|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_SMC6_euk |
cd03276 |
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ... |
785-883 |
1.37e-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: 176.63 E-value: 1.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 785 NKASFNDMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQRFRQFILLTPQSMSSL 864
Cdd:cd03276 100 NKAAVRDVKTLSGGERSFSTVCLLLSLWEVMESPFRCLDEFDVFMDMVNRKISTDLLVKEAKKQPGRQFIFITPQDISGL 179
|
90
....*....|....*....
gi 1026346652 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 |
1.16e-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: 124.73 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 795 LSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSqrFRQFILLTPQSMSSLPSSKLIRILR 874
Cdd:cd03239 95 LSGGEKSLSALALIFALQEIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKH--TSQFIVITLKKEMFENADKLIGVLF 172
|
....*.
gi 1026346652 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 |
3.61e-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: 115.92 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 23 QLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNI-AGLSTMKTNLEYLKHEMAwavvnEIEKQLNAI 101
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqKELYALANEISRLEQQKQ-----ILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 102 RDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAFNDAEVLYNRSLNE 181
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 182 YKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKRicwLKEKVKALQDQEHTVNQEAEQFEQAIEKDKQEHGRVRKEDI 261
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKL---EEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 262 EVRHALNYNQRQLKELKdSKTDRLKRFGPHVPALLEAIDDAYRRRQFTHKPIGPLGACIHLrDPELALAIESCLKGLLQA 341
Cdd:TIGR02168 472 EAEQALDAAERELAQLQ-ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISV-DEGYEAAIEAALGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 342 YCCHNHADERVLQSLMKK-------FYPPGTSRPQIIVSefrdevyDVRLRAAYHPEFPTVLTALEIDNAVVANSLIDMR 414
Cdd:TIGR02168 550 VVVENLNAAKKAIAFLKQnelgrvtFLPLDSIKGTEIQG-------NDREILKNIEGFLGVAKDLVKFDPKLRKALSYLL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 415 SieTVLLIKNnsVARAVMQSQKPPKNCReAFTADGDQVFAG--RYYSSESTRPKFLSRDvdSEISDLETEIENKKGHIIT 492
Cdd:TIGR02168 623 G--GVLVVDD--LDNALELAKKLRPGYR-IVTLDGDLVRPGgvITGGSAKTNSSILERR--REIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 493 LQQRLSALEKDI--KRNEELLKRCQLHYKEIKM-------------------KIRKNISEIRELENIEEHQSVDIATLED 551
Cdd:TIGR02168 696 LEKALAELRKELeeLEEELEQLRKELEELSRQIsalrkdlarleaeveqleeRIAQLSKELTELEAEIEELEERLEEAEE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 552 EAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLK------------------------------------- 594
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEaanlrerleslerriaaterrledleeqieelsedie 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 595 -----INQLSELADPLKDELNLADSEVDSQKRG----KQHYEDKQKEhLDTLNKKRRELDMKEKELQEKMSQARQICpER 665
Cdd:TIGR02168 856 slaaeIEELEELIEELESELEALLNERASLEEAlallRSELEELSEE-LRELESKRSELRRELEELREKLAQLELRL-EG 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 666 IEVK---------------------------KSASILDKEINRLRQKIQA----EHASHGDREEIMKQYQEARETYLDLD 714
Cdd:TIGR02168 934 LEVRidnlqerlseeysltleeaealenkieDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYDFLTAQKEDLT 1013
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 715 NKVRTLRRFIKLLEEIMTHRYK-TYQQFRRCLTLRCKLYFDNllsQRAYCGKMNFDHKNET-LSITVQPGEGNKASfndM 792
Cdd:TIGR02168 1014 EAKETLEEAIEEIDREARERFKdTFDQVNENFQRVFPKLFGG---GEAELRLTDPEDLLEAgIEIFAQPPGKKNQN---L 1087
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1026346652 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 1026346652 795 LSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQrfRQFILLTPQSMSSLPSSKLIRILR 874
Cdd:cd03227 78 LSGGEKELSALALILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG--AQVIVITHLPELAELADKLIHIKK 155
|
...
gi 1026346652 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 |
7.81e-16 |
|
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: 82.42 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 9 KNEGDKYKFFMKATQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLSTMKTNLEYL--KHEM 86
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvKEKI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 87 A--WAVVNEIEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDViar 164
Cdd:TIGR02169 297 GelEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL--- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 165 trafNDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKR------ICWLKEKVKALQDQEHTVNQE 238
Cdd:TIGR02169 374 ----EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELadlnaaIAGIEAKINELEEEKEDKALE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 239 AEQFEQAIEKDKQEHGRVRKEDIEVRHALNYNQRQLKELK---DSKTDRLKRFGPHVPALLEAIDDAYRRRQFTHKPIGP 315
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQ 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 316 LGACihlrDPELALAIESCLKGLLQAYCCHNHADE-----------------------RVLQSLMKKFYPPGTSRPQIIV 372
Cdd:TIGR02169 530 LGSV----GERYATAIEVAAGNRLNNVVVEDDAVAkeaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 373 SEFRDE--------------VYDVRLRAAYHPEFPTVLTALEI--------------------------DNAVVANSLID 412
Cdd:TIGR02169 606 VEFDPKyepafkyvfgdtlvVEDIEAARRLMGKYRMVTLEGELfeksgamtggsraprggilfsrsepaELQRLRERLEG 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 413 MRSIETVLLIKNNSVARAVMQSQKPPKNC-REAFTADGDQVFAGRYYSSESTRPKflsrDVDSEISDLETEIENKKGHII 491
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDAsRKIGEIEKEIEQLEQEEEKLKERLE----ELEEDLSSLEQEIENVKSELK 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 492 TLQQRLSALEKDI------------KRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATLEDEAEENKIK 559
Cdd:TIGR02169 762 ELEARIEELEEDLhkleealndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 560 MQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELnladSEVDSQKRGKQHYEDKQKEHLDTLNK 639
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER----DELEAQLRELERKIEELEAQIEKKRK 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 640 KRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKeINRLRQKIQAEHASHGD-REEIMKQYQEARETYLDLDNKVR 718
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-VQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDELKEKRA 996
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 719 TLRR----FIKLLEEIMTHRYKTYQQFRRCLTLRCKLYFDNLLSQRAYCGKMNFDHK-NETLSITVQPgeGNKASfNDMR 793
Cdd:TIGR02169 997 KLEEerkaILERIEEYEKKKREVFMEAFEAINENFNEIFAELSGGTGELILENPDDPfAGGLELSAKP--KGKPV-QRLE 1073
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026346652 794 ALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQrfrQFILLT 857
Cdd:TIGR02169 1074 AMSGGEKSLTALSFIFAIQRYKPSPFYAFDEVDMFLDGVNVERVAKLIREKAGEA---QFIVVS 1134
|
|
| ABC_SMC5_euk |
cd03277 |
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ... |
796-873 |
7.02e-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: 74.55 E-value: 7.02e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1026346652 796 SGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQRFRQFILLTPQSMSSLPSSKLIRIL 873
Cdd:cd03277 128 SGGERSVSTMLYLLSLQELTRCPFRVVDEINQGMDPTNERKVFDMLVETACKEGTSQYFLITPKLLPGLNYHEKMTVL 205
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
470-729 |
7.21e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 470 RDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATL 549
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 550 EDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQ-------LSELADPLKDELNLADSEVDSQKRG 622
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEaeealleAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 623 KQHYEDKQKEHLDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQ 702
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260
....*....|....*....|....*..
gi 1026346652 703 YQEARETYLDLDNKVRTLRRFIKLLEE 729
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEA 501
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
475-722 |
3.14e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 475 EISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLkrcqlhyKEIKMKIRKNISEIRELENIEEHQSVDIATLEDEAE 554
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERR-------RELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 555 ENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKI-NQLSELADPLKDELNLADSEVDSQKRgKQHYEDKQKEH 633
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELlEALRAAAELAAQLEELEEAEEALLER-LERLEEELEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 634 LDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARETYLDL 713
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
....*....
gi 1026346652 714 DNKVRTLRR 722
Cdd:COG1196 507 LEGVKAALL 515
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
470-689 |
8.89e-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: 61.70 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 470 RDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATL 549
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 550 EDEA----EENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQH 625
Cdd:COG4942 110 LRALyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1026346652 626 YEDKQKEHLDTLNKKRRELDMKEKELQEKMSQARQicperievkksasiLDKEINRLRQKIQAE 689
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEE--------------LEALIARLEAEAAAA 239
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
5-841 |
4.02e-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: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 5 FLQSKNEGDKYKFFMKATQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLSTMKTNLEYLKH 84
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 85 EMAWAVVNE----IEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNArapecmALKTD 160
Cdd:pfam02463 292 AKEEEELKSellkLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE------LEKLQ 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 161 VIARTRAFNDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKRICWLKEKVKALQDQEHTVNQEAE 240
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 241 QFEQAIEKDKQEHGRVRKEDIEVRHALNYNQRQLKELKDSKTDRLKRF-GPHVPALLEAIDDAY---RRRQFTHKPIGPL 316
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQkLEERSQKESKARSGLkvlLALIKDGVGGRII 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 317 GACIHLRDPELALAIESCLKGLLQAYCCHNHADERVLQSLMKKFYPPGTSRPQIIVSEFRDE--------VYDVRLRAAY 388
Cdd:pfam02463 526 SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLklplksiaVLEIDPILNL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 389 HPEFPTVLTALEIDNAVVANSLIDMRSIETVL----------LIKNNSVARAVMQSQKPPKNCREAFTADGDQVFAGRYY 458
Cdd:pfam02463 606 AQLDKATLEADEDDKRAKVVEGILKDTELTKLkesakakesgLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 459 SSESTRPKFLSRDVD--SEISDLETEIENKKGHIITLQQRLSALEKD-----IKRNEELLKRCQLHYKEIKMKIRKNISE 531
Cdd:pfam02463 686 ESELAKEEILRRQLEikKKEQREKEELKKLKLEAEELLADRVQEAQDkineeLKLLKQKIDEEEEEEEKSRLKKEEKEEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 532 IRELENIEEHQSVDIA-----TLEDEAEENKIKMQMVEKNMEQQK----------ENMENLKSLKIEAENKYDTIKLKIN 596
Cdd:pfam02463 766 KSELSLKEKELAEEREkteklKVEEEKEEKLKAQEEELRALEEELkeeaelleeeQLLIEQEEKIKEEELEELALELKEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 597 QLSELADPLKDELNLADS--EVDSQKRGKQHYEDKQKEHLDTLNKKRRELDMKEKELQEKMSQARQ-------------- 660
Cdd:pfam02463 846 QKLEKLAEEELERLEEEItkEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLleekeneieerike 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 661 ----------------ICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARETYLDLDNKVRTLRRFI 724
Cdd:pfam02463 926 eaeillkyeeepeellLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 725 KLLEEIMTHRYKTYQQFRRCL----TLRCKLYFDNLLSQRAYCGKMNFDHK-NETLSITVQPGegnKASFNDMRALSGGE 799
Cdd:pfam02463 1006 KLIRAIIEETCQRLKEFLELFvsinKGWNKVFFYLELGGSAELRLEDPDDPfSGGIEISARPP---GKGVKNLDLLSGGE 1082
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1026346652 800 RSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMI 841
Cdd:pfam02463 1083 KTLVALALIFAIQKYKPAPFYLLDEIDAALDDQNVSRVANLL 1124
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
468-688 |
1.16e-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: 58.88 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 468 LSRDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIA 547
Cdd:TIGR04523 308 WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 548 TLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQHYE 627
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1026346652 628 DKQKEHLDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQA 688
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
9-584 |
1.26e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 9 KNEGDKYKFFMKATQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLSTMKTNLEYLkhemAW 88
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE----LL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 89 AVVNEIEKQLNAIrdnikigEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAF 168
Cdd:COG1196 295 AELARLEQDIARL-------EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 169 NDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKSTdQSLEPERLERQKRICWLKEKVKALQDQEHTVNQEAEQFEQAIEK 248
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 249 DKQEHGRVRKEDIEVRHALNYNQRQLKELKDSKTDRLKRFGPHVP---ALLEAIDDA---YRRRQFTHKPIGPLGACIHL 322
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAArllLLLEAEADYegfLEGVKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 323 R-----DPELALAIESCLKGLLQAYCCHNHADERVLQSLMKK-------FYPPGTSRPQIIVSEFRDEVYDVRLRAayhp 390
Cdd:COG1196 527 AvligvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagratFLPLDKIRARAALAAALARGAIGAAVD---- 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 391 efptvLTALEIDNAVVANSLIDMRSIETVLLIKNNSVARAVMQsqkppkncreafTADGDQVFAGRYYSSESTRPKFLSR 470
Cdd:COG1196 603 -----LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV------------TLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 471 DVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATLE 550
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
570 580 590
....*....|....*....|....*....|....
gi 1026346652 551 DEAEENKIKMQMVEKNMEQQKENMENLKSlKIEA 584
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERLER-EIEA 778
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
473-660 |
1.68e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 473 DSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELE-NIEEHQsvdiATLED 551
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEaEIEERR----EELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 552 EAEENKI----------------------KMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDEL 609
Cdd:COG3883 91 RARALYRsggsvsyldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1026346652 610 NLADSEVDSQKRGKQHYEDKQKEHLDTLNKKRRELDMKEKELQEKMSQARQ 660
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
476-721 |
1.69e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 476 ISDLETEIEnkkghiitlqQRLSALEKD---------IKRNEELLKRCQ--LHYKEIKMKIRKNISEIRELENIEEHQSV 544
Cdd:COG1196 191 LEDILGELE----------RQLEPLERQaekaeryreLKEELKELEAELllLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 545 DIATLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQ 624
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 625 HYEDKQKEHLDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQ 704
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250
....*....|....*..
gi 1026346652 705 EARETYLDLDNKVRTLR 721
Cdd:COG1196 421 EELEELEEALAELEEEE 437
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
482-729 |
2.75e-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: 53.61 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 482 EIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENieehqsvDIATLEDEAEENKIKMQ 561
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ-------ELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 562 MVEKNMEQQKENMENLkslkieaenkydtikLKINQLSELADPLKDELNlADSEVDSQKRGK--QHYEDKQKEHLDTLNK 639
Cdd:COG4942 94 ELRAELEAQKEELAEL---------------LRALYRLGRQPPLALLLS-PEDFLDAVRRLQylKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 640 KRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEaretylDLDNKVRT 719
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE------ELEALIAR 231
|
250
....*....|
gi 1026346652 720 LRRFIKLLEE 729
Cdd:COG4942 232 LEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
495-729 |
4.45e-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: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 495 QRLSALEKDIKRNEELLKR---CQLHYKEIKmkirkniSEIRELEnieehqsVDIATLEDEAEENKIKMQMVEKNMEQQK 571
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERqaeKAERYKELK-------AELRELE-------LALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 572 enMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQHYedkqkehldtlNKKRRELDMKEKEL 651
Cdd:TIGR02168 255 --LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL-----------RERLANLERQLEEL 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1026346652 652 QEKMSQARQicpERIEVKKSASILDKEINRLRQKIQAEHASHgdrEEIMKQYQEARETYLDLDNKVRTLRRFIKLLEE 729
Cdd:TIGR02168 322 EAQLEELES---KLDELAEELAELEEKLEELKEELESLEAEL---EELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
519-729 |
2.05e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.55 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 519 KEIKMKIRKNISEIRELENieehqSVDIAtledeaeENKIKMQmvEKNM-EQQKENMENLKslkiEAENKYDTIKLKINQ 597
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDM-----KIDHI-------QQQIKTY--NKNIeEQRKKNGENIA----RKQNKYDELVEEAKT 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 598 LSELADPLKDELnladSEVDSQKrgkqhyeDKQKEHLDTLNKKRRELDMKEKELQ--EKMSQARQICP----------ER 665
Cdd:PHA02562 232 IKAEIEELTDEL----LNLVMDI-------EDPSAALNKLNTAAAKIKSKIEQFQkvIKMYEKGGVCPtctqqisegpDR 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1026346652 666 I-EVKKSASILDKEINRLRQKIQAEhashgdrEEIMKQYQEARETYLDLDNKVRTLRRFIKLLEE 729
Cdd:PHA02562 301 ItKIKDKLKELQHSLEKLDTAIDEL-------EEIMDEFNEQSKKLLELKNKISTNKQSLITLVD 358
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
470-731 |
6.85e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 470 RDVDSEISDLET---EIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDI 546
Cdd:PRK03918 217 PELREELEKLEKevkELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 547 aTLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKydtiKLKINQLSELADPLKDELNLADSEVDSQKRGKQhy 626
Cdd:PRK03918 297 -KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERHELYEEAKA-- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 627 edkQKEHLDTLNKKR--RELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHG---------- 694
Cdd:PRK03918 370 ---KKEELERLKKRLtgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGkcpvcgrelt 446
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1026346652 695 --DREEIMKQY----QEARETYLDLDNKVRTLRRFIKLLEEIM 731
Cdd:PRK03918 447 eeHRKELLEEYtaelKRIEKELKEIEEKERKLRKELRELEKVL 489
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-850 |
1.18e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 49 EERLTELKRQClEKEERFQNIaglstmKTNLEYLKHEMAWAVVNEIEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLND 128
Cdd:COG1196 199 ERQLEPLERQA-EKAERYREL------KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 129 AEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAFNDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKStDQSLE 208
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE-LEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 209 PERLERQKRICWLKEKVKALQDQEHTVNQEAEQFEQAIEKDKQEHGRVRKEDIEVRHALNYNQRQLKELKDSKTDRLKRF 288
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 289 GPHVPALLEAIDDAYRRRQFthkpigplgaciHLRDPELALAIESCLKGLLQAYCCHNHADERVLQSLMKKfyppgtsRP 368
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEE------------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-------AA 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 369 QIIVSEfrdevydvRLRAAYHPEFPTVLTALEIDN-AVVANSLIDMRSIETVLLIKNNSVARAVMQsqkpPKNCREAFTA 447
Cdd:COG1196 492 RLLLLL--------EAEADYEGFLEGVKAALLLAGlRGLAGAVAVLIGVEAAYEAALEAALAAALQ----NIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 448 DGDQVFAGRyysSESTRPKFLSRDVDSEISDLEteienkkghiitLQQRLSALEKDIKRNEELLKRCQLHYKEIkmkiRK 527
Cdd:COG1196 560 AAAIEYLKA---AKAGRATFLPLDKIRARAALA------------AALARGAIGAAVDLVASDLREADARYYVL----GD 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 528 NISEIRELENIEEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKydtIKLKINQLSELADPLKD 607
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE---LEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 608 ELNLADSEVDSQKRGKQHYEDKQKEHLDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQ 687
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 688 A----------EHashgdrEEIMKQYQEARETYLDLDNKVRTLRRFIKLLEEIMTHRYK-TYQQ--------FRR----- 743
Cdd:COG1196 778 AlgpvnllaieEY------EELEERYDFLSEQREDLEEARETLEEAIEEIDRETRERFLeTFDAvnenfqelFPRlfggg 851
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 744 --CLTLRCKlyfDNLLSqrayCGkmnfdhknetLSITVQPGeGNKASfnDMRALSGGERSFSTVCFILSLWSIAESPFrC 821
Cdd:COG1196 852 eaELLLTDP---DDPLE----TG----------IEIMAQPP-GKKLQ--RLSLLSGGEKALTALALLFAIFRLNPSPF-C 910
|
810 820 830
....*....|....*....|....*....|.
gi 1026346652 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 |
1.33e-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: 46.69 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 766 MNFDHKNETLSITVQ---------PGEGNKasfnDMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVN-RR 835
Cdd:cd03278 80 LTFDNSDGRYSIISQgdvseiieaPGKKVQ----RLSLLSGGEKALTALALLFAIFRVRPSPFCVLDEVDAALDDANvER 155
|
90 100
....*....|....*....|..
gi 1026346652 836 IAmDMILKMADSQrfrQFILLT 857
Cdd:cd03278 156 FA-RLLKEFSKET---QFIVIT 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
471-621 |
1.46e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 471 DVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQlhyKEIKMKIR------------------KNISE- 531
Cdd:COG3883 41 ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR---EELGERARalyrsggsvsyldvllgsESFSDf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 532 ---IRELENIEEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDE 608
Cdd:COG3883 118 ldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQ 197
|
170
....*....|...
gi 1026346652 609 LNLADSEVDSQKR 621
Cdd:COG3883 198 LAELEAELAAAEA 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-286 |
1.78e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 22 TQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNI----AGLSTMKTNLEYLKHEmawavVNEIEKQ 97
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELreelEKLEKEVKELEELKEE-----IEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 98 LNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQdKLEKISEETNarapECMALKTDVIARTRAFNDAEVLYNR 177
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYI----KLSEFYEEYLDELREIEKRLSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 178 SLNEYKALKKDGEQLCKRIEELKKstdqslepERLERQKRICWLKEKVKALQDQEHTVNQ----EAEQFEQAIEKDKQEH 253
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKK--------KLKELEKRLEELEERHELYEEAKAKKEElerlKKRLTGLTPEKLEKEL 393
|
250 260 270
....*....|....*....|....*....|...
gi 1026346652 254 GRVRKEDIEVRHALNYNQRQLKELKDSKTDRLK 286
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
471-725 |
3.33e-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: 47.54 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 471 DVDSEISDLETEIEN-----KKGHIITLQQRLSALEKDIKRNEELLKRCQlhyKEIKMKIRKNISEIRELENieehQSVD 545
Cdd:pfam06160 157 EIEEEFSQFEELTESgdyleAREVLEKLEEETDALEELMEDIPPLYEELK---TELPDQLEELKEGYREMEE----EGYA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 546 IATLEDEAEENKIKmqmveknmEQQKENMENLKSLKI-EAENKYDTIKLKINQLSELadpLKDELNlADSEVDSQKRGKQ 624
Cdd:pfam06160 230 LEHLNVDKEIQQLE--------EQLEENLALLENLELdEAEEALEEIEERIDQLYDL---LEKEVD-AKKYVEKNLPEIE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 625 HYEDKQKEHLDTLNKKRRELDMK--------------EKELQEKMSQARQICPERIEVKKSASILDKEINRLRQ---KIQ 687
Cdd:pfam06160 298 DYLEHAEEQNKELKEELERVQQSytlnenelervrglEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEqleEIE 377
|
250 260 270
....*....|....*....|....*....|....*....
gi 1026346652 688 AEHASHGDR-EEIMKQYQEARETYLDLDNKVRTLRRFIK 725
Cdd:pfam06160 378 EEQEEFKESlQSLRKDELEAREKLDEFKLELREIKRLVE 416
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
494-743 |
3.42e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 494 QQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQS--VDIATLEDEAEENKIKMQMVEKNMEQqk 571
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdeIDVASAEREIAELEAELERLDASSDD-- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 572 enMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQHYEDKQKEHLDT-LNKKRRELDMK--E 648
Cdd:COG4913 687 --LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDavE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 649 KELQEKMSQARQicperievkksasILDKEINRLRQKIqaehashgdrEEIMKQYQEA-RETYLDLDNKVRTLRRFIKLL 727
Cdd:COG4913 765 RELRENLEERID-------------ALRARLNRAEEEL----------ERAMRAFNREwPAETADLDADLESLPEYLALL 821
|
250
....*....|....*....
gi 1026346652 728 EEIMT---HRYKtyQQFRR 743
Cdd:COG4913 822 DRLEEdglPEYE--ERFKE 838
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
470-597 |
4.24e-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: 46.07 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 470 RDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIrKNISEIRELENIE---EHQSVDI 546
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-GNVRNNKEYEALQkeiESLKRRI 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1026346652 547 ATLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQ 597
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
470-731 |
6.31e-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: 46.94 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 470 RDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENieehqsvdiatl 549
Cdd:TIGR04523 443 KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEE------------ 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 550 edeaeenkiKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSEL--ADPLKDELNLADSEVDSQKRGKQHYE 627
Cdd:TIGR04523 511 ---------KVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLK 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 628 DKQKEHLDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKiqaEHASHGDREEIMKQYQEAR 707
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSK---KNKLKQEVKQIKETIKEIR 658
|
250 260
....*....|....*....|....
gi 1026346652 708 ETYLDLDNKVRTLRRFIKLLEEIM 731
Cdd:TIGR04523 659 NKWPEIIKKIKESKTKIDDIIELM 682
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
469-705 |
7.39e-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: 46.97 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 469 SRDVDSEISDLETEIENKKGHIItlqqrlSALEKDIKRNEELLKrcqlhyKEIKMKIRKNISEIRELENIEEHQSVDIAT 548
Cdd:TIGR01612 1035 IEDANKNIPNIEIAIHTSIYNII------DEIEKEIGKNIELLN------KEILEEAEINITNFNEIKEKLKHYNFDDFG 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 549 LEDEA----EENKIKMQMveKNMEQQ-KENMENLKSLKIEAENKYDTIKLKINQLSELADplKDELNLADSEVDSQKRGK 623
Cdd:TIGR01612 1103 KEENIkyadEINKIKDDI--KNLDQKiDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD--KAISNDDPEEIEKKIENI 1178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 624 QHYEDKQKEHLDTLNKKRRELDMKEKElQEKMSQARQIcpeRIEVKKSASIL-----DKEINRLRQKIQAEHASHGDREE 698
Cdd:TIGR01612 1179 VTKIDKKKNIYDEIKKLLNEIAEIEKD-KTSLEEVKGI---NLSYGKNLGKLflekiDEEKKKSEHMIKAMEAYIEDLDE 1254
|
....*..
gi 1026346652 699 IMKQYQE 705
Cdd:TIGR01612 1255 IKEKSPE 1261
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
497-731 |
9.18e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 497 LSALEKDIKRNEELLKRCQLHYKEIKMKI---------RKNISEIRELEniEEHQSVDIATLEDEAEE--------NKIK 559
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLkkeseliklKELAEQLKELE--EKLKKYNLEELEKKAEEyeklkeklIKLK 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 560 MQMveKNMEQQKENMENLKSLKIEAENKYDTIKlkinqlSELADPLKDELNLADSEVDSQKRGKQHYEDKQKEHLdTLNK 639
Cdd:PRK03918 539 GEI--KSLKKELEKLEELKKKLAELEKKLDELE------EELAELLKELEELGFESVEELEERLKELEPFYNEYL-ELKD 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 640 KRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEhashgDREEIMKQYQEARETYLDLDNKVRT 719
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE-----EYEELREEYLELSRELAGLRAELEE 684
|
250
....*....|..
gi 1026346652 720 LRrfiKLLEEIM 731
Cdd:PRK03918 685 LE---KRREEIK 693
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
471-653 |
1.36e-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: 45.78 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 471 DVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKrcqlhykeikmkirKNISEIRELENIEEHQSVDIATLE 550
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNID--------------KFLTEIKKKEKELEKLNNKYNDLK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 551 DEAEENKIKMQMVEKNMEQQKENMENLKS---------LKIEAEN-KYDTIKLKINQLSELADPLKDELNLADSEVDSQK 620
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNkllklelllSNLKKKIqKNKSLESQISELKKQNNQLKDNIEKKQQEINEKT 245
|
170 180 190
....*....|....*....|....*....|...
gi 1026346652 621 RGKQHYEDKQKEHLDTLNKKRRELDMKEKELQE 653
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
43-276 |
1.50e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 43 EQINQGEERLTELKRQCLEKEERFQNIAglstmktnleylkhemawAVVNEIEKQLNAIRDNIKIGEERAAKLDRKMEEQ 122
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK------------------KEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 123 QVRLNDAEKKYKDIQDKLEKISEETNARAPECMAL----KTDVIARTRAFNDAEVL--YNRSLNEykALKKDGEQLCKRI 196
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLgrqpPLALLLSPEDFLDAVRRlqYLKYLAP--ARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 197 EELKKSTdQSLEPERLERQKRICWLKEKVKALQDQEHTVNQEAEQFEQAIEKDKQEHGRVRKEDIEVRHALNYNQRQLKE 276
Cdd:COG4942 160 AELAALR-AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
457-730 |
1.56e-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: 45.40 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 457 YYSSESTRPKFLSRDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELE 536
Cdd:TIGR04523 142 KFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQIS 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 537 NIEEHQSvdiaTLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELNLADSEV 616
Cdd:TIGR04523 222 ELKKQNN----QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 617 DSQKrgkqhyedKQKEHlDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLR---QKIQAEHASH 693
Cdd:TIGR04523 298 SDLN--------NQKEQ-DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEK 368
|
250 260 270
....*....|....*....|....*....|....*...
gi 1026346652 694 GDR-EEIMKQYQEARETYLDLDNKVRTLRRFIKLLEEI 730
Cdd:TIGR04523 369 QNEiEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
475-615 |
1.69e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 475 EISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQL-----HYKEIKMKIRKNISEIRELENIEEHQSVDIATL 549
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaelaELPERLEELEERLEELRELEEELEELEAELAEL 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1026346652 550 EDEAEENKIKM-QMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELNLADSE 615
Cdd:COG4717 176 QEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
791-857 |
2.85e-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: 2.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1026346652 791 DMRALSGGERSFSTVCFILSLWSIAESPFRCLDEFDVYMDMVNRRIAMDMILKMADSQrfrQFILLT 857
Cdd:cd03272 155 EMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGA---QFITTT 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
471-718 |
4.50e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 471 DVDSEISDLETEIEnkkghiiTLQQRLSALEKDIKRNEELlKRCQLHYKEIKMKiRKNISE-IRELENIEEHQSVDIATL 549
Cdd:PRK02224 472 EDRERVEELEAELE-------DLEEEVEEVEERLERAEDL-VEAEDRIERLEER-REDLEElIAERRETIEEKRERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 550 EDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELNLAD--SEVDSQKRGKQHYE 627
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDeiERLREKREALAELN 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 628 DKQKEHLDTLNKKRRELDMKE-----KELQEKMSQA-----------RQICPERIEVKKSASILDKEINR---LRQKIQA 688
Cdd:PRK02224 623 DERRERLAEKRERKRELEAEFdeariEEAREDKERAeeyleqveeklDELREERDDLQAEIGAVENELEEleeLRERREA 702
|
250 260 270
....*....|....*....|....*....|
gi 1026346652 689 EHASHGDREEIMKQYQEARETYLDLDNKVR 718
Cdd:PRK02224 703 LENRVEALEALYDEAEELESMYGDLRAELR 732
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-278 |
6.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 83 KHEMAWAVVNEIEKQLNAIRDNikigEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEETNARAP--ECMALKTD 160
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 161 VIARTRAFNDAEvlynRSLNEYKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKRICWLKEKVKALQDQEHTVNQEAE 240
Cdd:COG4717 141 LAELPERLEELE----ERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190
....*....|....*....|....*....|....*...
gi 1026346652 241 QFEQAIEKDKQEhgrvrKEDIEVRHALNYNQRQLKELK 278
Cdd:COG4717 217 EAQEELEELEEE-----LEQLENELEAAALEERLKEAR 249
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
456-728 |
7.10e-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: 43.50 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 456 RYYSSESTRPKFLSRDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIREL 535
Cdd:TIGR00606 839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFL 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 536 ENIEEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENLKS--------LKIEAENKYDTIKLKINQLSELADPLKD 607
Cdd:TIGR00606 919 EKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENkiqdgkddYLKQKETELNTVNAQLEECEKHQEKINE 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 608 ELNLADSEVDSQKRGKQHYEDKQkehldTLNKKRRELDMKEKELQEKMSQARQIcpERIEVKKSASILDKEINRL----- 682
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQERWLQDNL-----TLRKRENELKEVEEELKQHLKEMGQM--QVLQMKQEHQKLEENIDLIkrnhv 1071
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1026346652 683 ----RQKIQAEHASHGDREEIMKQYQEARETYLDLDNKVRTLRRFIKLLE 728
Cdd:TIGR00606 1072 lalgRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELVNKDLD 1121
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
470-746 |
7.80e-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: 43.18 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 470 RDVDSEIS----DLETEIENKKGHIITLQQRLSALEKDIKRNEELLkrCQLHYKEIKmkirkniseirelENIEEHQsVD 545
Cdd:pfam15921 216 RSLGSAISkilrELDTEISYLKGRIFPVEDQLEALKSESQNKIELL--LQQHQDRIE-------------QLISEHE-VE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 546 IATLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKI----EAENKYDTIKLKINQLSEL----ADPLKDELNLADSEVD 617
Cdd:pfam15921 280 ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMrqlsDLESTVSQLRSELREAKRMyedkIEELEKQLVLANSELT 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 618 SQKRGKQHYEDKQKEHLDTLNKKRRELDMKEKELQEKMSQARQICPERI-------EVKKSASILDKEINRLRQKIQA-E 689
Cdd:pfam15921 360 EARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitidHLRRELDDRNMEVQRLEALLKAmK 439
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 690 HASHGDREEIMKQYQ---EARETYLDLDNKVRTLRRFIKLLEEIMTHRYKTYQQFRRCLT 746
Cdd:pfam15921 440 SECQGQMERQMAAIQgknESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS 499
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
470-718 |
1.45e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 470 RDVDSEISDLeteiENKKGHIitlQQRLSALEKDIKRNEELLKRCQLHYKEikmKIRKNISEIRELENieehqsvDIATL 549
Cdd:PHA02562 177 RELNQQIQTL----DMKIDHI---QQQIKTYNKNIEEQRKKNGENIARKQN---KYDELVEEAKTIKA-------EIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 550 EDEAEEnkikmqmVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSE------LADPLKDELNLADSEVDSQKRGK 623
Cdd:PHA02562 240 TDELLN-------LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 624 QHYEdKQKEHLDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLrqkiQAEHASHgdREEIMKQY 703
Cdd:PHA02562 313 HSLE-KLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL----QAEFVDN--AEELAKLQ 385
|
250
....*....|....*
gi 1026346652 704 QEARETYLDLDNKVR 718
Cdd:PHA02562 386 DELDKIVKTKSELVK 400
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
26-283 |
1.57e-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: 42.40 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 26 QMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLStmktnleylkhEMAWAVVNEIEKQLNAIRDNI 105
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLL-----------EESRDKANQLEEKTKLQDENL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 106 KIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLE-------KISEETNARAPECMALKTDVIARTRAFNDAEVLYNRS 178
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 179 L-NEYKALKKDGEQLCKRIEELKKSTDQSLEPERLERQKRICWlkEKVKALQDQEHTVNQEAEQFEQAIEKDK------- 250
Cdd:pfam05483 365 LrTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL--EELKKILAEDEKLLDEKKQFEKIAEELKgkeqeli 442
|
250 260 270
....*....|....*....|....*....|....*..
gi 1026346652 251 ----QEHGRVRKEDIEVRHALNYNQRQLKELKDSKTD 283
Cdd:pfam05483 443 fllqAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
519-740 |
1.96e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 519 KEIKMKIRKNISEIRELENIEEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQL 598
Cdd:TIGR00606 832 QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 599 SELADPLKDELNLADSEVDSQKRGKQHYEDK---QKEHLDTLNKKRREL-----DMKEKELQEKMSQARQICPERIEVKK 670
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKvndIKEKVKNIHGYMKDIenkiqDGKDDYLKQKETELNTVNAQLEECEK 991
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 671 SASILDKEINRLRQKIQAEHAshgdREEIMKQYQEARETYLDLDNKVRTLRRFIKLLEEIMTHRYKTYQQ 740
Cdd:TIGR00606 992 HQEKINEDMRLMRQDIDTQKI----QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
24-283 |
1.98e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 24 LEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERFQNIAGLStmKTNLEYLKhemawavvneIEKQLNAIRD 103
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK--EKAEEYIK----------LSEFYEEYLD 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 104 NIKIGEERAAKLDRKMEEQQVRLNDAEKKykdiQDKLEKISEETNARAPECMALKTDViartRAFNDAEVLYNRsLNEYK 183
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEERH----ELYEEAKAKKEE-LERLK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 184 ALKKdgeqlCKRIEELKKSTDqSLEPERLERQKRICWLKEKVKALqdqehtvNQEAEQFEQAIEKDKQEHGR--VRKEDI 261
Cdd:PRK03918 379 KRLT-----GLTPEKLEKELE-ELEKAKEEIEEEISKITARIGEL-------KKEIKELKKAIEELKKAKGKcpVCGREL 445
|
250 260
....*....|....*....|..
gi 1026346652 262 EVRHALNYNQRQLKELKDSKTD 283
Cdd:PRK03918 446 TEEHRKELLEEYTAELKRIEKE 467
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
471-666 |
2.14e-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: 40.68 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 471 DVDSEISDLETEIENkkghiitLQQRLSALEKDIKRNEELLKRCQLHYKEIKmkirkniSEIRELENieehqsvDIATLE 550
Cdd:COG1579 14 ELDSELDRLEHRLKE-------LPAELAELEDELAALEARLEAAKTELEDLE-------KEIKRLEL-------EIEEVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 551 DEAEENKIKMQMVEKNMEQ---QKEnMENLKSLKIEAENkydtiklKINQLSELADPLKDELNLADSEVDSQkrgKQHYE 627
Cdd:COG1579 73 ARIKKYEEQLGNVRNNKEYealQKE-IESLKRRISDLED-------EILELMERIEELEEELAELEAELAEL---EAELE 141
|
170 180 190
....*....|....*....|....*....|....*....
gi 1026346652 628 DKQKEhldtLNKKRRELDMKEKELQEKMSQARQICPERI 666
Cdd:COG1579 142 EKKAE----LDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
469-729 |
2.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 469 SRDVDSEISDLETEIENkkghiitLQQRLSALEKDIKRNEELLKRcqlhYKEIKmkirkniseiRELENIEEHQSVDIAT 548
Cdd:PRK03918 309 LREIEKRLSRLEEEING-------IEERIKELEEKEERLEELKKK----LKELE----------KRLEELEERHELYEEA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 549 LEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLselaDPLKDELNLADSEVDSQKR-----GK 623
Cdd:PRK03918 368 KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL----KKEIKELKKAIEELKKAKGkcpvcGR 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 624 QHYEDKQKEhldTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASiLDKEINRLRQ------KIQAEHASHG--D 695
Cdd:PRK03918 444 ELTEEHRKE---LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK-KESELIKLKElaeqlkELEEKLKKYNleE 519
|
250 260 270
....*....|....*....|....*....|....
gi 1026346652 696 REEIMKQYQEARETYLDLDNKVRTLRRFIKLLEE 729
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
530-710 |
2.98e-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: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 530 SEIRELENIEEHQSVDIATLEDEAEEnkikmqmVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKD-- 607
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAA-------LEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 608 ELNLADSEVDSQKRGKQHYEDKQKEHLDtlnkkrrELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQ 687
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELME-------RIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|....*
gi 1026346652 688 AEHASHGDR--EEIMKQYQEARETY 710
Cdd:COG1579 163 AEREELAAKipPELLALYERIRKRK 187
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
22-317 |
3.53e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 22 TQLEQMKEDYSYIMETKERTKEQINQGEERLTELKRQCLEKEERfqnIAGLSTMKTNLEYLKHEMawavvNEIEKQLNAI 101
Cdd:PRK03918 286 KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER---IKELEEKEERLEELKKKL-----KELEKRLEEL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 102 RDNIKIGEERAAKLDRK-----------MEEQQVRLNDAEKKYKDIQDKLEKISEETNARAPECMALKTDVIARTRAFND 170
Cdd:PRK03918 358 EERHELYEEAKAKKEELerlkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 171 AEV------------LYNRSLNEYKALKKDGEQLCKRIEELKKSTdQSLEPErLERQKRICWLKEKVKALQDQEHTVNqe 238
Cdd:PRK03918 438 CPVcgrelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKEL-RELEKV-LKKESELIKLKELAEQLKELEEKLK-- 513
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1026346652 239 aEQFEQAIEKDKQEHGRVRKEDIEVRHALNYNQRQLKELKDSKTDRLkrfgphvpALLEAIDDAYRRRQFTHKPIGPLG 317
Cdd:PRK03918 514 -KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA--------ELEKKLDELEEELAELLKELEELG 583
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
92-252 |
3.58e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 92 NEIEKQLNAIRDNIKIGEERAAKLDRKMEEQQVRLNDAEKKYKDIQDKLEKISEE---TNARAPECMA-LK--------- 158
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREeLGeraralyrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 159 ----------------TDVIARTRAFNDAEVLYNRSLNEYKALKKDGEQLCKRIEELKKSTDQ---SLEPERLERQKRIC 219
Cdd:COG3883 99 ggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAlkaELEAAKAELEAQQA 178
|
170 180 190
....*....|....*....|....*....|...
gi 1026346652 220 WLKEKVKALQDQEHTVNQEAEQFEQAIEKDKQE 252
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
546-729 |
3.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 546 IATLEDEAEE-NKIKMQMVEKNMEQQKENMENLKSLKIEAEnKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRGKQ 624
Cdd:COG4717 48 LERLEKEADElFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 625 HYEDKQKehLDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAehASHGDREEIMKQYQ 704
Cdd:COG4717 127 LLPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL--ATEEELQDLAEELE 202
|
170 180
....*....|....*....|....*
gi 1026346652 705 EARETYLDLDNKVRTLRRFIKLLEE 729
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEE 227
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
470-687 |
5.05e-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: 40.77 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 470 RDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENieehQSVDIATL 549
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS----DLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 550 EDEAEENKIKMQMVEKNMEQQ-KENMENLKSLKIEAENKYDTIKL---KINQLSELADPLKDELNLADSEVdsqkrgkqh 625
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQkKENKKNIDKFLTEIKKKEKELEKlnnKYNDLKKQKEELENELNLLEKEK--------- 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1026346652 626 yeDKQKEHLDTLNKKRRELDMKEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQ 687
Cdd:TIGR04523 183 --LNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
501-708 |
5.06e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 501 EKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENIEEHQSVDIATLEDE---AEENKIKMQMVEKNMEQQKENMENL 577
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkkkADAAKKKAEEKKKADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 578 KslKIEAENKYDTIKLKINQLSELADPLK--DELNLADSEVDSQKRGKQHYEDKQK-EHLDTLNKKRRELDMKEKELQEK 654
Cdd:PTZ00121 1405 K--KADELKKAAAAKKKADEAKKKAEEKKkaDEAKKKAEEAKKADEAKKKAEEAKKaEEAKKKAEEAKKADEAKKKAEEA 1482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1026346652 655 mSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARE 708
Cdd:PTZ00121 1483 -KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
36-293 |
6.06e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.24 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 36 ETKERTKE---QINQGEERLTELKRQclEKEERFQNIAGLSTMKTNLEYLKHEMAWAVVNEIEKqlNAIRDNIKIGEERA 112
Cdd:pfam02029 81 EALERQKEfdpTIADEKESVAERKEN--NEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQE--NKWSTEVRQAEEEG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 113 AKLDRKMEEQQVRLNDAEKKY--KDIQDKLEKISEETNARAPECMALKTDVIARTRAFNDAEVLYN-----RSLNEYKAL 185
Cdd:pfam02029 157 EEEEDKSEEAEEVPTENFAKEevKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTtkrrqGGLSQSQER 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 186 KKDGEQLC---KRIEELKKSTD----QSLEPERLERQKRICWLKEkVKALQDQEHTVNQEAEQFEQAIEKDKQ----EHG 254
Cdd:pfam02029 237 EEEAEVFLeaeQKLEELRRRRQekesEEFEKLRQKQQEAELELEE-LKKKREERRKLLEEEEQRRKQEEAERKlreeEEK 315
|
250 260 270
....*....|....*....|....*....|....*....
gi 1026346652 255 RVRKEDIEVRHALNYNQRQlKELKDSKTDRLKRFGPHVP 293
Cdd:pfam02029 316 RRMKEEIERRRAEAAEKRQ-KLPEDSSSEGKKPFKCFSP 353
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
501-681 |
6.41e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 501 EKDIKRNEELLKRCQLHYKEIKMKIRKNISEIRELENI---EEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENL 577
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELkkaEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 578 KSlKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVDSQKRgKQHYEDKQKEHLDTLNKKRRELDMKEKELQEKMSQ 657
Cdd:PTZ00121 1695 KK-EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK-EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
170 180
....*....|....*....|....*.
gi 1026346652 658 ARQICPERIE--VKKSASILDKEINR 681
Cdd:PTZ00121 1773 IRKEKEAVIEeeLDEEDEKRRMEVDK 1798
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
631-728 |
6.43e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 631 KEHLDTLNKKRRELDMKEKELQEKMSQARQicPERIEVKKSA--SILDKEINRLRQKIqaehashgdreeimkqyQEARE 708
Cdd:COG2433 426 EAEVEELEAELEEKDERIERLERELSEARS--EERREIRKDReiSRLDREIERLEREL-----------------EEERE 486
|
90 100
....*....|....*....|
gi 1026346652 709 TYLDLDNKVRTLRRFIKLLE 728
Cdd:COG2433 487 RIEELKRKLERLKELWKLEH 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
508-727 |
6.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 508 EELLKRCQLHYKEIKMKIRKNISEIRELEnieehqsVDIATLEDEAEENKIKmqmvEKNMEQQKENMENLKSLKIEAENK 587
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELE-------EELKEAEEKEEEYAEL----QEELEELEEELEELEAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 588 YDTIKLKINQLSELADP--LKDELNLADSEVDSQKRGKQHYEDKQKEhldtLNKKRRELDMKEKELQEKMSQARQICPER 665
Cdd:COG4717 118 LEKLEKLLQLLPLYQELeaLEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1026346652 666 IE-VKKSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARETyLDLDNKVRTLRRFIKLL 727
Cdd:COG4717 194 LQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA-AALEERLKEARLLLLIA 255
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
524-721 |
7.37e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 524 KIRKNISEI-RELENI-EEHQSVDiatLEDEAeenkikmQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSE- 600
Cdd:COG3206 186 ELRKELEEAeAALEEFrQKNGLVD---LSEEA-------KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDa 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 601 ----LADP----LKDELNLADSEVD--SQKRGKQHYEdkqkehLDTLNKKRRELD-MKEKELQEKMSQARQicpERIEVK 669
Cdd:COG3206 256 lpelLQSPviqqLRAQLAELEAELAelSARYTPNHPD------VIALRAQIAALRaQLQQEAQRILASLEA---ELEALQ 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1026346652 670 KSASILDKEINRLRQKIQAEHASHGDREEIMKQYQEARETYLDLDNKVRTLR 721
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
470-712 |
7.63e-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: 40.42 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 470 RDVDSEISDLETEIENKKGHIITLQQRLSALEKDIKRNEELlkrcqlhyKEIKMKIRKN---------ISEIRELENIEE 540
Cdd:TIGR01612 1361 KKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINL--------EECKSKIESTlddkdidecIKKIKELKNHIL 1432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 541 HQSVDIATLEDEAEENKIKMQMVEKNMEqqkenMENLKS---LKIEAENKYDTIKLKINQLSELADPLKDELNLADSEVD 617
Cdd:TIGR01612 1433 SEESNIDTYFKNADENNENVLLLFKNIE-----MADNKSqhiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAK 1507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 618 SQKRGKQHYEDKQKEHLDTLNKkrreldMKEKELQEKMSQArqicperievKKSASILDKEINRLRQKIQAEhasHGDRE 697
Cdd:TIGR01612 1508 AIEKNKELFEQYKKDVTELLNK------YSALAIKNKFAKT----------KKDSEIIIKEIKDAHKKFILE---AEKSE 1568
|
250
....*....|....*
gi 1026346652 698 EIMKQYQEARETYLD 712
Cdd:TIGR01612 1569 QKIKEIKKEKFRIED 1583
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
487-725 |
9.54e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.43 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 487 KGHIITLQQRLSALEKDIKRNEELLKRCQLHY----KEIKMKIRKNISE---------IRELENIEEHQS---VDIATLE 550
Cdd:PRK04778 197 REILDQLEEELAALEQIMEEIPELLKELQTELpdqlQELKAGYRELVEEgyhldhldiEKEIQDLKEQIDenlALLEELD 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 551 -DEAEEnkiKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELnladsevdsqKRGKQHYEDK 629
Cdd:PRK04778 277 lDEAEE---KNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEI----------DRVKQSYTLN 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 630 QKEhldtlNKKRRELdmkEKELQEKMSQARQICPERIEVKKSASILDKEINRLRQKIQAEHASHGD-REEIMKQYQ---E 705
Cdd:PRK04778 344 ESE-----LESVRQL---EKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKlSEMLQGLRKdelE 415
|
250 260
....*....|....*....|
gi 1026346652 706 ARETYLDLDNKVRTLRRFIK 725
Cdd:PRK04778 416 AREKLERYRNKLHEIKRYLE 435
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
531-671 |
9.93e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 39.66 E-value: 9.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1026346652 531 EIRELENIEEHQSVDIATLEDEAEENKIKMQMVEKNMEQQKENMENLKSLKIEAENKYDTIKLKINQLSELADPLKDELN 610
Cdd:pfam05911 689 EFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEAELN 768
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1026346652 611 LADSEVDSQKrgkQHYEDKQKEHldtlnkkrRELDMKEKELQEKMsqarqicpERIEVKKS 671
Cdd:pfam05911 769 ELRQKFEALE---VELEEEKNCH--------EELEAKCLELQEQL--------ERNEKKES 810
|
|
| |
