEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 123 QVRLNDAEKKYKDIQDKLEKISEETNARAPECMAL----KTDVIARTRAFNDAE--VLYNRSLNEykALKKDGEQLCKRI 196
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpPLALLLSPEDFLDAVrrLQYLKYLAP--ARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 197 EELKKSTdQSLEPERLERQKRICWLKEKVKALQDQENTVNQEVEQFEQAIEKDKQEHVRIKREDVEVRHTLSYNQRQLKE 276
Cdd:COG4942 160 AELAALR-AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-850 |
1.51e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 49 EERLTELKRQClEKEERFQNIaglstmKTNLEYLKHEMAWAVVNEIEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLND 128
Cdd:COG1196 199 ERQLEPLERQA-EKAERYREL------KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 129 AEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAFNDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKStDQSLE 208
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE-LEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 209 PERLERQKRICWLKEKVKALQDQENTVNQEVEQFEQAIEKDKQEHVRIKREDVEVRHTLSYNQRQLKELKDSKTDRLKRF 288
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 289 GPHVPALLEAIDDAYRRRQFthkpigplgaciHLRDPELALAIESCLKGLLQAYCCHNHADERVLQSLMKKfyppgtsRP 368
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEE------------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-------AA 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 369 QIIVSEfrnevydvRLRAAYHPEFPTVLTALEIDN-AVVANSLIDMRSIETVLLIKNNSVARAVMQsqkpPKNCREAFTA 447
Cdd:COG1196 492 RLLLLL--------EAEADYEGFLEGVKAALLLAGlRGLAGAVAVLIGVEAAYEAALEAALAAALQ----NIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 448 DGDQVFAGRyysSESTRPKFLSRDVDSEISDLEteienkkghimnLQHRLSALEKDIKRNEELLKRCQLHYKEIkmkiRK 527
Cdd:COG1196 560 AAAIEYLKA---AKAGRATFLPLDKIRARAALA------------AALARGAIGAAVDLVASDLREADARYYVL----GD 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 528 NISEIRELENIEEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKydtIKLKINQLSELADPLKD 607
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE---LEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 608 ELNLADSEVDSQKRGKQHYEDKQKEHMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQ 687
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 688 A----------EHashgdrEEIMKQYQEARETYLDLDSKVRTLRRFIKLLEEIMTHRYK-TYQQ--------FRR----- 743
Cdd:COG1196 778 AlgpvnllaieEY------EELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLeTFDAvnenfqelFPRlfggg 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 744 --CLTLRCKlyfDNLLSqrayCGkmnfdhknetLSISVQPGeGNKASfnDMRALSGGERSFSTVCFILSLWSIAESPFrC 821
Cdd:COG1196 852 eaELLLTDP---DDPLE----TG----------IEIMAQPP-GKKLQ--RLSLLSGGEKALTALALLFAIFRLNPSPF-C 910
|
810 820 830
....*....|....*....|....*....|.
gi 1958782907 822 -LDEFDVYMDMVN-RRIAmDMILKMADSQRF 850
Cdd:COG1196 911 vLDEVDAPLDDANvERFA-ELLKEMSEDTQF 940
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
766-857 |
2.22e-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: 46.30 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 766 MNFDHKNETLSISVQ---------PGEGNKasfnDMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVN-RR 835
Cdd:cd03278 80 LTFDNSDGRYSIISQgdvseiieaPGKKVQ----RLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANvER 155
|
90 100
....*....|....*....|..
gi 1958782907 836 IAmDMILKMADSQrfrQFILLT 857
Cdd:cd03278 156 FA-RLLKEFSKET---QFIVIT 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-286 |
5.33e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 22 TQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNI----AGLSTMKTNLEYLKHEmawavVNEIEKQ 97
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELreelEKLEKEVKELEELKEE-----IEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 98 LNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQdKLEKISEETNarapECMALKTDVIARTRAFNDAEVLYNR 177
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYI----KLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 178 SLNEYKALKKDGEQLCKRIEELKKstdqslepERLERQKRICWLKEKVKALQD----QENTVNQEVEQFEQAIEKDKQEH 253
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKK--------KLKELEKRLEELEERHELYEEakakKEELERLKKRLTGLTPEKLEKEL 393
|
250 260 270
....*....|....*....|....*....|...
gi 1958782907 254 VRIKREDVEVRHTLSYNQRQLKELKDSKTDRLK 286
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
471-725 |
6.57e-05 |
|
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: 46.39 E-value: 6.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 471 DVDSEISDLETEIEN-----KKGHIMNLQHRLSALEKDIKRNEELLKRCQlhyKEIKMKIRKNISEIRELENieehQSVD 545
Cdd:pfam06160 157 EIEEEFSQFEELTESgdyleAREVLEKLEEETDALEELMEDIPPLYEELK---TELPDQLEELKEGYREMEE----EGYA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 546 IATLEDEAEENKIKmqmveknmEQQKENMENLKTLKI-EAENKYDTIKLKINQLSELadpLKDELNlADSEVDSQKRGKQ 624
Cdd:pfam06160 230 LEHLNVDKEIQQLE--------EQLEENLALLENLELdEAEEALEEIEERIDQLYDL---LEKEVD-AKKYVEKNLPEIE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 625 HYEDKQKEHMDTLNKKRRELDMK--------------EKELQEKMSQARQICPERIEVKKSASILDKEINRLRQ---KIQ 687
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVQQSytlnenelervrglEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEqleEIE 377
|
250 260 270
....*....|....*....|....*....|....*....
gi 1958782907 688 AEHASHGDR-EEIMKQYQEARETYLDLDSKVRTLRRFIK 725
Cdd:pfam06160 378 EEQEEFKESlQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
476-705 |
8.24e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 476 ISDLETEIENKKGHIMNLQ--------HRLSALEKDIKRNEELLKrcqlhyKEIKMKIRKNISEIRELENIEEHQSVDIA 547
Cdd:TIGR01612 1028 TNDIEQKIEDANKNIPNIEiaihtsiyNIIDEIEKEIGKNIELLN------KEILEEAEINITNFNEIKEKLKHYNFDDF 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 548 TLEDEA----EENKIKMQMveKNMEQQ-KENMENLKTLKIEAENKYDTIKLKINQLSELADplKDELNLADSEVDSQKRG 622
Cdd:TIGR01612 1102 GKEENIkyadEINKIKDDI--KNLDQKiDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD--KAISNDDPEEIEKKIEN 1177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 623 KQHYEDKQKEHMDTLNKKRRELDMKEKElQEKMSQARQIcpeRIEVKKSASIL-----DKEINRLRQKIQAEHASHGDRE 697
Cdd:TIGR01612 1178 IVTKIDKKKNIYDEIKKLLNEIAEIEKD-KTSLEEVKGI---NLSYGKNLGKLflekiDEEKKKSEHMIKAMEAYIEDLD 1253
|
....*...
gi 1958782907 698 EIMKQYQE 705
Cdd:TIGR01612 1254 EIKEKSPE 1261
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
484-731 |
9.83e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 9.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 484 ENKKGHIMNLQHR-LSALEKDIKRNEELLKRCQLHYKEIKMKI---------RKNISEIRELEniEEHQSVDIATLEDEA 553
Cdd:PRK03918 447 EEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKELRELEKVLkkeseliklKELAEQLKELE--EKLKKYNLEELEKKA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 554 EE--------NKIKMQMveKNMEQQKENMENLKTLKIEAENKYDTIKlkinqlSELADPLKDELNLADSEVDSQKRGKQH 625
Cdd:PRK03918 525 EEyeklkeklIKLKGEI--KSLKKELEKLEELKKKLAELEKKLDELE------EELAELLKELEELGFESVEELEERLKE 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 626 YEDKQKEHMdTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEhashgDREEIMKQYQE 705
Cdd:PRK03918 597 LEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE-----EYEELREEYLE 670
|
250 260
....*....|....*....|....*.
gi 1958782907 706 ARETYLDLDSKVRTLRrfiKLLEEIM 731
Cdd:PRK03918 671 LSRELAGLRAELEELE---KRREEIK 693
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
475-731 |
9.84e-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: 46.17 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 475 EISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATLEDEAE 554
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 555 ENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSEL--ADPLKDELNLADSEVDSQKRGKQHYEDKQKE 632
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 633 HMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKiqaEHASHGDREEIMKQYQEARETYLD 712
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK---KNKLKQEVKQIKETIKEIRNKWPE 663
|
250
....*....|....*....
gi 1958782907 713 LDSKVRTLRRFIKLLEEIM 731
Cdd:TIGR04523 664 IIKKIKESKTKIDDIIELM 682
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
519-731 |
1.50e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 519 KEIKMKIRKNISEIRELENIEEHqsvdIATLEDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEaenkYDTIKLKINQL 598
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEEL----IKEKEKELEEVLREINEISSELPELREELEKLEKEVKE----LEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 599 SELADPLKDELnladSEVDSQKRGKQHYEDKQKEHMDTLNKKRRELdmkeKELQEKMSQARQICPERIEVKKSASILDKE 678
Cdd:PRK03918 244 EKELESLEGSK----RKLEEKIRELEERIEELKKEIEELEEKVKEL----KELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1958782907 679 INRLRQKIQAEHASHGDREEIMKQYQEARETYLDLDSKVRTLRRFIKLLEEIM 731
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAK 368
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-278 |
1.67e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 83 KHEMAWAVVNEIEKQLNAIRDNikigEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAP--ECMALKTD 160
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 161 VIARTRAFNDAEvlynRSLNEYKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKRICWLKEKVKALQDQENTVNQEVE 240
Cdd:COG4717 141 LAELPERLEELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190
....*....|....*....|....*....|....*...
gi 1958782907 241 QFEQAIEKDKQEhvrikREDVEVRHTLSYNQRQLKELK 278
Cdd:COG4717 217 EAQEELEELEEE-----LEQLENELEAAALEERLKEAR 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
470-597 |
1.76e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 470 RDVDSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRcqlhYKEIKMKIRKNiseiRELENIE---EHQSVDI 546
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK----YEEQLGNVRNN----KEYEALQkeiESLKRRI 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1958782907 547 ATLEDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQ 597
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
475-615 |
2.32e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 475 EISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQL-----HYKEIKMKIRKNISEIRELENIEEHQSVDIATL 549
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaelaELPERLEELEERLEELRELEEELEELEAELAEL 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782907 550 EDEAEENKIKM-QMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKDELNLADSE 615
Cdd:COG4717 176 QEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
791-857 |
2.88e-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: 43.40 E-value: 2.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782907 791 DMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQrfrQFILLT 857
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGA---QFITTT 218
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
26-283 |
3.09e-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: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 26 QMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLStmktnleylkhEMAWAVVNEIEKQLNAIRDNI 105
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLL-----------EESRDKANQLEEKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 106 KIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLE-------KISEETNARAPECMALKTDVIARTRAFNDAEVLYNRS 178
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 179 L-NEYKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKRIcWLKEKVKALQDQENTV--NQEVEQFEQAIEKDKQEHV- 254
Cdd:pfam05483 365 LrTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEV-ELEELKKILAEDEKLLdeKKQFEKIAEELKGKEQELIf 443
|
250 260 270
....*....|....*....|....*....|....*.
gi 1958782907 255 -------RIKREDVEVRHTLSYNQRQLKELKDSKTD 283
Cdd:pfam05483 444 llqarekEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
530-710 |
3.90e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 530 SEIRELENIEEHQSVDIATLEDEAEEnkikmqmVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKD-- 607
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 608 ELNLADSEVDSQKRGKQHYEDKQKEHMDtlnkkrrELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQ 687
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELME-------RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|....*
gi 1958782907 688 AEHASHGDR--EEIMKQYQEARETY 710
Cdd:COG1579 163 AEREELAAKipPELLALYERIRKRK 187
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
474-729 |
4.15e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 474 SEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEhqsvDIATLEDEA 553
Cdd:PRK01156 183 SNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED----MKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 554 EENKIKMQMVEKNMEQQKENMENLKTL-------KIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQHY 626
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIindpvykNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 627 ED--KQKEHMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAehashgDREEIMKQYQ 704
Cdd:PRK01156 339 NDyiKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEI------DPDAIKKELN 412
|
250 260
....*....|....*....|....*
gi 1958782907 705 EARETYLDLDSKVRTLRRFIKLLEE 729
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRE 437
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
457-730 |
5.28e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 457 YYSSESTRPKFLSRDVDSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELE 536
Cdd:TIGR04523 142 KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 537 NIEEHQSvdiaTLEDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEV 616
Cdd:TIGR04523 222 ELKKQNN----QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 617 DSQKrgkqhyedKQKEHmDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLR---QKIQAEHASH 693
Cdd:TIGR04523 298 SDLN--------NQKEQ-DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEK 368
|
250 260 270
....*....|....*....|....*....|....*...
gi 1958782907 694 GDR-EEIMKQYQEARETYLDLDSKVRTLRRFIKLLEEI 730
Cdd:TIGR04523 369 QNEiEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
91-278 |
6.05e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 91 VNEIEKQLNAIR---------DNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNA--RAPECMALKT 159
Cdd:COG3206 191 LEEAEAALEEFRqknglvdlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 160 DVIARTRAFNDAEVLYNRSLNEYKALKKdgeqlckRIEELKKSTDQSLEPERLERQKRICWLKEKVKALQDQENTVNQEV 239
Cdd:COG3206 271 QLAELEAELAELSARYTPNHPDVIALRA-------QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL 343
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958782907 240 EQFEQAiekdKQEHVRIKReDVEVRHTLsYNQ--RQLKELK 278
Cdd:COG3206 344 AELPEL----EAELRRLER-EVEVAREL-YESllQRLEEAR 378
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
22-278 |
7.29e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 22 TQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNI--------AGLSTMKTNLEYLKHEMAWAVVNE 93
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkikeleKQLNQLKSEISDLNNQKEQDWNKE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 94 -------IEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAE-------KKYKDIQDKLEKISEETNARAPECMALKT 159
Cdd:TIGR04523 312 lkselknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensekqRELEEKQNEIEKLKKENQSYKQEIKNLES 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 160 DVIARTRAFNDAEVLYNRSLNEYKALKKDGEQLCKRIEELK-------------KSTDQSLEPERLERQKRICWLKEKVK 226
Cdd:TIGR04523 392 QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKetiiknnseikdlTNQDSVKELIIKNLDNTRESLETQLK 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1958782907 227 ALQDQENTVNQEVEQFEQAIEKDKQEHVRIKREDVEVRHTLSYNQRQLKELK 278
Cdd:TIGR04523 472 VLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLK 523
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
471-718 |
9.60e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 471 DVDSEISDLETEIENKKGHImnlqHRLSALEKDIKRNEELLKRcqlhykeikmkiRKNISE-IRELENIEEHQSVDIATL 549
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERL----ERAEDLVEAEDRIERLEER------------REDLEElIAERRETIEEKRERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 550 EDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKDELNLAD--SEVDSQKRGKQHYE 627
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDeiERLREKREALAELN 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 628 DKQKEHMDTLNKKRRELDMKE-----KELQEKMSQA-----------RQICPERIEVKKSASILDKEINR---LRQKIQA 688
Cdd:PRK02224 623 DERRERLAEKRERKRELEAEFdeariEEAREDKERAeeyleqveeklDELREERDDLQAEIGAVENELEEleeLRERREA 702
|
250 260 270
....*....|....*....|....*....|
gi 1958782907 689 EHASHGDREEIMKQYQEARETYLDLDSKVR 718
Cdd:PRK02224 703 LENRVEALEALYDEAEELESMYGDLRAELR 732
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
92-307 |
1.00e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 92 NEIEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAfnda 171
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA---- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 172 evLYNRSLNEYKAL---KKDGEQLCKRIEELKKSTDQsleperleRQKRICWLKEKVKALQDQENTVNQEVEQFEQAIEK 248
Cdd:COG4942 113 --LYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPA--------RREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782907 249 DKQEhvrikredvevrhtlsynQRQLKELKDSKTDRLKRFGPHVPALLEAIDDAYRRRQ 307
Cdd:COG4942 183 LEEE------------------RAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
470-746 |
1.04e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 470 RDVDSEIS----DLETEIENKKGHIMNLQHRLSALEKDIKRNEELLkrCQLHYKEIKmkirkniseirelENIEEHQsVD 545
Cdd:pfam15921 216 RSLGSAISkilrELDTEISYLKGRIFPVEDQLEALKSESQNKIELL--LQQHQDRIE-------------QLISEHE-VE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 546 IATLEDEAEENKIKMQMVEKNMEQQKENMENLKTLKI----EAENKYDTIKLKINQLSEL----ADPLKDELNLADSEVD 617
Cdd:pfam15921 280 ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMrqlsDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSELT 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 618 SQKRGKQHYEDKQKEHMDTLNKKRRELDMKEKELQEKMSQARQICPERI-------EVKKSASILDKEINRLRQKIQA-E 689
Cdd:pfam15921 360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidHLRRELDDRNMEVQRLEALLKAmK 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 690 HASHGDREEIMKQYQ---EARETYLDLDSKVRTLRRFIKLLEEIMTHRYKTYQQFRRCLT 746
Cdd:pfam15921 440 SECQGQMERQMAAIQgknESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS 499
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
470-687 |
1.12e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 470 RDVDSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENieehQSVDIATL 549
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS----DLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 550 EDEAEENKIKMQMVEKNMEQQ-KENMENLKTLKIEAENKYDTIKL---KINQLSELADPLKDELNLADSEVdsqkrgkqh 625
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQkKENKKNIDKFLTEIKKKEKELEKlnnKYNDLKKQKEELENELNLLEKEK--------- 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782907 626 yeDKQKEHMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQ 687
Cdd:TIGR04523 183 --LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
456-728 |
1.16e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 456 RYYSSESTRPKFLSRDVDSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIREL 535
Cdd:TIGR00606 839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 536 ENIEEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENLKT--------LKIEAENKYDTIKLKINQLSELADPLKD 607
Cdd:TIGR00606 919 EKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEKHQEKINE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 608 ELNLADSEVDSQKRGKQHYEDKQkehmdTLNKKRRELDMKEKELQEKMSQARQIcpERIEVKKSASILDKEINRL----- 682
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQERWLQDNL-----TLRKRENELKEVEEELKQHLKEMGQM--QVLQMKQEHQKLEENIDLIkrnhv 1071
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1958782907 683 ----RQKIQAEHASHGDREEIMKQYQEARETYLDLDSKVRTLRRFIKLLE 728
Cdd:TIGR00606 1072 lalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
471-686 |
1.35e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 471 DVDSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKrcqlhykeikmkirKNISEIRELENIEEHQSVDIATLE 550
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNID--------------KFLTEIKKKEKELEKLNNKYNDLK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 551 DEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKInqlsELADPLKDELNladsevdsqkrgkqHYEDKQ 630
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKI----QKNKSLESQIS--------------ELKKQN 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1958782907 631 KEHMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKI 686
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKI 283
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
92-252 |
1.40e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 92 NEIEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEE---TNARAPECMA-LK--------- 158
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREeLGeraralyrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 159 ----------------TDVIARTRAFNDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKSTDQSLepERLERQKRIcwLK 222
Cdd:COG3883 99 ggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK--AELEAAKAE--LE 174
|
170 180 190
....*....|....*....|....*....|
gi 1958782907 223 EKVKALQDQENTVNQEVEQFEQAIEKDKQE 252
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-317 |
1.41e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 22 TQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERfqnIAGLSTMKTNLEYLKHEMawavvNEIEKQLNAI 101
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER---IKELEEKEERLEELKKKL-----KELEKRLEEL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 102 RDNIKIGEERAAKLDRK-----------MEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAFND 170
Cdd:PRK03918 358 EERHELYEEAKAKKEELerlkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 171 AEV------------LYNRSLNEYKALKKDGEQLCKRIEELKKSTdQSLEPErLERQKRICWLKEKVKALQDQENTVNqe 238
Cdd:PRK03918 438 CPVcgrelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKEL-RELEKV-LKKESELIKLKELAEQLKELEEKLK-- 513
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958782907 239 vEQFEQAIEKDKQEHVRIKREDVEVRHTLSYNQRQLKELKDSKTDRLkrfgphvpALLEAIDDAYRRRQFTHKPIGPLG 317
Cdd:PRK03918 514 -KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA--------ELEKKLDELEEELAELLKELEELG 583
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
519-740 |
1.46e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 519 KEIKMKIRKNISEIRELENIEEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQL 598
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 599 SELADPLKDELNLADSEVDSQKRGKQHYEDK---QKEHMDTLNKKRREL-----DMKEKELQEKMSQARQICPERIEVKK 670
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKvndIKEKVKNIHGYMKDIenkiqDGKDDYLKQKETELNTVNAQLEECEK 991
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 671 SASILDKEINRLRQKIQAEHAshgdREEIMKQYQEARETYLDLDSKVRTLRRFIKLLEEIMTHRYKTYQQ 740
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKI----QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
475-712 |
2.14e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 475 EISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIREL--ENIEEHQSVDIATLEDE 552
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKrdELNGELSAADAAVAKDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 553 AEENKI---KMQMVEKNMEQQKENMENLKTLKIEAEN-----------------KYDTIKLKINQlseladPLKDELNLA 612
Cdd:pfam12128 322 SELEALedqHGAFLDADIETAAADQEQLPSWQSELENleerlkaltgkhqdvtaKYNRRRSKIKE------QNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 613 DSEVDSQKRGKQ--------HYEDKQKEHMDTLNKKRRELDMKEKELQEKMSQAR------QICPERIEVKKsasILDKE 678
Cdd:pfam12128 396 KDKLAKIREARDrqlavaedDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKlrlnqaTATPELLLQLE---NFDER 472
|
250 260 270
....*....|....*....|....*....|....
gi 1958782907 679 INRLRQKIQAEHASHGDREEIMKQYQEARETYLD 712
Cdd:pfam12128 473 IERAREEQEAANAEVERLQSELRQARKRRDQASE 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-245 |
2.93e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 24 LEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLStmKTNLEYLKhemawavvneIEKQLNAIRD 103
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK--EKAEEYIK----------LSEFYEEYLD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 104 NIKIGEERAAKLDRKMEEQQVRLNDAEKKykdiQDKLEKISEETNARAPECMALKTDViartRAFNDAEVLYNRsLNEYK 183
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERH----ELYEEAKAKKEE-LERLK 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958782907 184 ALKKdgeqlCKRIEELKKSTDqSLEPERLERQKRICWLKEKVKALQDQENTVNQEVEQFEQA 245
Cdd:PRK03918 379 KRLT-----GLTPEKLEKELE-ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA 434
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
500-707 |
2.93e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 500 LEKD-IKRNEELLKRCQLHYKEIKMKIR---KNISEIREL--ENIEEHQSVdIATLEDEAEENK-IKMQM------VEKN 566
Cdd:PHA02562 171 LNKDkIRELNQQIQTLDMKIDHIQQQIKtynKNIEEQRKKngENIARKQNK-YDELVEEAKTIKaEIEELtdellnLVMD 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 567 MEQQKENMENLKTLKIEAENKYDTIKLKINQLSE------LADPLKDELNLADsevdsqkrgkqhyedKQKEHMDTLNKK 640
Cdd:PHA02562 250 IEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRIT---------------KIKDKLKELQHS 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958782907 641 RRELDMKEKELQEKMSQARQIcperievKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEAR 707
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEFNEQ-------SKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
470-712 |
4.33e-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: 41.19 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 470 RDVDSEISDLETEIENKKGHIMNLQHRLSALEKDIKRNEELlkrcqlhyKEIKMKIRKN---------ISEIRELENIEE 540
Cdd:TIGR01612 1361 KKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINL--------EECKSKIESTlddkdidecIKKIKELKNHIL 1432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 541 HQSVDIATLEDEAEENKIKMQMVEKNMEqqkenMENLKT---LKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVD 617
Cdd:TIGR01612 1433 SEESNIDTYFKNADENNENVLLLFKNIE-----MADNKSqhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAK 1507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 618 SQKRGKQHYEDKQKEHMDTLNKkrreldMKEKELQEKMSQArqicperievKKSASILDKEINRLRQKIQAEhasHGDRE 697
Cdd:TIGR01612 1508 AIEKNKELFEQYKKDVTELLNK------YSALAIKNKFAKT----------KKDSEIIIKEIKDAHKKFILE---AEKSE 1568
|
250
....*....|....*
gi 1958782907 698 EIMKQYQEARETYLD 712
Cdd:TIGR01612 1569 QKIKEIKKEKFRIED 1583
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
524-721 |
4.61e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 524 KIRKNISEI-RELENI-EEHQSVDiatLEDEAeenkikmQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSE- 600
Cdd:COG3206 186 ELRKELEEAeAALEEFrQKNGLVD---LSEEA-------KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDa 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 601 ----LADP----LKDELNLADSEVD--SQKRGKQHYEdkqkehMDTLNKKRRELD-MKEKELQEKMSQARQicpERIEVK 669
Cdd:COG3206 256 lpelLQSPviqqLRAQLAELEAELAelSARYTPNHPD------VIALRAQIAALRaQLQQEAQRILASLEA---ELEALQ 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1958782907 670 KSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARETYLDLDSKVRTLR 721
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
631-728 |
5.47e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 631 KEHMDTLNKKRRELDMKEKELQEKMSQARQicPERIEVKKSA--SILDKEINRLRQKIqaehashgdreeimkqyQEARE 708
Cdd:COG2433 426 EAEVEELEAELEEKDERIERLERELSEARS--EERREIRKDReiSRLDREIERLEREL-----------------EEERE 486
|
90 100
....*....|....*....|
gi 1958782907 709 TYLDLDSKVRTLRRFIKLLE 728
Cdd:COG2433 487 RIEELKRKLERLKELWKLEH 506
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-281 |
6.08e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 24 LEQMKEDYSYIMETKERTKEQINQGEERLTELkRQCLEKEERfqniagLSTMKTNLEYLKhemawavvnEIEKQLNaird 103
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELREL-EKVLKKESE------LIKLKELAEQLK---------ELEEKLK---- 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 104 niKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEetnarapecmaLKTDVIARTRAFNDAEVLYNRSLNEYK 183
Cdd:PRK03918 514 --KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE-----------LKKKLAELEKKLDELEEELAELLKELE 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 184 ALK-KDGEQLCKRIEELKKSTDQSLE----PERLER-QKRICWLKEKVKALQDQENTVNQEVEQFEQAIEK-----DKQE 252
Cdd:PRK03918 581 ELGfESVEELEERLKELEPFYNEYLElkdaEKELEReEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkySEEE 660
|
250 260
....*....|....*....|....*....
gi 1958782907 253 HVRIKREDVEVRHTLSYNQRQLKELKDSK 281
Cdd:PRK03918 661 YEELREEYLELSRELAGLRAELEELEKRR 689
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
487-725 |
6.38e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.20 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 487 KGHIMNLQHRLSALEKDIKRNEELLKRCQLHY----KEIKMKIRKNISE---------IRELENIEEHQS---VDIATLE 550
Cdd:PRK04778 197 REILDQLEEELAALEQIMEEIPELLKELQTELpdqlQELKAGYRELVEEgyhldhldiEKEIQDLKEQIDenlALLEELD 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 551 -DEAEEnkiKMQMVEKNMEQQKENMENLKTLKIEAENKYDTIKLKINQLSELADPLKDELnladsevdsqKRGKQHYEDK 629
Cdd:PRK04778 277 lDEAEE---KNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEI----------DRVKQSYTLN 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 630 QKEhmdtlNKKRRELdmkEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGD-REEIMKQYQ---E 705
Cdd:PRK04778 344 ESE-----LESVRQL---EKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKlSEMLQGLRKdelE 415
|
250 260
....*....|....*....|
gi 1958782907 706 ARETYLDLDSKVRTLRRFIK 725
Cdd:PRK04778 416 AREKLERYRNKLHEIKRYLE 435
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
546-729 |
7.00e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 546 IATLEDEAEE-NKIKMQMVEKNMEQQKENMENLKTLKIEAEnKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQ 624
Cdd:COG4717 48 LERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 625 HYEDKQKehMDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAehASHGDREEIMKQYQ 704
Cdd:COG4717 127 LLPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELE 202
|
170 180
....*....|....*....|....*
gi 1958782907 705 EARETYLDLDSKVRTLRRFIKLLEE 729
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEE 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-259 |
7.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 22 TQLEQMKEDYSYIMETK---ERTKEQInqgeERLTELKRQCLEKEERFQNIAGLSTMKTNLEYLKHEMAwavVNEIEKQL 98
Cdd:COG4913 225 EAADALVEHFDDLERAHealEDAREQI----ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR---LELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 99 NAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQ-DKLEkiseetnarapecmALKTDVIARTRAFNDAEvlynR 177
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLE--------------QLEREIERLERELEERE----R 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 178 SLNEYkalkkdgEQLCKRIEElkkstDQSLEPERLERQKRIcwLKEKVKALQDQENTVNQEVEQFEQAIEKDKQEHVRIK 257
Cdd:COG4913 360 RRARL-------EALLAALGL-----PLPASAEEFAALRAE--AAALLEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
..
gi 1958782907 258 RE 259
Cdd:COG4913 426 AE 427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
501-708 |
8.55e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 501 EKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATLEDE---AEENKIKMQMVEKNMEQQKENMENL 577
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEEKKKADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958782907 578 KtlKIEAENKYDTIKLKINQLSELADPLK--DELNLADSEVDSQKRGKQHYEDKQK-EHMDTLNKKRRELDMKEKELQEK 654
Cdd:PTZ00121 1405 K--KADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKaEEAKKKAEEAKKADEAKKKAEEA 1482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1958782907 655 mSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARE 708
Cdd:PTZ00121 1483 -KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
|
| |
