|
Name |
Accession |
Description |
Interval |
E-value |
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
281-575 |
6.04e-149 |
|
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: 431.71 E-value: 6.04e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 281 EGIKVTGNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKE 360
Cdd:pfam02841 1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 361 AMAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKI 438
Cdd:pfam02841 81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 439 EHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKS 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 116812914 519 HKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
16-279 |
1.10e-141 |
|
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: 411.77 E-value: 1.10e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 16 NEQLSVNQEAIEILDKISQPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263 1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLHYVTELTELirakSSPNPAGIKNSTEFVSFFPDFV 175
Cdd:pfam02263 81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 176 WIVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
|
250 260
....*....|....*....|....
gi 116812914 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 |
8.56e-139 |
|
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: 405.42 E-value: 8.56e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 287 GNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKEAMAVFM 366
Cdd:cd16269 1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 367 EHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKIEHDYWQ 444
Cdd:cd16269 81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 445 VPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIE 524
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 116812914 525 QLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:cd16269 241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
31-272 |
3.52e-68 |
|
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: 221.04 E-value: 3.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 31 KISQPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:cd01851 2 DVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 109 NDLWIFALSVLLSSTFIYNSMITINHQALEQLHYVTELTElirakSSPNPAGIKNsteFVSFFPDFVWIVRDFMLELKLN 188
Cdd:cd01851 82 NDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 189 GEDITsddylenalkliPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKldSITEDQLDPKFQEVTKAFVS 268
Cdd:cd01851 154 GLDVT------------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQ 219
|
....
gi 116812914 269 YIFT 272
Cdd:cd01851 220 RFFS 223
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1-108 |
2.12e-05 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 46.68 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 1 MTQPQMAPICLVENHNEQLSVNQEAI-EILD--KISQPVVVVAIVGWSRTGKSYLMNCLAGQN-----HGFPlgstvqsQ 72
Cdd:COG3596 1 MSTEVSSLTERLEALKRLPQVLRELLaEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------C 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 116812914 73 TKGIwmWCMPHPTKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:COG3596 74 TREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
485-574 |
1.20e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 485 AEERAQKVAAEKEQDlLRQKQKEQQEYMEAQEKshKENIEQLRRKLMQEREQLIKDHnmmlKKQLKDQKAFLEEGFKKKA 564
Cdd:PRK09510 77 AEEQRKKKEQQQAEE-LQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALK----QKQAEEAAAKAAAAAKAKA 149
|
90
....*....|
gi 116812914 565 EEMNKEIQQL 574
Cdd:PRK09510 150 EAEAKRAAAA 159
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
471-592 |
1.16e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 471 LQA-DTALTAGKKAIAEERAQKVAAEKEQDLLRQ---KQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQL-----IKDH 541
Cdd:COG1579 12 LQElDSELDRLEHRLKELPAELAELEDELAALEArleAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 116812914 542 NMMLKK--QLKDQKAFLEE---GFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG1579 92 EALQKEieSLKRRISDLEDeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
486-592 |
4.05e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 486 EERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQL--IKDHNMMLKKQLKDQKAFLEEgFKKK 563
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkkLNEEKKELEEKVKDLTKKISS-LKEK 525
|
90 100
....*....|....*....|....*....
gi 116812914 564 AEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFEL 554
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
281-575 |
6.04e-149 |
|
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: 431.71 E-value: 6.04e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 281 EGIKVTGNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKE 360
Cdd:pfam02841 1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 361 AMAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKI 438
Cdd:pfam02841 81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 439 EHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKS 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 116812914 519 HKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
16-279 |
1.10e-141 |
|
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: 411.77 E-value: 1.10e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 16 NEQLSVNQEAIEILDKISQPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263 1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLHYVTELTELirakSSPNPAGIKNSTEFVSFFPDFV 175
Cdd:pfam02263 81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 176 WIVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
|
250 260
....*....|....*....|....
gi 116812914 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 |
8.56e-139 |
|
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: 405.42 E-value: 8.56e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 287 GNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKEAMAVFM 366
Cdd:cd16269 1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 367 EHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKIEHDYWQ 444
Cdd:cd16269 81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 445 VPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIE 524
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 116812914 525 QLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:cd16269 241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
31-272 |
3.52e-68 |
|
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: 221.04 E-value: 3.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 31 KISQPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:cd01851 2 DVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 109 NDLWIFALSVLLSSTFIYNSMITINHQALEQLHYVTELTElirakSSPNPAGIKNsteFVSFFPDFVWIVRDFMLELKLN 188
Cdd:cd01851 82 NDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 189 GEDITsddylenalkliPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKldSITEDQLDPKFQEVTKAFVS 268
Cdd:cd01851 154 GLDVT------------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQ 219
|
....
gi 116812914 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 |
1.14e-06 |
|
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: 48.61 E-value: 1.14e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116812914 40 AIVGWSRTGKSYLMNCLAGQNHGFPlgSTVQSQTKGIWMWCMPHPtKPEHTLVLLDTEGLGDVEKGDPKNDLWIFA 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 |
1.32e-06 |
|
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: 51.76 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 436 EKIEHDYW-----QVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAiaEERAQKVAAEKEQDLLR---QKQKE 507
Cdd:pfam12128 588 KRIDVPEWaaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASRE--ETFARTALKNARLDLRRlfdEKQSE 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 508 QQEyMEAQEKSHKENIEQLRRKLMQEREQLIKDHnmmlkkqlkdqKAFLEEgFKKKAEEMNKEIQQ-LRDVIKDKKRNTD 586
Cdd:pfam12128 666 KDK-KNKALAERKDSANERLNSLEAQLKQLDKKH-----------QAWLEE-QKEQKREARTEKQAyWQVVEGALDAQLA 732
|
....*..
gi 116812914 587 RIKDALL 593
Cdd:pfam12128 733 LLKAAIA 739
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
316-591 |
4.19e-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: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 316 LAQRENSVAVQKAADHYSEQMAQRLRLptetlqelldvhaacEKEAMAVFMEHSFKDEN-----QQFLKKLVELIGENKE 390
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQ---------------EKEEKAREVERRRKLEEaekarQAEMDRQAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 391 LFLSKNEEASNKYCQE---ELDRLSKDF----MENISTFfvpcgHKLYMDKREKIEH--DYWQVPRKGVKASEVFQSFLQ 461
Cdd:pfam17380 342 MAMERERELERIRQEErkrELERIRQEEiameISRMREL-----ERLQMERQQKNERvrQELEAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 462 SQAFIESSI-LQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQ----------EKSHKENIEQLRRKL 530
Cdd:pfam17380 417 QQKVEMEQIrAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEErkrkklelekEKRDRKRAEEQRRKI 496
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116812914 531 ----MQEREQLI---KDHNMMLKKQLKD-QKAFLEEGFKKKAEEMNKEIQQlrdvIKDKKRNTDRIKDA 591
Cdd:pfam17380 497 lekeLEERKQAMieeERKRKLLEKEMEErQKAIYEEERRREAEEERRKQQE----MEERRRIQEQMRKA 561
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
1-108 |
2.12e-05 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 46.68 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 1 MTQPQMAPICLVENHNEQLSVNQEAI-EILD--KISQPVVVVAIVGWSRTGKSYLMNCLAGQN-----HGFPlgstvqsQ 72
Cdd:COG3596 1 MSTEVSSLTERLEALKRLPQVLRELLaEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------C 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 116812914 73 TKGIwmWCMPHPTKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:COG3596 74 TREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
485-574 |
1.20e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 485 AEERAQKVAAEKEQDlLRQKQKEQQEYMEAQEKshKENIEQLRRKLMQEREQLIKDHnmmlKKQLKDQKAFLEEGFKKKA 564
Cdd:PRK09510 77 AEEQRKKKEQQQAEE-LQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALK----QKQAEEAAAKAAAAAKAKA 149
|
90
....*....|
gi 116812914 565 EEMNKEIQQL 574
Cdd:PRK09510 150 EAEAKRAAAA 159
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
482-591 |
6.40e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 482 KAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSH-KENIEQLRRKLMQER--EQLIKDHNMM-----LKKQLKDQK 553
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEeAKKADEAKKKAEEAKkaEEAKKKAEEAkkadeAKKKAEEAK 1483
|
90 100 110
....*....|....*....|....*....|....*...
gi 116812914 554 AflEEGFKKKAEEMNKEIQQLRDVIKDKKRnTDRIKDA 591
Cdd:PTZ00121 1484 K--ADEAKKKAEEAKKKADEAKKAAEAKKK-ADEAKKA 1518
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
472-591 |
7.39e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 472 QADTALTAGKKAIAEE--RAQKVAAEKEQDLLRQKQKEQQEYMEAQEKShkENIEQLRRKLMQEREQLIKDHNMMLKKQL 549
Cdd:PTZ00121 1535 KADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKA--EEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 116812914 550 KDQKaflEEGFK----KKAEEMNKEIQQLRDVIKDKKRNTDRIKDA 591
Cdd:PTZ00121 1613 KKAE---EAKIKaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
481-593 |
7.57e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 481 KKAIAEERAQKV--AAEKEQDLLRQKQKEQ--QEYMEAQEKSHKENIEqlRRKLMQEREQLIKDHNMMLKKQLkdqkafl 556
Cdd:PRK12704 32 KIKEAEEEAKRIleEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRE--RRNELQKLEKRLLQKEENLDRKL------- 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 116812914 557 eEGFKKKAEEMNK---EIQQLRDVIKDKKRNTDRIKDALL 593
Cdd:PRK12704 103 -ELLEKREEELEKkekELEQKQQELEKKEEELEELIEEQL 141
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
485-572 |
8.83e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 485 AEERAQKVAAEKEqdllRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKA 564
Cdd:PRK09510 89 AEELQQKQAAEQE----RLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA 164
|
....*...
gi 116812914 565 EEMNKEIQ 572
Cdd:PRK09510 165 AEAKKKAE 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
471-592 |
1.16e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 471 LQA-DTALTAGKKAIAEERAQKVAAEKEQDLLRQ---KQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQL-----IKDH 541
Cdd:COG1579 12 LQElDSELDRLEHRLKELPAELAELEDELAALEArleAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEY 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 116812914 542 NMMLKK--QLKDQKAFLEE---GFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG1579 92 EALQKEieSLKRRISDLEDeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
451-593 |
1.45e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 451 KASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKE-----NIEQ 525
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakKAEE 1706
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116812914 526 LRRKLMQER---EQLIK--DHNMMLKKQLKDQkaflEEGFKKKAEEMNKE------IQQLRDVIKDKKRNTDRIKDALL 593
Cdd:PTZ00121 1707 LKKKEAEEKkkaEELKKaeEENKIKAEEAKKE----AEEDKKKAEEAKKDeeekkkIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
486-575 |
1.45e-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: 39.64 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 486 EERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKEnIEQLRRKLMQEREQLikdhnMMLKKQLKDQKAFLEEGFKKKAE 565
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLEKEEEERLR-KEELRRRAEEERARR-----EEEARRLEEERRREEEERQRKAE 82
|
90
....*....|
gi 116812914 566 EMNKEIQQLR 575
Cdd:pfam05672 83 EEAEEREQRE 92
|
|
| iSH2_PIK3R2 |
cd12926 |
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ... |
509-593 |
1.51e-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: 39.68 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 509 QEYMEAQEKSHKENIEQLRRKLMQEREQLIKDHNMMLKK---QLKDQKAFLEEGFKKKAEEmNKEIQQLRDVIKDKKRNT 585
Cdd:cd12926 56 EEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSriaEIHESRTKLEQDLRAQASD-NREIDKRMNSLKPDLMQL 134
|
....*...
gi 116812914 586 DRIKDALL 593
Cdd:cd12926 135 RKIRDQYL 142
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
294-594 |
2.24e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 294 VTTYVDAINSGAVpcLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVhaacekeamavfmehSFKDE 373
Cdd:COG3206 83 LETQIEILKSRPV--LERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVIEI---------------SYTSP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 374 NQQFLKKLVELIGEN--KELFLSKNEEASN--KYCQEELDRLskdfmenistffvpcghklymdkREKIEhdywqvprkg 449
Cdd:COG3206 146 DPELAAAVANALAEAylEQNLELRREEARKalEFLEEQLPEL-----------------------RKELE---------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 450 vKASEVFQSFLQSQAFIESS--ILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKS-----HKEN 522
Cdd:COG3206 193 -EAEAALEEFRQKNGLVDLSeeAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqLRAQ 271
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116812914 523 IEQLRRKLMQEREQLIKDHNMM--LKKQLKDQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDALLN 594
Cdd:COG3206 272 LAELEAELAELSARYTPNHPDViaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
472-583 |
2.40e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 472 QADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQLIK-DHNmmlKKQLK 550
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSElRAN---ESRLR 246
|
90 100 110
....*....|....*....|....*....|...
gi 116812914 551 DQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKR 583
Cdd:PRK11637 247 DSIARAEREAKARAEREAREAARVRDKQKQAKR 279
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
481-573 |
2.53e-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: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 481 KKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQ-------------------EKSHKENIEQLRRKLMQEREQLIKDH 541
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERdelraklyqeeqerkerqkEREEAEKKARQRQELQQAREEQIELK 248
|
90 100 110
....*....|....*....|....*....|..
gi 116812914 542 NMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQ 573
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQAEDEEIEQEE 280
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
486-592 |
4.05e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 486 EERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQL--IKDHNMMLKKQLKDQKAFLEEgFKKK 563
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkkLNEEKKELEEKVKDLTKKISS-LKEK 525
|
90 100
....*....|....*....|....*....
gi 116812914 564 AEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFEL 554
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
486-573 |
4.30e-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: 38.10 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 486 EERAQKVAAEkeqdllRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAE 565
Cdd:pfam05672 46 EELRRRAEEE------RARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQ 119
|
....*...
gi 116812914 566 EMNKEIQQ 573
Cdd:pfam05672 120 EREKIMQQ 127
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
476-611 |
4.72e-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: 39.75 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 476 ALTAGKKAIAEERAQKvAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIEQLR--RKLMQEREQLIKDhnmmLKKQLKDQK 553
Cdd:COG4942 8 ALLLALAAAAQADAAA-EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRA----LEQELAALE 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116812914 554 AFLEEgFKKKAEEMNKEIQQLRDVIKD------KKRNTDRIKdALLNGFSTVLFHYLVRYLKHL 611
Cdd:COG4942 83 AELAE-LEKEIAELRAELEAQKEELAEllralyRLGRQPPLA-LLLSPEDFLDAVRRLQYLKYL 144
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
485-569 |
4.81e-03 |
|
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: 39.93 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 485 AEERAQKVAAE---KEQDLLRQKQKEQQEYMEAQEKSHKENIEQL-----RRKLMQEREQLikdhNMMLKKQLKDQKAFL 556
Cdd:pfam15709 417 AQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQRQKELEMQLaeeqkRLMEMAEEERL----EYQRQKQEAEEKARL 492
|
90
....*....|....
gi 116812914 557 E-EGFKKKAEEMNK 569
Cdd:pfam15709 493 EaEERRQKEEEAAR 506
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
481-590 |
5.27e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 481 KKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKEN---IEQLRRKLMQER----------------EQLIKDH 541
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENkikAEEAKKEAEEDKkkaeeakkdeeekkkiAHLKKEE 1766
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 116812914 542 NMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQlrdVIKDKKRNTDRIKD 590
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFANIIE 1812
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
485-593 |
5.86e-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: 39.13 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 485 AEERAQKVAAEKEQDL--LRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEgfKK 562
Cdd:pfam13868 100 REQMDEIVERIQEEDQaeAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER--EE 177
|
90 100 110
....*....|....*....|....*....|....
gi 116812914 563 KAEEMNKEIQQLRDV---IKDKKRNTDRIKDALL 593
Cdd:pfam13868 178 IEEEKEREIARLRAQqekAQDEKAERDELRAKLY 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-69 |
8.32e-03 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 37.92 E-value: 8.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 116812914 27 EILDKIS---QPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTV 69
Cdd:cd03213 23 QLLKNVSgkaKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEV 68
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
477-592 |
8.83e-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: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 477 LTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQE-----KSHKENIEQLRrklmQEREQLIKDHNMM--LKKQL 549
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdeidvASAEREIAELE----AELERLDASSDDLaaLEEQL 694
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 116812914 550 KDQKAFLEEgFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG4913 695 EELEAELEE-LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
481-573 |
9.06e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.04 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 481 KKAIAEERAQKVAAEKEQ------DLLRQKQKEQQEYMEAQEKSHKEnIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKA 554
Cdd:PRK00409 528 LERELEQKAEEAEALLKEaeklkeELEEKKEKLQEEEDKLLEEAEKE-AQQAIKEAKKEADEIIKELRQLQKGGYASVKA 606
|
90
....*....|....*....
gi 116812914 555 fleegfkKKAEEMNKEIQQ 573
Cdd:PRK00409 607 -------HELIEARKRLNK 618
|
|
|