|
Name |
Accession |
Description |
Interval |
E-value |
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
281-575 |
5.62e-147 |
|
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: 426.70 E-value: 5.62e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 281 EGIKVTGNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAASHYSEQMAQRLSLPTETLQELLDVHVACEKE 360
Cdd:pfam02841 1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 361 AIAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKI 438
Cdd:pfam02841 81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 439 EHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKS 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 34786063 519 HKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
16-279 |
8.33e-145 |
|
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: 419.47 E-value: 8.33e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 16 NEQLSVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263 1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTINHQALEQLHYVTELTELirakSSPNLAGIKNSTEFVSFFPDFV 175
Cdd:pfam02263 81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 176 WIVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
|
250 260
....*....|....*....|....
gi 34786063 256 DPKFQEVTKAFVSYIFTYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
287-575 |
6.74e-138 |
|
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: 403.11 E-value: 6.74e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 287 GNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAASHYSEQMAQRLSLPTETLQELLDVHVACEKEAIAVFM 366
Cdd:cd16269 1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 367 EHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKIEHDYWQ 444
Cdd:cd16269 81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 445 VPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENLE 524
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 34786063 525 QLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:cd16269 241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
31-272 |
6.89e-71 |
|
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: 227.98 E-value: 6.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 31 KISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:cd01851 2 DVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 109 NDLWIFALSVLLSSTFIYNSMNTINHQALEQLHYVTELTEliraksspNLAGIKNSTEFVSFFPDFVWIVRDFMLELKLN 188
Cdd:cd01851 82 NDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL--------ETLGLAGLHNFSKPKPLLLFVVRDFTGPTPLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 189 GEDITsddylenalkliPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKldSITEDQLDPKFQEVTKAFVS 268
Cdd:cd01851 154 GLDVT------------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQ 219
|
....
gi 34786063 269 YIFT 272
Cdd:cd01851 220 RFFS 223
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
433-591 |
5.26e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 433 DKREKIEHDYWQVPRKG--VKASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKvAAEKEQDLLRQKQKEQQE 510
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEE 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 511 YMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAfLEEGFKKKAEEmNKEIQQLRDVIKDKKRNTDRIKD 590
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK-AAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKK 1723
|
.
gi 34786063 591 A 591
Cdd:PTZ00121 1724 A 1724
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1-108 |
1.99e-05 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 47.07 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 1 MTQPQMAPICLVENHNEQLSVNQEAI-EILD--KISQPVVVVAIVGLYRTGKSYLMNCLAGQN-----HGFPlgstvqsQ 72
Cdd:COG3596 1 MSTEVSSLTERLEALKRLPQVLRELLaEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------C 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 34786063 73 TKGIwmWCMPHPTKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:COG3596 74 TREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
467-592 |
1.80e-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: 44.66 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 467 ESSILQADTALTAGEKAIAEERAQKVAAEKEQDLLRQK---QKEQQEYMEAQEKSHKENLEQLRRKLEQ-----EREQDI 538
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEEleaqlEELESK 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 34786063 539 KDHDMMLKKLMKDQKAFLE---EGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
472-592 |
2.14e-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: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 472 QADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEymEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKD 551
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ--LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 34786063 552 QKAFLEEgfKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG1196 441 EEALEEA--AEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
281-575 |
5.62e-147 |
|
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: 426.70 E-value: 5.62e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 281 EGIKVTGNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAASHYSEQMAQRLSLPTETLQELLDVHVACEKE 360
Cdd:pfam02841 1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 361 AIAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKI 438
Cdd:pfam02841 81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 439 EHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKS 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 34786063 519 HKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
16-279 |
8.33e-145 |
|
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: 419.47 E-value: 8.33e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 16 NEQLSVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263 1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMNTINHQALEQLHYVTELTELirakSSPNLAGIKNSTEFVSFFPDFV 175
Cdd:pfam02263 81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 176 WIVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
|
250 260
....*....|....*....|....
gi 34786063 256 DPKFQEVTKAFVSYIFTYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
287-575 |
6.74e-138 |
|
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: 403.11 E-value: 6.74e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 287 GNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAASHYSEQMAQRLSLPTETLQELLDVHVACEKEAIAVFM 366
Cdd:cd16269 1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 367 EHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKIEHDYWQ 444
Cdd:cd16269 81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 445 VPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENLE 524
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 34786063 525 QLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:cd16269 241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
31-272 |
6.89e-71 |
|
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: 227.98 E-value: 6.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 31 KISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:cd01851 2 DVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 109 NDLWIFALSVLLSSTFIYNSMNTINHQALEQLHYVTELTEliraksspNLAGIKNSTEFVSFFPDFVWIVRDFMLELKLN 188
Cdd:cd01851 82 NDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL--------ETLGLAGLHNFSKPKPLLLFVVRDFTGPTPLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 189 GEDITsddylenalkliPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKldSITEDQLDPKFQEVTKAFVS 268
Cdd:cd01851 154 GLDVT------------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQ 219
|
....
gi 34786063 269 YIFT 272
Cdd:cd01851 220 RFFS 223
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
40-115 |
1.15e-07 |
|
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: 51.69 E-value: 1.15e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34786063 40 AIVGLYRTGKSYLMNCLAGQNHGFPlgSTVQSQTKGIWMWCMPHPtKPEHTLVLLDTEGLGDVEKGDPKNDLWIFA 115
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGEVGEV--SDVPGTTRDPDVYVKELD-KGKVKLVLVDTPGLDEFGGLGREELARLLL 73
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
436-593 |
3.49e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 436 EKIEHDYW-----QVPRKGVKASEVFQSFLQSQAFIESSILQADTALtaGEKAIAEERAQKVAAEKEQDLLR---QKQKE 507
Cdd:pfam12128 588 KRIDVPEWaaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGEL--EKASREETFARTALKNARLDLRRlfdEKQSE 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 508 QQEyMEAQEKSHKENLEQLRRKLEQEreqdikdhdmmLKKLMKDQKAFLEEgFKKKAEEMNKEIQQ-LRDVIKDKKRNTD 586
Cdd:pfam12128 666 KDK-KNKALAERKDSANERLNSLEAQ-----------LKQLDKKHQAWLEE-QKEQKREARTEKQAyWQVVEGALDAQLA 732
|
....*..
gi 34786063 587 RIKDALL 593
Cdd:pfam12128 733 LLKAAIA 739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
433-591 |
5.26e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 433 DKREKIEHDYWQVPRKG--VKASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKvAAEKEQDLLRQKQKEQQE 510
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEE 1645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 511 YMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAfLEEGFKKKAEEmNKEIQQLRDVIKDKKRNTDRIKD 590
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKK-AAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKK 1723
|
.
gi 34786063 591 A 591
Cdd:PTZ00121 1724 A 1724
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
429-591 |
1.70e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 429 KLYMDKREKIEH--DYWQVPRKGVKASEVFQSFLQSQAFIESSI-LQADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQ 505
Cdd:pfam17380 382 RLQMERQQKNERvrQELEAARKVKILEEERQRKIQQQKVEMEQIrAEQEEARQREVRRLEEERAREMERVRLEEQERQQQ 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 506 KE---QQE--------YMEAQEKSHKENLEQLRRKLEQEREQ------DIKDHDMMLKKLMKD-QKAFLEEGFKKKAEEM 567
Cdd:pfam17380 462 VErlrQQEeerkrkklELEKEKRDRKRAEEQRRKILEKELEErkqamiEEERKRKLLEKEMEErQKAIYEEERRREAEEE 541
|
170 180
....*....|....*....|....
gi 34786063 568 NKEIQQlrdvIKDKKRNTDRIKDA 591
Cdd:pfam17380 542 RRKQQE----MEERRRIQEQMRKA 561
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1-108 |
1.99e-05 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 47.07 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 1 MTQPQMAPICLVENHNEQLSVNQEAI-EILD--KISQPVVVVAIVGLYRTGKSYLMNCLAGQN-----HGFPlgstvqsQ 72
Cdd:COG3596 1 MSTEVSSLTERLEALKRLPQVLRELLaEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------C 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 34786063 73 TKGIwmWCMPHPTKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:COG3596 74 TREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
485-574 |
8.83e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 485 AEERAQKVAAEKEQDLlRQKQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQDIKdhdmmlKKLMKDQKAFLEEGFKKKA 564
Cdd:PRK09510 77 AEEQRKKKEQQQAEEL-QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149
|
90
....*....|
gi 34786063 565 EEMNKEIQQL 574
Cdd:PRK09510 150 EAEAKRAAAA 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
467-592 |
1.80e-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: 44.66 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 467 ESSILQADTALTAGEKAIAEERAQKVAAEKEQDLLRQK---QKEQQEYMEAQEKSHKENLEQLRRKLEQ-----EREQDI 538
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEEleaqlEELESK 331
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 34786063 539 KDHDMMLKKLMKDQKAFLE---EGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKeelESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
472-591 |
1.94e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 472 QADTALTAGEKAIAEERAQKVAAE--KEQDLLRQKQKEQQ---EYMEAQEKSHKENLEQLRRKLE---QEREQDIKDHDM 543
Cdd:PTZ00121 1303 KADEAKKKAEEAKKADEAKKKAEEakKKADAAKKKAEEAKkaaEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADA 1382
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 34786063 544 MLKKLMKDQKAfleEGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDA 591
Cdd:PTZ00121 1383 AKKKAEEKKKA---DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA 1427
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
472-592 |
2.14e-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: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 472 QADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEymEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKD 551
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ--LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 34786063 552 QKAFLEEgfKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG1196 441 EEALEEA--AEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
472-591 |
2.51e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 472 QADTALTAGEKAIAEE--RAQKVAAEKEQDLLRQKQKEQQEYMEAQEKShkenleQLRRKLEQEREQDIKDHDMMLKKlM 549
Cdd:PTZ00121 1535 KADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKA------EEAKKAEEARIEEVMKLYEEEKK-M 1607
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 34786063 550 KDQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDA 591
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
471-592 |
3.02e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 471 LQA-DTALTAGEKAIAEERAQKVAAEKEQDLLRQ---KQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQ-----DIKDH 541
Cdd:COG1579 12 LQElDSELDRLEHRLKELPAELAELEDELAALEArleAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKEY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 34786063 542 DMMLKKL--MKDQKAFLEE---GFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG1579 92 EALQKEIesLKRRISDLEDeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
481-572 |
3.33e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 481 EKAIAEERAQKVAAEKEqdllRQKQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGF 560
Cdd:PRK09510 85 EQQQAEELQQKQAAEQE----RLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160
|
90
....*....|..
gi 34786063 561 KKKAEEMNKEIQ 572
Cdd:PRK09510 161 KKAAAEAKKKAE 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
451-593 |
3.59e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 451 KASEVFQSFLQSQAFIESSILQADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKE-----NLEQ 525
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakKAEE 1706
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34786063 526 LRRKLEQER---EQDIKDHDMMLKKLMKDQKAFLEEgfKKKAEEMNKE------IQQLRDVIKDKKRNTDRIKDALL 593
Cdd:PTZ00121 1707 LKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAEED--KKKAEEAKKDeeekkkIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
486-575 |
4.97e-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: 40.79 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 486 EERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKEnLEQLRRKLEQEREQdikdhDMMLKKLMKDQKAFLEEGFKKKAE 565
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLEKEEEERLR-KEELRRRAEEERAR-----REEEARRLEEERRREEEERQRKAE 82
|
90
....*....|
gi 34786063 566 EMNKEIQQLR 575
Cdd:pfam05672 83 EEAEEREQRE 92
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
472-589 |
5.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 472 QADTALTAGEKAIAEERAQKVAAEKEQDLLrQKQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQD-IKDHDMMLKKLMK 550
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEA-EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADeAKKKAEEDKKKAD 1408
|
90 100 110
....*....|....*....|....*....|....*....
gi 34786063 551 DQKAFLEEgfKKKAEEMNKEIQQLRDVIKDKKRNTDRIK 589
Cdd:PTZ00121 1409 ELKKAAAA--KKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
479-591 |
5.98e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 479 AGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSH-KENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLE 557
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEeAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
90 100 110
....*....|....*....|....*....|....*...
gi 34786063 558 EGfKKKAEEMNK--EIQQLRDVIK--DKKRNTDRIKDA 591
Cdd:PTZ00121 1494 EA-KKKADEAKKaaEAKKKADEAKkaEEAKKADEAKKA 1530
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
485-573 |
7.57e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 485 AEERAQKVAAE-KEQDLLRQKQKEQQEYMEAQEKSHKENLEQ----LRRKLEQEREQDIKDHDMMLKKLMKDQKAfleeg 559
Cdd:PRK00409 532 LEQKAEEAEALlKEAEKLKEELEEKKEKLQEEEDKLLEEAEKeaqqAIKEAKKEADEIIKELRQLQKGGYASVKA----- 606
|
90
....*....|....
gi 34786063 560 fkKKAEEMNKEIQQ 573
Cdd:PRK00409 607 --HELIEARKRLNK 618
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
472-591 |
7.71e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 472 QADTALTAGEKAIAEERAQKVAAE--KEQDLLRQKQKEQQEYMEAQEKSH-KENLEQLRRKLEQEREQDIKDHDMMLKKL 548
Cdd:PTZ00121 1379 KADAAKKKAEEKKKADEAKKKAEEdkKKADELKKAAAAKKKADEAKKKAEeKKKADEAKKKAEEAKKADEAKKKAEEAKK 1458
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 34786063 549 MKDQKAFLEEgfKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDA 591
Cdd:PTZ00121 1459 AEEAKKKAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
481-590 |
9.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 481 EKAIAEERAQKVAAEKEQ-DLLRQKQKEQQEYMEAQEKSHKEN---LEQLRRKLEQER----------------EQDIKD 540
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKaEELKKKEAEEKKKAEELKKAEEENkikAEEAKKEAEEDKkkaeeakkdeeekkkiAHLKKE 1765
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 34786063 541 HDMMLKKLMKDQKAFLEEGFKKKAEEMNKEIQQlrdVIKDKKRNTDRIKD 590
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFANIIE 1812
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
493-580 |
1.21e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.48 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 493 AAEKEQDLLRQKQKEQQEYMEAQEKSHK---ENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGFKKKAEEMNK 569
Cdd:pfam03938 16 EGKAAQAQLEKKFKKRQAELEAKQKELQklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQP 95
|
90
....*....|.
gi 34786063 570 EIQQLRDVIKD 580
Cdd:pfam03938 96 IQDKINKAIKE 106
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
472-573 |
1.32e-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: 41.53 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 472 QADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQ---EYMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKl 548
Cdd:pfam05262 221 ELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKnlpKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALK- 299
|
90 100
....*....|....*....|....*
gi 34786063 549 MKDQKAFleeGFKKKAEEMNKEIQQ 573
Cdd:pfam05262 300 AKDHKAF---DLKQESKASEKEAED 321
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
485-593 |
1.43e-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: 41.06 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 485 AEERAQKVAAEKEQDL--LRQKQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEgfKK 562
Cdd:pfam13868 100 REQMDEIVERIQEEDQaeAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER--EE 177
|
90 100 110
....*....|....*....|....*....|....
gi 34786063 563 KAEEMNKEIQQLRDV---IKDKKRNTDRIKDALL 593
Cdd:pfam13868 178 IEEEKEREIARLRAQqekAQDEKAERDELRAKLY 211
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
474-589 |
1.85e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.35 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 474 DTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENLEQLRRKLeQEREQ---DIKDHDMMLKK--L 548
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPEL-TEKESsliDLKEHASSLASsgL 513
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 34786063 549 MKDQK-AFLEEGFKKKAEEMNK------EIQQLRDVIKDKKRNTDRIK 589
Cdd:pfam10174 514 KKDSKlKSLEIAVEQKKEECSKlenqlkKAHNAEEAVRTNPEINDRIR 561
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
481-573 |
2.81e-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: 38.87 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 481 EKAIAEERAQKVAAEkeqdllRQKQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKLMKDQKAFLEEGF 560
Cdd:pfam05672 41 ERLRKEELRRRAEEE------RARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEA 114
|
90
....*....|...
gi 34786063 561 KKKAEEMNKEIQQ 573
Cdd:pfam05672 115 ERQRQEREKIMQQ 127
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
483-565 |
3.62e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.17 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 483 AIAEE-----RAQKVAAEKEQdlLRQKQKEQQeymeAQEKSHKENLEQLR-RKLEQER--EQDIKDHDMMLKKLMKDQKA 554
Cdd:PRK09510 59 AVVEQynrqqQQQKSAKRAEE--QRKKKEQQQ----AEELQQKQAAEQERlKQLEKERlaAQEQKKQAEEAAKQAALKQK 132
|
90
....*....|.
gi 34786063 555 FLEEGFKKKAE 565
Cdd:PRK09510 133 QAEEAAAKAAA 143
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
481-582 |
4.75e-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: 39.52 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 481 EKAIAEERAQKVAAEKEQDLLRQKQKEQQEymeaqeksHKENLEQLRRKL---EQEREQDIKDHDMMLKK------LMKD 551
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQD--------EKAERDELRAKLyqeEQERKERQKEREEAEKKarqrqeLQQA 240
|
90 100 110
....*....|....*....|....*....|.
gi 34786063 552 QKAFLEEGFKKKAEEMNKEIQQLRDVIKDKK 582
Cdd:pfam13868 241 REEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
485-584 |
5.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 485 AEERAQKV--AAEKEQDLLRQKQKeqqeyMEAQEKSHKenleqLRRKLEQEREQDIKDHDMMLKKLMkdQKaflEEGFKK 562
Cdd:PRK12704 36 AEEEAKRIleEAKKEAEAIKKEAL-----LEAKEEIHK-----LRNEFEKELRERRNELQKLEKRLL--QK---EENLDR 100
|
90 100
....*....|....*....|....*
gi 34786063 563 KAEEMNK---EIQQLRDVIKDKKRN 584
Cdd:PRK12704 101 KLELLEKreeELEKKEKELEQKQQE 125
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
509-593 |
5.86e-03 |
|
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.
Pssm-ID: 214019 [Multi-domain] Cd Length: 161 Bit Score: 38.14 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 509 QEYMEAQEKSHKENLEQLRRKLEQEREQDIKDHDMMLKKL---MKDQKAFLEEGFKKKAEEmNKEIQQLRDVIKDKKRNT 585
Cdd:cd12926 56 EEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRiaeIHESRTKLEQDLRAQASD-NREIDKRMNSLKPDLMQL 134
|
....*...
gi 34786063 586 DRIKDALL 593
Cdd:cd12926 135 RKIRDQYL 142
|
|
| ARGLU |
pfam15346 |
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ... |
479-583 |
7.47e-03 |
|
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.
Pssm-ID: 405931 [Multi-domain] Cd Length: 151 Bit Score: 37.34 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 479 AGEKAIAEERA----QKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENLEQLRRKLEQEREQDIKDHDM----------M 544
Cdd:pfam15346 3 AESKLLEEETArrveEAVAKRVEEELEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELEEERRkeeeerkkreE 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 34786063 545 LKKLMKDQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKR 583
Cdd:pfam15346 83 LERILEENNRKIEEAQRKEAEERLAMLEEQRRMKEERQR 121
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
493-580 |
7.50e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 37.89 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 493 AAEKEQDLLRQKQKEQQEYMEAQEKSHKENLEQLRRKLE-------QEREQDIKDhdmMLKKLMKDQKAFLEEGFKKKAE 565
Cdd:COG2825 40 EGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAAtlseeerQKKERELQK---KQQELQRKQQEAQQDLQKRQQE 116
|
90
....*....|....*
gi 34786063 566 EMNKEIQQLRDVIKD 580
Cdd:COG2825 117 LLQPILEKIQKAIKE 131
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
487-576 |
7.70e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 38.84 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 487 ERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENLEQLRRKLEQ-------EREQDIKDHDMMLKKLMKDQKA-FLEE 558
Cdd:PRK06669 47 EQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSiieklqmQIEREQEEWEEELERLIEEAKAeGYEE 126
|
90
....*....|....*...
gi 34786063 559 GFKKKAEEMNKEIQQLRD 576
Cdd:PRK06669 127 GYEKGREEGLEEVRELIE 144
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
472-592 |
7.70e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 472 QADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKEN----LEQLRRKLEQ------EREQDIKDH 541
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERlereleERERRRARL 364
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 542 DMMLKKL----MKDQKAFLE-----EGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG4913 365 EALLAALglplPASAEEFAAlraeaAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
461-583 |
8.06e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 38.67 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 461 QSQAFIESSILQADTALTAGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEymEAQEKSHKENLEQlRRKLEQEREQdiKD 540
Cdd:TIGR02794 70 QKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQK--QAEEAKAKQAAEA-KAKAEAEAER--KA 144
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 34786063 541 HDMMLKKLMKDQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKR 583
Cdd:TIGR02794 145 KEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEA 187
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
479-591 |
8.20e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 479 AGEKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSH--KENLEQLRRKLEQEREQDikdhdmMLKKLMKDQKAfl 556
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEeaKKKADEAKKAAEAKKKAD------EAKKAEEAKKA-- 1524
|
90 100 110
....*....|....*....|....*....|....*
gi 34786063 557 EEGfkKKAEEMNKEiQQLRDVikDKKRNTDRIKDA 591
Cdd:PTZ00121 1525 DEA--KKAEEAKKA-DEAKKA--EEKKKADELKKA 1554
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
485-584 |
9.08e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 38.87 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34786063 485 AEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKshkenLEQLRRKLEQEREQDIKDHDmmlkKLMKDQKAFLEEGfKKKA 564
Cdd:COG3064 53 AEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA-----AAEAEKKAAAEKAKAAKEAE----AAAAAEKAAAAAE-KEKA 122
|
90 100
....*....|....*....|
gi 34786063 565 EEMNKEIQQLRDVIKDKKRN 584
Cdd:COG3064 123 EEAKRKAEEEAKRKAEEERK 142
|
|
| |
