|
Name |
Accession |
Description |
Interval |
E-value |
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
16-279 |
1.42e-146 |
|
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460516 Cd Length: 260 Bit Score: 424.48 E-value: 1.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 16 NEQLLVNQEAIEILEKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263 1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 96 TEGLGDVEKSNPKNDSWIFALSVLLSSTFVYNSMSTINHQALEQLHYVTELTELIRSKSSRNphgiKNSTEFVSFFPDFV 175
Cdd:pfam02263 81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTELSSPRYGRV----ADSADFVSFFPDFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 176 WTVRDFMLELKLNGEDITSDEYLENALKLIPGYNPRVQASNSARECIRCFFPNRKCFVFDRPTHDRELLQKLETISEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
|
250 260
....*....|....*....|....
gi 27370144 256 DLKFREGTKAFVSYVFTYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
281-575 |
1.87e-143 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 417.84 E-value: 1.87e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 281 EGIKVTGNRLGTLVTTYVDAINSGAVPCLDDAMTSVARRENSVAVQKAADHYSEQMAQRLRLPTDTLQELLDVHAACEKE 360
Cdd:pfam02841 1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 361 AMAVFMEHSFKDENQQFLKKLVEIISEKIAFFWLKNEEASNKYCQEELDRLSKDFMDNIS--TFSVPGGHRIYTDMRKKI 438
Cdd:pfam02841 81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 439 ERDYWQVPRKGVKACEVFQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKR 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27370144 519 NKENLEQLRRKLMQEREQDIKDHDMMLEKQLKDQKAFLEEGFTNKAEEINAEIERLE 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
287-575 |
2.32e-133 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 391.94 E-value: 2.32e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 287 GNRLGTLVTTYVDAINSGAVPCLDDAMTSVARRENSVAVQKAADHYSEQMAQRLRLPTDTLQELLDVHAACEKEAMAVFM 366
Cdd:cd16269 1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 367 EHSFKDENQQFLKKLVEIISEKIAFFWLKNEEASNKYCQEELDRLSKDFMDNIS--TFSVPGGHRIYTDMRKKIERDYWQ 444
Cdd:cd16269 81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 445 VPRKGVKACEVFQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLE 524
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 27370144 525 QLRRKLMQEREQDIKDHDMMLEKQLKDQKAFLEEGFTNKAEEINAEIERLE 575
Cdd:cd16269 241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
30-272 |
1.61e-70 |
|
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.
Pssm-ID: 206650 Cd Length: 224 Bit Score: 227.21 E-value: 1.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 30 EKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKSNP 107
Cdd:cd01851 1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 108 KNDSWIFALSVLLSSTFVYNSMSTINHQALEQLHYVTELTElirskSSRNPHGIKNsteFVSFFPDFVWTVRDFMLELKL 187
Cdd:cd01851 81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 188 NGEDITSDEYlenalKLIPGYnprvqasNSARECIRCFFPNRKCFVFDRPTHDRELLQKleTISEDQLDLKFREGTKAFV 267
Cdd:cd01851 153 EGLDVTEKSE-----TLIEEL-------NKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALR 218
|
....*
gi 27370144 268 SYVFT 272
Cdd:cd01851 219 QRFFS 223
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
467-588 |
3.77e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 467 ESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMMLE 546
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27370144 547 KQLKDQKAFLEEGFtnKAEEINAEIERLEHNIkdkkENIGPI 588
Cdd:COG1196 747 LLEEEALEELPEPP--DLEELERELERLEREI----EALGPV 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
456-595 |
6.21e-05 |
|
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: 46.20 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 456 FQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNK---ENLEQLRRKLMQ 532
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVAQ 390
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370144 533 EREQdIKDHDMMLEkQLKDQKAFLEEGFTNKAEEINAEIERL-EHNIKDKKENIGPILELIEKA 595
Cdd:TIGR02168 391 LELQ-IASLNNEIE-RLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEEL 452
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
23-104 |
1.59e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 43.99 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 23 QEAIEIlEKISQPVVVVAIVGLYRTGKSYLMNCLAGQN-----HGFPlgstvqsQTKGIwmWCMPHPTKPEHTLVLLDTE 97
Cdd:COG3596 27 AEALER-LLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------CTREI--QRYRLESDGLPGLVLLDTP 96
|
....*..
gi 27370144 98 GLGDVEK 104
Cdd:COG3596 97 GLGEVNE 103
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
485-585 |
5.18e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 485 AEERAQK--EVAEKEQELLRqKQKEQQEYMEAQEKRNK-ENLEQLRRKLMQEREQDIKDHDMMLEKqlKDQKAFLEEgft 561
Cdd:PRK12704 36 AEEEAKRilEEAKKEAEAIK-KEALLEAKEEIHKLRNEfEKELRERRNELQKLEKRLLQKEENLDR--KLELLEKRE--- 109
|
90 100
....*....|....*....|....
gi 27370144 562 NKAEEINAEIERLEHNIKDKKENI 585
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEEL 133
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
478-584 |
4.25e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 40.03 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 478 TAGEKAIAEERAQKEVA---------------------EKEQELLRQKQKEQQEYMEAQEKRNKEnlEQLRRKlmqereq 536
Cdd:smart00435 246 NVAEKILAYNRANREVAilcnhqrtvsktheksmeklqEKIKALKYQLKRLKKMILLFEMISDLK--RKLKSK------- 316
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 27370144 537 DIKDHDMMLEKQLKDQKAFLEEGFTNKA-EEINAEIERLEHNIKDKKEN 584
Cdd:smart00435 317 FERDNEKLDAEVKEKKKEKKKEEKKKKQiERLEERIEKLEVQATDKEEN 365
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
16-279 |
1.42e-146 |
|
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460516 Cd Length: 260 Bit Score: 424.48 E-value: 1.42e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 16 NEQLLVNQEAIEILEKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263 1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 96 TEGLGDVEKSNPKNDSWIFALSVLLSSTFVYNSMSTINHQALEQLHYVTELTELIRSKSSRNphgiKNSTEFVSFFPDFV 175
Cdd:pfam02263 81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTELSSPRYGRV----ADSADFVSFFPDFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 176 WTVRDFMLELKLNGEDITSDEYLENALKLIPGYNPRVQASNSARECIRCFFPNRKCFVFDRPTHDRELLQKLETISEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
|
250 260
....*....|....*....|....
gi 27370144 256 DLKFREGTKAFVSYVFTYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
281-575 |
1.87e-143 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 417.84 E-value: 1.87e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 281 EGIKVTGNRLGTLVTTYVDAINSGAVPCLDDAMTSVARRENSVAVQKAADHYSEQMAQRLRLPTDTLQELLDVHAACEKE 360
Cdd:pfam02841 1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 361 AMAVFMEHSFKDENQQFLKKLVEIISEKIAFFWLKNEEASNKYCQEELDRLSKDFMDNIS--TFSVPGGHRIYTDMRKKI 438
Cdd:pfam02841 81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 439 ERDYWQVPRKGVKACEVFQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKR 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27370144 519 NKENLEQLRRKLMQEREQDIKDHDMMLEKQLKDQKAFLEEGFTNKAEEINAEIERLE 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
287-575 |
2.32e-133 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 391.94 E-value: 2.32e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 287 GNRLGTLVTTYVDAINSGAVPCLDDAMTSVARRENSVAVQKAADHYSEQMAQRLRLPTDTLQELLDVHAACEKEAMAVFM 366
Cdd:cd16269 1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 367 EHSFKDENQQFLKKLVEIISEKIAFFWLKNEEASNKYCQEELDRLSKDFMDNIS--TFSVPGGHRIYTDMRKKIERDYWQ 444
Cdd:cd16269 81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 445 VPRKGVKACEVFQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLE 524
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 27370144 525 QLRRKLMQEREQDIKDHDMMLEKQLKDQKAFLEEGFTNKAEEINAEIERLE 575
Cdd:cd16269 241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
30-272 |
1.61e-70 |
|
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.
Pssm-ID: 206650 Cd Length: 224 Bit Score: 227.21 E-value: 1.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 30 EKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKSNP 107
Cdd:cd01851 1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 108 KNDSWIFALSVLLSSTFVYNSMSTINHQALEQLHYVTELTElirskSSRNPHGIKNsteFVSFFPDFVWTVRDFMLELKL 187
Cdd:cd01851 81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 188 NGEDITSDEYlenalKLIPGYnprvqasNSARECIRCFFPNRKCFVFDRPTHDRELLQKleTISEDQLDLKFREGTKAFV 267
Cdd:cd01851 153 EGLDVTEKSE-----TLIEEL-------NKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALR 218
|
....*
gi 27370144 268 SYVFT 272
Cdd:cd01851 219 QRFFS 223
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
40-115 |
6.18e-08 |
|
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.
Pssm-ID: 206648 [Multi-domain] Cd Length: 161 Bit Score: 52.46 E-value: 6.18e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370144 40 AIVGLYRTGKSYLMNCLAGQNHGFPlgSTVQSQTKGIWMWCMPHPtKPEHTLVLLDTEGLGDVEKSNPKNDSWIFA 115
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEV--SDVPGTTRDPDVYVKELD-KGKVKLVLVDTPGLDEFGGLGREELARLLL 73
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
481-566 |
4.94e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 481 EKAIAEERAQKEVAEKEQ--ELLRQKQKEQ--QEYMEAQEKRNKENLEQLRRKL----MQEREQDI---KDHDMMLEKQL 549
Cdd:pfam17380 443 ERAREMERVRLEEQERQQqvERLRQQEEERkrKKLELEKEKRDRKRAEEQRRKIlekeLEERKQAMieeERKRKLLEKEM 522
|
90
....*....|....*...
gi 27370144 550 KD-QKAFLEEGFTNKAEE 566
Cdd:pfam17380 523 EErQKAIYEEERRREAEE 540
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
467-588 |
3.77e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 467 ESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMMLE 546
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 27370144 547 KQLKDQKAFLEEGFtnKAEEINAEIERLEHNIkdkkENIGPI 588
Cdd:COG1196 747 LLEEEALEELPEPP--DLEELERELERLEREI----EALGPV 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
456-595 |
6.21e-05 |
|
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: 46.20 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 456 FQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNK---ENLEQLRRKLMQ 532
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVAQ 390
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27370144 533 EREQdIKDHDMMLEkQLKDQKAFLEEGFTNKAEEINAEIERL-EHNIKDKKENIGPILELIEKA 595
Cdd:TIGR02168 391 LELQ-IASLNNEIE-RLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEEL 452
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
485-566 |
1.29e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.94 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 485 AEERA---QKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQL---RRKLMQEREQDikdhdmMLEKQLKDQKAflEE 558
Cdd:pfam15709 417 AQERArqqQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLaeeQKRLMEMAEEE------RLEYQRQKQEA--EE 488
|
....*...
gi 27370144 559 GFTNKAEE 566
Cdd:pfam15709 489 KARLEAEE 496
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
23-104 |
1.59e-04 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 43.99 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 23 QEAIEIlEKISQPVVVVAIVGLYRTGKSYLMNCLAGQN-----HGFPlgstvqsQTKGIwmWCMPHPTKPEHTLVLLDTE 97
Cdd:COG3596 27 AEALER-LLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------CTREI--QRYRLESDGLPGLVLLDTP 96
|
....*..
gi 27370144 98 GLGDVEK 104
Cdd:COG3596 97 GLGEVNE 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
466-595 |
2.03e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 466 IESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEymEAQEKRNKENLEQLRrklmQEREQDIKDHDMML 545
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL--ELEEAQAEEYELLAE----LARLEQDIARLEER 310
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 27370144 546 EKQLKDQKAFLEEGFTNKAEEINAEIERLEhNIKDKKENIGPILELIEKA 595
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELE-ELEEELEEAEEELEEAEAE 359
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
471-583 |
2.21e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 471 LQADRALTAGEKAIAEE--RAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKenLEQLRrklmQEREQDIKDhdmmLEKQ 548
Cdd:COG4942 138 LQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEALLAELEEERAA--LEALK----AERQKLLAR----LEKE 207
|
90 100 110
....*....|....*....|....*....|....*
gi 27370144 549 LKDQKAFLEEgFTNKAEEINAEIERLEHNIKDKKE 583
Cdd:COG4942 208 LAELAAELAE-LQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
466-590 |
3.39e-04 |
|
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: 43.90 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 466 IESSILQADRALTAGEKAIAEERAQKEVAEKEqellRQKQKEQQEYMEAQEKRNKENLEQLRRKL--MQEREQDIKDHDM 543
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKE----IQELQEQRIDLKEQIKSIEKEIENLNGKKeeLEEELEELEAALR 878
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 27370144 544 MLEKQLKDQKAFLEE------GFTNKAEEINAEIERLEHNIKDKKENIGPILE 590
Cdd:TIGR02169 879 DLESRLGDLKKERDEleaqlrELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
431-595 |
4.69e-04 |
|
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: 43.51 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 431 YTDMRKKIERDYWQVPRKGVKACEVFQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEvaekEQELLRQKQKEQQE 510
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE----EAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 511 YMEAQEKRNKENLEQLRRKL----MQEREQDIKDHDM-----MLEKQLKDQKAFLEEgFTNKAEEINAEIERLEHNIKDK 581
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALdelrAELTLLNEEAANLrerleSLERRIAATERRLED-LEEQIEELSEDIESLAAEIEEL 864
|
170
....*....|....
gi 27370144 582 KENIGPILELIEKA 595
Cdd:TIGR02168 865 EELIEELESELEAL 878
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
486-575 |
4.72e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 486 EERAQKEVAEKEQELLRQKQKEQQEYMEaQEKRNKENLEQLRRKLMQEREQdikdhDMMLEKQLKDQKAFLEEGFTNKAE 565
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLE-KEEEERLRKEELRRRAEEERAR-----REEEARRLEEERRREEEERQRKAE 82
|
90
....*....|
gi 27370144 566 EINAEIERLE 575
Cdd:pfam05672 83 EEAEEREQRE 92
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
486-585 |
4.88e-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: 43.09 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 486 EERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQ--DIKDHDMMLEKQLKDQKAFLEEgFTNK 563
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKElkKLNEEKKELEEKVKDLTKKISS-LKEK 525
|
90 100
....*....|....*....|..
gi 27370144 564 AEEINAEIERLEHNIKDKKENI 585
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDEL 547
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
485-585 |
5.18e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 485 AEERAQK--EVAEKEQELLRqKQKEQQEYMEAQEKRNK-ENLEQLRRKLMQEREQDIKDHDMMLEKqlKDQKAFLEEgft 561
Cdd:PRK12704 36 AEEEAKRilEEAKKEAEAIK-KEALLEAKEEIHKLRNEfEKELRERRNELQKLEKRLLQKEENLDR--KLELLEKRE--- 109
|
90 100
....*....|....*....|....
gi 27370144 562 NKAEEINAEIERLEHNIKDKKENI 585
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEEL 133
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
477-584 |
5.47e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 477 LTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQ----LRRKLMQEREQDIKDHDMMLEKQLKDQ 552
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKeaqqAIKEAKKEADEIIKELRQLQKGGYASV 604
|
90 100 110
....*....|....*....|....*....|...
gi 27370144 553 KAF-LEEgftnKAEEINAEIERLEHNIKDKKEN 584
Cdd:PRK00409 605 KAHeLIE----ARKRLNKANEKKEKKKKKQKEK 633
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
466-583 |
5.57e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 466 IESSILQADRALTAGEKAIAEERAqkEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMML 545
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRL--ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110
....*....|....*....|....*....|....*...
gi 27370144 546 EKQLKDQKAFLEEGfTNKAEEINAEIERLEHNIKDKKE 583
Cdd:COG1196 329 EEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEE 365
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
485-583 |
7.88e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 485 AEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENlEQLRRKLMQEREQDIKdhdmmlEKQLKDQKAFLEEGFTNKA 564
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149
|
90
....*....|....*....
gi 27370144 565 EeinAEIERLEHNIKDKKE 583
Cdd:PRK09510 150 E---AEAKRAAAAAKKAAA 165
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
475-585 |
8.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 475 RALTAGEKAIAEERAQKEVAEKEQEllrqkQKEQQEYMEAQEKRNKENLEQLRRKLMQER----------------EQDI 538
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAE-----EKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaeeakkdeeekkkiAHLK 1763
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 27370144 539 KDHDMMLEKQLKDQKAFLEEGFTNKAEEINAEIERLEHNIKDKKENI 585
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
467-584 |
9.92e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.05 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 467 ESSILQADRALTAGEKAIAEERAQKEvaEKEQELLRqKQKEQQEYMEAQEKRNKEN-----LEQLRRKLMQEREQDIKDH 541
Cdd:pfam09731 286 NSLIAHAHREIDQLSKKLAELKKREE--KHIERALE-KQKEELDKLAEELSARLEEvraadEAQLRLEFEREREEIRESY 362
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 27370144 542 DMMLEKQLKDQKAFLEEGFTNKAEEINAEIER-LEHNIKDKKEN 584
Cdd:pfam09731 363 EEKLRTELERQAEAHEEHLKDVLVEQEIELQReFLQDIKEKVEE 406
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
487-576 |
9.98e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 487 ERAQKEVAEKEQELLRQKQKEQQEymEAQEKRNKENLEQLRRKLMQEREQDIKdhdmmLEKQLKDQKAFLEegftnkaEE 566
Cdd:PRK12704 71 NEFEKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKKEKELEQ-----KQQELEKKEEELE-------EL 136
|
90
....*....|
gi 27370144 567 INAEIERLEH 576
Cdd:PRK12704 137 IEEQLQELER 146
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
481-590 |
1.08e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 481 EKAIAEERAQKEVAEKEQELLRQKQKEQQ---EYMEAQEKRNKENLEQLRRKlmqEREQDIKDHDMMLEKQLKDQKAFLE 557
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKE---AEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 27370144 558 EGFTNKAEEINAEIE----------------RLEHNIKDKKENIGPILE 590
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEavieeeldeedekrrmEVDKKIKDIFDNFANIIE 1812
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
466-595 |
1.17e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 466 IESSILQADRALTAGEKAIAEERAQ-----KEVAEKEQELLRQKQKEQQEymEAQEKRNKENLEQLRRKL--MQEREQDI 538
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQAEeyellAELARLEQDIARLEERRREL--EERLEELEEELAELEEELeeLEEELEEL 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 27370144 539 KDHDMMLEKQLKDQKAFLEEGFTNKAEEINAEIERLEHNIKDKKENIGPILELIEKA 595
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
490-595 |
1.30e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 490 QKEVAEKEQELLRQKQKEQQEYMEAQEKRNKE---NLEQLRRKLMQEREQDIKDHDMMLEKQLKDQKAFLEEgFTNKAEE 566
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEElrkELEELEKKYSEEEYEELREEYLELSRELAGLRAELEE-LEKRREE 691
|
90 100
....*....|....*....|....*....
gi 27370144 567 INAEIERLEHNIKDKKENIGPIlELIEKA 595
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKEL-EKLEKA 719
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
481-582 |
1.34e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 481 EKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQE----KRNKENLE---------------QLRRKLMQEREQDIKDH 541
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDelraKLYQEEQErkerqkereeaekkaRQRQELQQAREEQIELK 248
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 27370144 542 DMMLEKQLKDQKAFLEegftnKAEEINAEIERLEHNIKDKK 582
Cdd:pfam13868 249 ERRLAEEAEREEEEFE-----RMLRKQAEDEEIEQEEAEKR 284
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
467-585 |
1.59e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 467 ESSILQADRALTAGEKAIAE-ERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMML 545
Cdd:COG1196 221 ELKELEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 27370144 546 EKQLKDQKAfLEEGFTNKAEEINAEIERLEHNIKDKKENI 585
Cdd:COG1196 301 EQDIARLEE-RRRELEERLEELEEELAELEEELEELEEEL 339
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
486-574 |
1.60e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 39.25 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 486 EERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMMLEKQLKDQKAFLEEgftnKAE 565
Cdd:pfam05672 40 EERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKARE----EAE 115
|
....*....
gi 27370144 566 EINAEIERL 574
Cdd:pfam05672 116 RQRQEREKI 124
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
465-583 |
2.21e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 465 IIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMM 544
Cdd:COG2268 197 IIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAE 276
|
90 100 110
....*....|....*....|....*....|....*....
gi 27370144 545 LEKQLKDQKAFLEEGFTNKAEEINAEIERLEHNIKDKKE 583
Cdd:COG2268 277 REVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAE 315
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
467-595 |
2.56e-03 |
|
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: 41.21 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 467 ESSILQADRALTAGEKAIAEERAQkeVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMMLE 546
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSRIEAR--LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 27370144 547 KQLKDQKAFLEEgFTNKAEEINAEIERLEHNIKDKKENIGPILELIEKA 595
Cdd:TIGR02169 868 EELEELEAALRD-LESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
466-595 |
2.59e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 466 IESSILQADRALTAGEKAIAE-----ERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNK-ENLEQLRRKLMQEREQDIK 539
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEaeealLEAEAELAEAEEELEELAEELLEALRAAAELAAQlEELEEAEEALLERLERLEE 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 27370144 540 DHDMMLEKQLKDQKAFLEEgfTNKAEEINAEIERLEHNIKDKKENIGPILELIEKA 595
Cdd:COG1196 422 ELEELEEALAELEEEEEEE--EEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
472-544 |
2.68e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 40.74 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 472 QADRALTAGEKAIAE--ER--AQKEVAEKEQELlRQKQkeqQEYMEAQEKRNKENLEQLRRKLMQE----REQDIKdhDM 543
Cdd:pfam13779 486 DAERRLRAAQERLSEalERgaSDEEIAKLMQEL-REAL---DDYMQALAEQAQQNPQDLQQPDDPNaqemTQQDLQ--RM 559
|
.
gi 27370144 544 M 544
Cdd:pfam13779 560 L 560
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
481-575 |
2.78e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.29 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 481 EKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDmmlEKQLKDQKAFLEEGf 560
Cdd:pfam13868 242 EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEERE---EQRAAEREEELEEG- 317
|
90
....*....|....*
gi 27370144 561 TNKAEEINAEIERLE 575
Cdd:pfam13868 318 ERLREEEAERRERIE 332
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
476-589 |
2.92e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 476 ALTAGEKAIAEERAQKEvAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLR--RKLMQEREQDIKDhdmmLEKQLKDQK 553
Cdd:COG4942 8 ALLLALAAAAQADAAAE-AEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRA----LEQELAALE 82
|
90 100 110
....*....|....*....|....*....|....*.
gi 27370144 554 AFLeegftnkaEEINAEIERLEHNIKDKKENIGPIL 589
Cdd:COG4942 83 AEL--------AELEKEIAELRAELEAQKEELAELL 110
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
481-570 |
3.06e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 481 EKAIAEERAQKEVAEKEQEL--------LRQKQ---KEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDmmLEKQL 549
Cdd:COG0542 417 ERRLEQLEIEKEALKKEQDEasferlaeLRDELaelEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPE--LEKEL 494
|
90 100
....*....|....*....|.
gi 27370144 550 KDQKAFLEEGFTNKAEEINAE 570
Cdd:COG0542 495 AELEEELAELAPLLREEVTEE 515
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
478-584 |
4.25e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 40.03 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 478 TAGEKAIAEERAQKEVA---------------------EKEQELLRQKQKEQQEYMEAQEKRNKEnlEQLRRKlmqereq 536
Cdd:smart00435 246 NVAEKILAYNRANREVAilcnhqrtvsktheksmeklqEKIKALKYQLKRLKKMILLFEMISDLK--RKLKSK------- 316
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 27370144 537 DIKDHDMMLEKQLKDQKAFLEEGFTNKA-EEINAEIERLEHNIKDKKEN 584
Cdd:smart00435 317 FERDNEKLDAEVKEKKKEKKKEEKKKKQiERLEERIEKLEVQATDKEEN 365
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
481-595 |
4.40e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 481 EKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKE-----NLEQLRRKLMQEREQDIKDHDMMLEKQLKDQKAF 555
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaeaGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 27370144 556 LEEgFTNKAEEINAEIERLEHNIKDKKENIGPILELIEKA 595
Cdd:PRK02224 337 AQA-HNEEAESLREDADDLEERAEELREEAAELESELEEA 375
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
472-594 |
4.44e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.99 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 472 QADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQ---EYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMMLEKQ 548
Cdd:pfam05262 221 ELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKnlpKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKA 300
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 27370144 549 lKDQKAFleegftNKAEEINAEIERLEHNIKDKKENIGPILELIEK 594
Cdd:pfam05262 301 -KDHKAF------DLKQESKASEKEAEDKELEAQKKREPVAEDLQK 339
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
465-582 |
4.47e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 465 IIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEY-MEAQEKRNkenlEQLRRKLMQEREQdikdhdm 543
Cdd:COG1842 27 MLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKaRLALEKGR----EDLAREALERKAE------- 95
|
90 100 110
....*....|....*....|....*....|....*....
gi 27370144 544 mLEKQLKDQKAFLEEgFTNKAEEINAEIERLEHNIKDKK 582
Cdd:COG1842 96 -LEAQAEALEAQLAQ-LEEQVEKLKEALRQLESKLEELK 132
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
463-594 |
4.55e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.11 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 463 QYIIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEaqEKRNKENLEQLRRKLMQEREQDIKDHD 542
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVE--RRRKLEEAEKARQAEMDRQAAIYAEQE 340
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27370144 543 MM-------LEK-QLKDQKAFLEEgftNKAEEINAEI------ERLEHNIKDKKENIGPILELIEK 594
Cdd:pfam17380 341 RMamerereLERiRQEERKRELER---IRQEEIAMEIsrmrelERLQMERQQKNERVRQELEAARK 403
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
464-579 |
5.22e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.47 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 464 YIIES----SILQADRALTA-GEKAIAEERAQKEVA----EKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRrklmQER 534
Cdd:COG2268 169 LELESvaitDLEDENNYLDAlGRRKIAEIIRDARIAeaeaERETEIAIAQANREAEEAELEQEREIETARIAE----AEA 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 27370144 535 EQDIKDHDMMLEKQLK----DQKAFLEEGFTNKAEEINAEIERLEHNIK 579
Cdd:COG2268 245 ELAKKKAEERREAETAraeaEAAYEIAEANAEREVQRQLEIAEREREIE 293
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
481-585 |
5.36e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 481 EKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLmQEREQDIKDhdmmLEKQLKD--QKAFLEE 558
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAEL-EEKDERIER----LERELSEarSEERREI 461
|
90 100
....*....|....*....|....*..
gi 27370144 559 GFTNKAEEINAEIERLEHNIKDKKENI 585
Cdd:COG2433 462 RKDREISRLDREIERLERELEEERERI 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
472-583 |
5.94e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 472 QADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMMLEKQL-K 550
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkK 1614
|
90 100 110
....*....|....*....|....*....|...
gi 27370144 551 DQKAFLEEGFTNKAEEINAEIERLEHNIKDKKE 583
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
435-585 |
6.69e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 435 RKKIERDYWQVPRKG--VKACEVFQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEvAEKEQELLRQKQKEQQEYM 512
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKK 1647
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370144 513 EAQEKRNKENLEQLRRKLMQEREQDIKDHDMMLEKQLKDQKAfLEEGFTNKAEEINA--EIERLEHNIKDKKENI 585
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK-AAEALKKEAEEAKKaeELKKKEAEEKKKAEEL 1721
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
488-584 |
6.94e-03 |
|
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: 39.67 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 488 RAQKEVAEKEQELLRQKQK--------------EQQEYMEAQEKRNKENLEQL------RRKLMQEREQDIKDhdmmLEK 547
Cdd:TIGR02169 204 RREREKAERYQALLKEKREyegyellkekealeRQKEAIERQLASLEEELEKLteeiseLEKRLEEIEQLLEE----LNK 279
|
90 100 110
....*....|....*....|....*....|....*..
gi 27370144 548 QLKDQKAFLEEGFTNKAEEINAEIERLEHNIKDKKEN 584
Cdd:TIGR02169 280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
475-585 |
8.25e-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: 38.37 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 475 RALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENleqlRRKLMQ---EREQDIKDHDMmleKQLKD 551
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY----EEQLGNvrnNKEYEALQKEI---ESLKR 103
|
90 100 110
....*....|....*....|....*....|....*..
gi 27370144 552 QKAFLEE---GFTNKAEEINAEIERLEHNIKDKKENI 585
Cdd:COG1579 104 RISDLEDeilELMERIEELEEELAELEAELAELEAEL 140
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
461-585 |
9.40e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 461 QSQYIIESSI--LQADRALTAGEKAIAEERAQkEVAEKEQELLRQKQKEQQEYMEAQEKRNK-----ENLEQLRRKLMQE 533
Cdd:COG1196 288 AEEYELLAELarLEQDIARLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEaeeelEEAEAELAEAEEA 366
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 27370144 534 REQDIKDHDMMLEKQLKDQKAFLEEgfTNKAEEINAEIERLEHNIKDKKENI 585
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEEAEEALLERL 416
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
460-604 |
9.95e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370144 460 LQSQYIIESSilqADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKR-----NKENLEQLRRK---LM 531
Cdd:COG4913 598 IRSRYVLGFD---NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswDEIDVASAEREiaeLE 674
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370144 532 QEREQDIKDHD--MMLEKQLKDQKAFLEEgFTNKAEEINAEIERLEHNIKDKKENIG---PILELIEKAFCAGVFSSL 604
Cdd:COG4913 675 AELERLDASSDdlAALEEQLEELEAELEE-LEEELDELKGEIGRLEKELEQAEEELDelqDRLEAAEDLARLELRALL 751
|
|
| |
