|
Name |
Accession |
Description |
Interval |
E-value |
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
283-579 |
2.93e-160 |
|
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: 460.99 E-value: 2.93e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 283 EGIMVNGNRLATLVTTYVDAINSGAVPCLENAVTTLAQRENSAAVQKAAEHYSEQMAQRLRLPTDTLQELLDVHSACEKE 362
Cdd:pfam02841 1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 363 AIAVFMEHSFKDENQEFQKNLVVTIVEKREDFSRQNEAASLSHCQAELDKLSESLRESISCGAFSVPGGHSLYLEARKKV 442
Cdd:pfam02841 81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 443 EQDYEQVPRKGVKANHVLQSFLQSQIVIENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQERS 522
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958755446 523 YKENIVQLHEKMETERKNILEKQEEMLAHKLKVQEEMLNEGFKRKYEAMDSEISQLQ 579
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
18-281 |
4.76e-160 |
|
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: 459.15 E-value: 4.76e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 18 NEELRVNPKAINILERITQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFNLGTTVRSETKGIWMWCVPHPCKPKFTLVLLD 97
Cdd:pfam02263 1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 98 TEGLGDVEKCDPKNDSWIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTELirtkSTPRSEEIDDSDEFVGFFPDFI 177
Cdd:pfam02263 81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 178 WVVRDFVLELKLDGRVITADEYLENALKLIPGRSLKAQNSNLPRECIRHFFPRRKCFVFDRPIKEKELLVHVEEMPEDEL 257
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
|
250 260
....*....|....*....|....
gi 1958755446 258 DHNFREQSNVFCSYIFSNAKAKTL 281
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
289-579 |
4.04e-147 |
|
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: 427.38 E-value: 4.04e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 289 GNRLATLVTTYVDAINSGAVPCLENAVTTLAQRENSAAVQKAAEHYSEQMAQRLRLPTDTLQELLDVHSACEKEAIAVFM 368
Cdd:cd16269 1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 369 EHSFKDENQEFQKNLVVTIVEKREDFSRQNEAASLSHCQAELDKLSESLRESISCGAFSVPGGHSLYLEARKKVEQDYEQ 448
Cdd:cd16269 81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 449 VPRKGVKANHVLQSFLQSQIVIENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQERSYKENIV 528
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958755446 529 QLHEKMETERKNILEKQEEMLAHKLKVQEEMLNEGFKRKYEAMDSEISQLQ 579
Cdd:cd16269 241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
32-275 |
7.28e-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: 220.66 E-value: 7.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 32 ERITQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFNLGTTVRSETKGIWMWCVPHP--CKPKFTLVLLDTEGLGDVEKCDP 109
Cdd:cd01851 1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 110 KNDSWIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTELirtkstprSEEIDDSDEFVGFFPDFIWVVRDFVLELKL 189
Cdd:cd01851 81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTALE--------TLGLAGLHNFSKPKPLLLFVVRDFTGPTPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 190 DGRVITADEYLENALKlipgrslkaqnsNLPRECIRHFFPRRKCFVFDRPIKEKELLVHveEMPEDELDHNFREQSNVFC 269
Cdd:cd01851 153 EGLDVTEKSETLIEEL------------NKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALR 218
|
....*.
gi 1958755446 270 SYIFSN 275
Cdd:cd01851 219 QRFFSS 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
437-595 |
3.56e-05 |
|
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: 46.30 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 437 EARKKVEQDYEQVPRKGVKANHVLQSFLQSQIVIENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVM 516
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958755446 517 ESQERSYKENIVQLHEKMETERKNILEKQEEMLahklkvQEEMLNEGFKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQ 595
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFL------DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
490-592 |
6.58e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 490 VERAQKEAAEKEQELLRQKQKELQQVMESQERSYKE--NIVQLHEKMETERKNILEKQEEMLAHK---LKVQEEMLNEgF 564
Cdd:PRK12704 44 LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRErrNELQKLEKRLLQKEENLDRKLELLEKReeeLEKKEKELEQ-K 122
|
90 100
....*....|....*....|....*...
gi 1958755446 565 KRKYEAMDSEISQLQKQIQQNKEQNSSL 592
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQELERISGL 150
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
460-598 |
7.24e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 460 LQSFLQSQ----IVIENSILQSDKAL-----TVNQKAMEVERAQKEAAEKEQELlRQKQKELQQVmESQERSYKENIVQL 530
Cdd:TIGR04523 312 LKSELKNQekklEEIQNQISQNNKIIsqlneQISQLKKELTNSESENSEKQREL-EEKQNEIEKL-KKENQSYKQEIKNL 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958755446 531 hekmeTERKNILEKqeemlahKLKVQEEmLNEGFKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQIFD 598
Cdd:TIGR04523 390 -----ESQINDLES-------KIQNQEK-LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
32-110 |
1.12e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 41.68 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 32 ERITQPVVVVAIVGLYRTGKSYLMNRLAGQnhgfNLGTT--VRSETKGIwmWCVPHPCKPKFTLVLLDTEGLGDVEKCDP 109
Cdd:COG3596 33 LLVELPPPVIALVGKTGAGKSSLINALFGA----EVAEVgvGRPCTREI--QRYRLESDGLPGLVLLDTPGLGEVNERDR 106
|
.
gi 1958755446 110 K 110
Cdd:COG3596 107 E 107
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
473-586 |
3.88e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 473 SILQSDKALTVNQKAMEVE-----RAQKEAAEKEQELLRQKQKELQQVMESQERSYKENIVQLHEKMETERKNILEKQEE 547
Cdd:smart00787 154 EGLKEDYKLLMKELELLNSikpklRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEE 233
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958755446 548 MLAHKLKVQEEmlnegfKRKYEAMDSEISQLQKQIQQNK 586
Cdd:smart00787 234 LQELESKIEDL------TNKKSELNTEIAEAEKKLEQCR 266
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
283-579 |
2.93e-160 |
|
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: 460.99 E-value: 2.93e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 283 EGIMVNGNRLATLVTTYVDAINSGAVPCLENAVTTLAQRENSAAVQKAAEHYSEQMAQRLRLPTDTLQELLDVHSACEKE 362
Cdd:pfam02841 1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 363 AIAVFMEHSFKDENQEFQKNLVVTIVEKREDFSRQNEAASLSHCQAELDKLSESLRESISCGAFSVPGGHSLYLEARKKV 442
Cdd:pfam02841 81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 443 EQDYEQVPRKGVKANHVLQSFLQSQIVIENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQERS 522
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1958755446 523 YKENIVQLHEKMETERKNILEKQEEMLAHKLKVQEEMLNEGFKRKYEAMDSEISQLQ 579
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
18-281 |
4.76e-160 |
|
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: 459.15 E-value: 4.76e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 18 NEELRVNPKAINILERITQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFNLGTTVRSETKGIWMWCVPHPCKPKFTLVLLD 97
Cdd:pfam02263 1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 98 TEGLGDVEKCDPKNDSWIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTELirtkSTPRSEEIDDSDEFVGFFPDFI 177
Cdd:pfam02263 81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 178 WVVRDFVLELKLDGRVITADEYLENALKLIPGRSLKAQNSNLPRECIRHFFPRRKCFVFDRPIKEKELLVHVEEMPEDEL 257
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
|
250 260
....*....|....*....|....
gi 1958755446 258 DHNFREQSNVFCSYIFSNAKAKTL 281
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
289-579 |
4.04e-147 |
|
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: 427.38 E-value: 4.04e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 289 GNRLATLVTTYVDAINSGAVPCLENAVTTLAQRENSAAVQKAAEHYSEQMAQRLRLPTDTLQELLDVHSACEKEAIAVFM 368
Cdd:cd16269 1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 369 EHSFKDENQEFQKNLVVTIVEKREDFSRQNEAASLSHCQAELDKLSESLRESISCGAFSVPGGHSLYLEARKKVEQDYEQ 448
Cdd:cd16269 81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 449 VPRKGVKANHVLQSFLQSQIVIENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQERSYKENIV 528
Cdd:cd16269 161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1958755446 529 QLHEKMETERKNILEKQEEMLAHKLKVQEEMLNEGFKRKYEAMDSEISQLQ 579
Cdd:cd16269 241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
32-275 |
7.28e-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: 220.66 E-value: 7.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 32 ERITQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFNLGTTVRSETKGIWMWCVPHP--CKPKFTLVLLDTEGLGDVEKCDP 109
Cdd:cd01851 1 LDVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 110 KNDSWIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTELirtkstprSEEIDDSDEFVGFFPDFIWVVRDFVLELKL 189
Cdd:cd01851 81 ENDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTALE--------TLGLAGLHNFSKPKPLLLFVVRDFTGPTPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 190 DGRVITADEYLENALKlipgrslkaqnsNLPRECIRHFFPRRKCFVFDRPIKEKELLVHveEMPEDELDHNFREQSNVFC 269
Cdd:cd01851 153 EGLDVTEKSETLIEEL------------NKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALR 218
|
....*.
gi 1958755446 270 SYIFSN 275
Cdd:cd01851 219 QRFFSS 224
|
|
| Ras_like_GTPase |
cd00882 |
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ... |
42-105 |
1.97e-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: 50.92 E-value: 1.97e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958755446 42 AIVGLYRTGKSYLMNRLAGQNhgFNLGTTVRSETKGIWMWCVPHPcKPKFTLVLLDTEGLGDVE 105
Cdd:cd00882 1 VVVGRGGVGKSSLLNALLGGE--VGEVSDVPGTTRDPDVYVKELD-KGKVKLVLVDTPGLDEFG 61
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
390-588 |
3.18e-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: 47.04 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 390 KREDFSRQNEAASLSHCQAELDKLSESLResiscgafsvpgghsLYLEARKK---VEQDYEQVPRKGVKANHVLQSFLQS 466
Cdd:pfam17380 354 RQEERKRELERIRQEEIAMEISRMRELER---------------LQMERQQKnerVRQELEAARKVKILEEERQRKIQQQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 467 QIVIENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQERSYKENIVQLHEK---METERKNILE 543
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDrkrAEEQRRKILE 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1958755446 544 KqeEMLAHKLKVQEEmlnegfKRKYEAMDSEISQLQKQIQQNKEQ 588
Cdd:pfam17380 499 K--ELEERKQAMIEE------ERKRKLLEKEMEERQKAIYEEERR 535
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
437-595 |
3.56e-05 |
|
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: 46.30 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 437 EARKKVEQDYEQVPRKGVKANHVLQSFLQSQIVIENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVM 516
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958755446 517 ESQERSYKENIVQLHEKMETERKNILEKQEEMLahklkvQEEMLNEGFKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQ 595
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFL------DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
490-592 |
6.58e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 490 VERAQKEAAEKEQELLRQKQKELQQVMESQERSYKE--NIVQLHEKMETERKNILEKQEEMLAHK---LKVQEEMLNEgF 564
Cdd:PRK12704 44 LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRErrNELQKLEKRLLQKEENLDRKLELLEKReeeLEKKEKELEQ-K 122
|
90 100
....*....|....*....|....*...
gi 1958755446 565 KRKYEAMDSEISQLQKQIQQNKEQNSSL 592
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQELERISGL 150
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
479-596 |
2.72e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 479 KALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQER-----SYKENIVQLHEKMETERKNILEKQEEMLAHKL 553
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleeleERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1958755446 554 KVQEEMLNE--GFKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQI 596
Cdd:COG4717 185 QLSLATEEElqDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
485-588 |
4.22e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.40 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 485 QKAMEVERAQKEaaEKEQELLRQKQKELQQVM----ESQERSYKENIVQLHEKMETERknilEKQEEMLAhKLKVQEEML 560
Cdd:pfam15709 345 MRRLEVERKRRE--QEEQRRLQQEQLERAEKMreelELEQQRRFEEIRLRKQRLEEER----QRQEEEER-KQRLQLQAA 417
|
90 100
....*....|....*....|....*...
gi 1958755446 561 NEGFKRKYEAMDSEISQLQKQIQQNKEQ 588
Cdd:pfam15709 418 QERARQQQEEFRRKLQELQRKKQQEEAE 445
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
476-595 |
5.82e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 42.82 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 476 QSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQER-SYKENIVQLHEKMETERKNILEKQEEMLAHKLK 554
Cdd:pfam09731 303 LAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRlEFEREREEIRESYEEKLRTELERQAEAHEEHLK 382
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958755446 555 ----VQEEMLN---------------EGFKRKYEAMDSEISQLQKQIQQNKE-QNSSLAAQ 595
Cdd:pfam09731 383 dvlvEQEIELQreflqdikekveeerAGRLLKLNELLANLKGLEKATSSHSEvEDENRKAQ 443
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
319-594 |
6.56e-04 |
|
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: 42.80 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 319 AQRENSAAVQKAAEHYSEQmaQRLRLPTdtlqelldvhsacEKEAIAVFMEHSFKDENQEFQKNLVVTIVEKREdfsrqn 398
Cdd:pfam17380 321 AEKARQAEMDRQAAIYAEQ--ERMAMER-------------ERELERIRQEERKRELERIRQEEIAMEISRMRE------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 399 eaasLSHCQAELDKLSESLRESiscgafsvpgghslyLEARKKVEQDYEQVPRKGVKANHVLQSFLQSQiviENSILQSD 478
Cdd:pfam17380 380 ----LERLQMERQQKNERVRQE---------------LEAARKVKILEEERQRKIQQQKVEMEQIRAEQ---EEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 479 KALTvNQKAMEVERAQKEAAEKEQ--ELLRQ-------------KQKELQQVMESQERSYKENIVQLHEK--METERK-N 540
Cdd:pfam17380 438 RRLE-EERAREMERVRLEEQERQQqvERLRQqeeerkrkkleleKEKRDRKRAEEQRRKILEKELEERKQamIEEERKrK 516
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1958755446 541 ILEKQEEMLAHKLKVQEEMLNEGFKRKYEAMDSEISQLQKQIQQNKEQNSSLAA 594
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEA 570
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
460-598 |
7.24e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 460 LQSFLQSQ----IVIENSILQSDKAL-----TVNQKAMEVERAQKEAAEKEQELlRQKQKELQQVmESQERSYKENIVQL 530
Cdd:TIGR04523 312 LKSELKNQekklEEIQNQISQNNKIIsqlneQISQLKKELTNSESENSEKQREL-EEKQNEIEKL-KKENQSYKQEIKNL 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958755446 531 hekmeTERKNILEKqeemlahKLKVQEEmLNEGFKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQIFD 598
Cdd:TIGR04523 390 -----ESQINDLES-------KIQNQEK-LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
436-595 |
9.01e-04 |
|
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: 42.42 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 436 LEARKKVEQDYEQV----PRKGVKANhvlqsflqSQIVIENSILQSDKALTVNQKAMEvERAQKEAAEK-EQELLRQKQK 510
Cdd:pfam17380 236 MERRKESFNLAEDVttmtPEYTVRYN--------GQTMTENEFLNQLLHIVQHQKAVS-ERQQQEKFEKmEQERLRQEKE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 511 ELQQVMESQ------------ERSYKENIVQLHEKMETERKNILE--------------KQEEMLAHKLKVQE-EMLNEG 563
Cdd:pfam17380 307 EKAREVERRrkleeaekarqaEMDRQAAIYAEQERMAMERERELErirqeerkreleriRQEEIAMEISRMRElERLQME 386
|
170 180 190
....*....|....*....|....*....|..
gi 1958755446 564 FKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQ 595
Cdd:pfam17380 387 RQQKNERVRQELEAARKVKILEEERQRKIQQQ 418
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
412-595 |
9.93e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.32 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 412 KLSESLRESISCGAFSVPGghslylearkkveqdyeqVPRKGVKANHVLQSFLQS----QIVIENSILQSDKALTVNQKA 487
Cdd:pfam05667 251 RIAEQLRSAALAGTEATSG------------------ASRSAQDLAELLSSFSGSsttdTGLTKGSRFTHTEKLQFTNEA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 488 MEVERAQKEAAEKEQELLRQKQKELQQV-------------MESQERSYKENIVQLHEKMETERKNILEKQEEMLAHKLK 554
Cdd:pfam05667 313 PAATSSPPTKVETEEELQQQREEELEELqeqledlessiqeLEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKT 392
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1958755446 555 VqeEMLNEGfkrkyeamDSEISQLQKQIQQNKEQNSSLAAQ 595
Cdd:pfam05667 393 L--DLLPDA--------EENIAKLQALVDASAQRLVELAGQ 423
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
471-596 |
1.02e-03 |
|
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: 42.35 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 471 ENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQV----------MESQERSYKENIVQLHEKME--TER 538
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleeLSRQISALRKDLARLEAEVEqlEER 748
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1958755446 539 KNILEKQEEMLAHKLKVQEEMLNEGFKRKYEAmDSEISQLQKQIQQNKEQNSSLAAQI 596
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEA-EAEIEELEAQIEQLKEELKALREAL 805
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
32-110 |
1.12e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 41.68 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 32 ERITQPVVVVAIVGLYRTGKSYLMNRLAGQnhgfNLGTT--VRSETKGIwmWCVPHPCKPKFTLVLLDTEGLGDVEKCDP 109
Cdd:COG3596 33 LLVELPPPVIALVGKTGAGKSSLINALFGA----EVAEVgvGRPCTREI--QRYRLESDGLPGLVLLDTPGLGEVNERDR 106
|
.
gi 1958755446 110 K 110
Cdd:COG3596 107 E 107
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
296-595 |
1.31e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 296 VTTYVDAINSGAVpcLENAVTTLaqrensaavqKAAEHYSEQMAQRLRLpTDTLQELLDVHSACEKEAIAVfmehSFKDE 375
Cdd:COG3206 83 LETQIEILKSRPV--LERVVDKL----------NLDEDPLGEEASREAA-IERLRKNLTVEPVKGSNVIEI----SYTSP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 376 NQEFQKNLVVTIVE--KREDFSRQNEAAS--LSHCQAELDKLSESLRES--------ISCGAFSVPGGHSLYLEARKKVE 443
Cdd:COG3206 146 DPELAAAVANALAEayLEQNLELRREEARkaLEFLEEQLPELRKELEEAeaaleefrQKNGLVDLSEEAKLLLQQLSELE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 444 QDYEQVPRKGVKANHVLQSfLQSQIVIENSILQSDKALTVNQKameveraqkeaaekeqelLRQKQKELQQVMESQERSY 523
Cdd:COG3206 226 SQLAEARAELAEAEARLAA-LRAQLGSGPDALPELLQSPVIQQ------------------LRAQLAELEAELAELSARY 286
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958755446 524 KEN---IVQLHEKMETERKNILEKQEEMLAhKLKVQeemlnegfkrkYEAMDSEISQLQKQIQQNKEQNSSLAAQ 595
Cdd:COG3206 287 TPNhpdVIALRAQIAALRAQLQQEAQRILA-SLEAE-----------LEALQAREASLQAQLAQLEARLAELPEL 349
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
492-596 |
2.13e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 492 RAQKEAAEKEQEL---LRQKQKELQ----QVMESQERSYKENIVQLHEKMETERKNILEKQEEMLAHKLKVQEEMLN-EG 563
Cdd:COG1196 206 ERQAEKAERYRELkeeLKELEAELLllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELElEE 285
|
90 100 110
....*....|....*....|....*....|...
gi 1958755446 564 FKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQI 596
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
427-588 |
2.43e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 40.99 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 427 SVPGGHSLYLEARKKVEQDYEQVpRKGVKANHVLQSFLQSQIvieNSILQSDKALT--VNQKAMEVERAQKeaaeKEQEL 504
Cdd:pfam09726 385 CIPNNQLSKPDALVRLEQDIKKL-KAELQASRQTEQELRSQI---SSLTSLERSLKseLGQLRQENDLLQT----KLHNA 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 505 L--RQKQKELQQVMESQERSYKENIVQLHEKMETERKNilEKQEEMLAHKLKVQEEMLN----EGFKRKYEAMDSEISQL 578
Cdd:pfam09726 457 VsaKQKDKQTVQQLEKRLKAEQEARASAEKQLAEEKKR--KKEEEATAARAVALAAASRgectESLKQRKRELESEIKKL 534
|
170
....*....|
gi 1958755446 579 QKQIQQNKEQ 588
Cdd:pfam09726 535 THDIKLKEEQ 544
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
373-596 |
2.47e-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: 41.16 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 373 KDENQEFQKNLVVTIVEKREDFSR-QNEAASLSHCQAELDKLSESLRESIScgafsvpgghsLYLEARKKVEQDYEQVPR 451
Cdd:TIGR04523 421 KELLEKEIERLKETIIKNNSEIKDlTNQDSVKELIIKNLDNTRESLETQLK-----------VLSRSINKIKQNLEQKQK 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 452 KGVKANHVLQSFLQSQIVIENSI---LQSDKALTVNQKAMEVERAQKEA--AEKEQELLRQKQKELQQVMESQERSYKEN 526
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVkdlTKKISSLKEKIEKLESEKKEKESkiSDLEDELNKDDFELKKENLEKEIDEKNKE 569
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 527 IVQLHEkmetERKNILEKQEEmlAHKLKVQEEMLNEGFKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQI 596
Cdd:TIGR04523 570 IEELKQ----TQKSLKKKQEE--KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
506-596 |
2.75e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.45 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 506 RQKQKELQQVMESQERSykeniVQLHEKMETERKNILEKQEEMLAH---KLKVQEEMLNEgFKRKYEAMDSEISQLQkqi 582
Cdd:PRK11637 46 RDQLKSIQQDIAAKEKS-----VRQQQQQRASLLAQLKKQEEAISQasrKLRETQNTLNQ-LNKQIDELNASIAKLE--- 116
|
90
....*....|....
gi 1958755446 583 QQNKEQNSSLAAQI 596
Cdd:PRK11637 117 QQQAAQERLLAAQL 130
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
485-588 |
2.93e-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: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 485 QKAMEVERAQKEAAEKEQEL-LRQKQKELQQVMESQERSYKENIVQLHEKMETERKNILEKQEEMLAHKLKVQEEMLNEG 563
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEeRKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100
....*....|....*....|....*
gi 1958755446 564 fKRKYEAMDSEISQLQKQIQQNKEQ 588
Cdd:pfam13868 126 -RQLREEIDEFNEEQAEWKELEKEE 149
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
495-596 |
2.98e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 495 KEAAEKEQELLRQKQKELQQVMESQERSYKENIVQLHEKMETE---RKNILEKQEEmlahKLKVQEEMLNegfkRKYEAM 571
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElreRRNELQKLEK----RLLQKEENLD----RKLELL 105
|
90 100
....*....|....*....|....*
gi 1958755446 572 DSEISQLQKQIQQNKEQNSSLAAQI 596
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKE 130
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
473-588 |
3.52e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 473 SILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQERSYKENIVQLHEKMETERKNILEKQEEMLAHK 552
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958755446 553 LKVQEEM---LNEGFKRKYEAMDSEISQLQKQIQQNKEQ 588
Cdd:COG1196 737 LLEELLEeeeLLEEEALEELPEPPDLEELERELERLERE 775
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
474-596 |
3.79e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 474 ILQSDKALTVNQKAMEVERAQKEAAEKEQELlRQKQKELQQVmESQERSYKENIVQLHEKMETERKNILEKQEEmlahkL 553
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREEL-EQAREELEQL-EEELEQARSELEQLEEELEELNEQLQAAQAE-----L 96
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958755446 554 KVQEEMLNEgFKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQI 596
Cdd:COG4372 97 AQAQEELES-LQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
473-586 |
3.88e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 473 SILQSDKALTVNQKAMEVE-----RAQKEAAEKEQELLRQKQKELQQVMESQERSYKENIVQLHEKMETERKNILEKQEE 547
Cdd:smart00787 154 EGLKEDYKLLMKELELLNSikpklRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEE 233
|
90 100 110
....*....|....*....|....*....|....*....
gi 1958755446 548 MLAHKLKVQEEmlnegfKRKYEAMDSEISQLQKQIQQNK 586
Cdd:smart00787 234 LQELESKIEDL------TNKKSELNTEIAEAEKKLEQCR 266
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
437-590 |
4.44e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 437 EARKKVEQDYEQVpRKGVKanhvlqsflqsQIVIENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVM 516
Cdd:COG5185 286 NLIKQFENTKEKI-AEYTK-----------SIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 517 ESQE--RSYKENIV------QLHEKMETERKNILEKQEE--MLAHKLKVQEEMLNEGFKRKYEAMDSEISQLQKQIQQNK 586
Cdd:COG5185 354 ENLEaiKEEIENIVgevelsKSSEELDSFKDTIESTKESldEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQAT 433
|
....
gi 1958755446 587 EQNS 590
Cdd:COG5185 434 SSNE 437
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
485-558 |
4.72e-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: 4.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958755446 485 QKAMEVERA---QKEAAEKEQELLRQKQKELQQVMESQERSYKENIVQLHEkmetERKNILE-KQEEMLAHKLKVQEE 558
Cdd:pfam15709 413 QLQAAQERArqqQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAE----EQKRLMEmAEEERLEYQRQKQEA 486
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
42-105 |
4.91e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 38.00 E-value: 4.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958755446 42 AIVGLYRTGKSYLMNRLAGQN-------HgfnlGTTVRSETKgiwmwcvPHPCKPKFTLVLLDTEGLGDVE 105
Cdd:cd00880 1 AIFGRPNVGKSSLLNALLGQNvgivspiP----GTTRDPVRK-------EWELLPLGPVVLIDTPGLDEEG 60
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
492-586 |
5.79e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 37.16 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 492 RAQKEAAEKEQELLRQKQKELQQVMESQERSYKEN---IVQLHEKMETERKNILEKQEEMlaHKLKVQEEMLNegfkrky 568
Cdd:pfam13863 23 ERLEELLKQREEELEKKEQELKEDLIKFDKFLKENdakRRRALKKAEEETKLKKEKEKEI--KKLTAQIEELK------- 93
|
90
....*....|....*...
gi 1958755446 569 eamdSEISQLQKQIQQNK 586
Cdd:pfam13863 94 ----SEISKLEEKLEEYK 107
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
374-595 |
7.24e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 39.34 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 374 DENQEFQKNLvvTIVEKREdfsrqNEAASLSHCQAELDKLSESLRESISCGAFSvpgGHSLYLEARK---KVEQDYEQVP 450
Cdd:pfam05557 48 DRNQELQKRI--RLLEKRE-----AEAEEALREQAELNRLKKKYLEALNKKLNE---KESQLADAREvisCLKNELSELR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 451 RKGVKANHVLQS-FLQSQIVIENSILQSDKALTVNQKAMEVERAQKEAAEKEQ------------------------ELL 505
Cdd:pfam05557 118 RQIQRAELELQStNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQrikelefeiqsqeqdseivknsksELA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 506 R----QKQKELQQVMESQERSYKENIVQLHEKMETERKNiLEKQEEMLAHKLKVQ------EEMLNEGFK---------R 566
Cdd:pfam05557 198 RipelEKELERLREHNKHLNENIENKLLLKEEVEDLKRK-LEREEKYREEAATLElekeklEQELQSWVKlaqdtglnlR 276
|
250 260
....*....|....*....|....*....
gi 1958755446 567 KYEAMDSEISQLQKQIQQNKEQNSSLAAQ 595
Cdd:pfam05557 277 SPEDLSRRIEQLQQREIVLKEENSSLTSS 305
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
478-595 |
7.59e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 478 DKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMES---QERSYKENIVQLHEKM--ETERKNILEKQEEMLAHK 552
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEaqaEEYELLAELARLEQDIarLEERRRELEERLEELEEE 324
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1958755446 553 LKVQEEMLnEGFKRKYEAMDSEISQLQKQIQQNKEQNSSLAAQ 595
Cdd:COG1196 325 LAELEEEL-EELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
241-588 |
8.05e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 241 KEKELLVHVEEMPEDELDHNFREQSNVFCSYIFSNAKAKTLKEGIMVNGNRLATLVTTYVDAINsgAVPCLENAVTTLAQ 320
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV--AVENYKVAISTAVI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 321 RENSAAVQKAAEHYSEQMAQRLRLPTDTLQELLDVHSACEKEAIAVFMEHSFKDENQEFQKNLVVTIVEKREDFSRQNE- 399
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILk 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 400 -AASLSHCQAELDKLSESLRESISC--GAFSVPGGHSLYLEARKKVEQDYEQVPRKGVKANHVLQSFLQSQIVIENSILQ 476
Cdd:pfam02463 631 dTELTKLKESAKAKESGLRKGVSLEegLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 477 SDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQERSYK---------ENIVQLHEKMETERKNILEKQEE 547
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKkeekeeeksELSLKEKELAEEREKTEKLKVEE 790
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1958755446 548 MLAHKLKVQEEMLNEG-FKRKYEAMDSEISQLQKQIQQNKEQ 588
Cdd:pfam02463 791 EKEEKLKAQEEELRALeEELKEEAELLEEEQLLIEQEEKIKE 832
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
437-588 |
8.22e-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: 38.75 E-value: 8.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 437 EARKKVEQDYEQVPRKGVKANHVLQSFLQSQIViENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVM 516
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELEEQIE-EREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLR 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958755446 517 ESQERSYKENIV---QLHEKMETERKNILEKQEEMLAHKLKVQEEMlnegfKRKYEAMDSEISQLQKQIQQNKEQ 588
Cdd:pfam13868 130 EEIDEFNEEQAEwkeLEKEEEREEDERILEYLKEKAEREEEREAER-----EEIEEEKEREIARLRAQQEKAQDE 199
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
471-584 |
8.70e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958755446 471 ENSILQSDKALTVNQKAMEVERAQKEAAEKEQELLRQKQKELQQVMESQERSYKENIVQLHEKMETERKNILEKQEEMLA 550
Cdd:COG1196 667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746
|
90 100 110
....*....|....*....|....*....|....
gi 1958755446 551 HKLKVQEEMLNEGFKRkyEAMDSEISQLQKQIQQ 584
Cdd:COG1196 747 LLEEEALEELPEPPDL--EELERELERLEREIEA 778
|
|
| |
