|
Name |
Accession |
Description |
Interval |
E-value |
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
78-365 |
5.16e-141 |
|
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: 403.21 E-value: 5.16e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 78 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 157
Cdd:pfam02841 8 PRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKEAIAVFMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 158 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 235
Cdd:pfam02841 88 RSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKLEAKYNQV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 236 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 315
Cdd:pfam02841 168 PRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1039772807 316 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 365
Cdd:pfam02841 248 LIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
78-365 |
2.13e-133 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 383.85 E-value: 2.13e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 78 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 157
Cdd:cd16269 2 RRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFMK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 158 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 235
Cdd:cd16269 82 RSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 236 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 315
Cdd:cd16269 162 PRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQ 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1039772807 316 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 365
Cdd:cd16269 242 LKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
1-79 |
1.01e-26 |
|
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: 107.46 E-value: 1.01e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039772807 1 MNTISHDSLEKLHYVTELTELirakSSPNPDGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPG 79
Cdd:pfam02263 114 SQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQG 188
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
275-375 |
4.63e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 275 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENiEQLRRKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKA 354
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149
|
90 100
....*....|....*....|.
gi 1039772807 355 EEMDGEIQQLKHNIEDMKKKQ 375
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKK 170
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
3-89 |
3.46e-05 |
|
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: 44.62 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 3 TISHDSLEKLHYVTELTElirakSSPNPDGIKNsteFVSFFPDFVWTVRDFMLELKLNGEDITS-----DEYLENALKLI 77
Cdd:cd01851 104 TILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPLEGLDVTEksetlIEELNKIWSSI 175
|
90
....*....|..
gi 1039772807 78 PGLGILVTTYVD 89
Cdd:cd01851 176 RKPFTPITCFVL 187
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
265-360 |
1.51e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 265 TALTAGQKAIAEERTKKEAAEKEQDL--------LRQKQ---KEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNM 333
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELaelEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|....*..
gi 1039772807 334 mvEKKLKEQKALLEEGFKKKAEEMDGE 360
Cdd:COG0542 491 --EKELAELEEELAELAPLLREEVTEE 515
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-374 |
3.55e-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: 39.65 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 257 ESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQK---QKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNM 333
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1039772807 334 MVEKK-----LKEQKALLE---EGFKKKAEEMDGEIQQLKHNIEDMKKK 374
Cdd:TIGR02168 332 LDELAeelaeLEEKLEELKeelESLEAELEELEAELEELESRLEELEEQ 380
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
78-365 |
5.16e-141 |
|
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: 403.21 E-value: 5.16e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 78 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 157
Cdd:pfam02841 8 PRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKEAIAVFMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 158 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 235
Cdd:pfam02841 88 RSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKLEAKYNQV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 236 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 315
Cdd:pfam02841 168 PRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQ 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1039772807 316 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 365
Cdd:pfam02841 248 LIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
78-365 |
2.13e-133 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 383.85 E-value: 2.13e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 78 PGLGILVTTYVDAINSGAVPCVDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFME 157
Cdd:cd16269 2 RRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFMK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 158 HSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQV 235
Cdd:cd16269 82 RSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 236 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQ 315
Cdd:cd16269 162 PRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQ 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1039772807 316 LRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLK 365
Cdd:cd16269 242 LKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP |
pfam02263 |
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ... |
1-79 |
1.01e-26 |
|
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: 107.46 E-value: 1.01e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039772807 1 MNTISHDSLEKLHYVTELTELirakSSPNPDGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPG 79
Cdd:pfam02263 114 SQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQG 188
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
277-373 |
2.26e-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: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 277 ERTKKEAAEKEQDL--LRQKQKEQ--QEYMEAQEKRNKENIEQLRRK-----LEQEREQLIKDHN--MMVEKKLKE-QKA 344
Cdd:pfam17380 449 ERVRLEEQERQQQVerLRQQEEERkrKKLELEKEKRDRKRAEEQRRKilekeLEERKQAMIEEERkrKLLEKEMEErQKA 528
|
90 100 110
....*....|....*....|....*....|..
gi 1039772807 345 LLEEGFKKKAEE---MDGEIQQLKHNIEDMKK 373
Cdd:pfam17380 529 IYEEERRREAEEerrKQQEMEERRRIQEQMRK 560
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
275-375 |
4.63e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 275 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENiEQLRRKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKA 354
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149
|
90 100
....*....|....*....|.
gi 1039772807 355 EEMDGEIQQLKHNIEDMKKKQ 375
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKK 170
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
99-369 |
2.52e-05 |
|
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: 46.37 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 99 VDDAVTTLAQRENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVE-LIGE 177
Cdd:pfam12128 453 LNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqLFPQ 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 178 AKVLFLLKNEEASD------KYCQEELdRLSKDLMDNISTFSVPGGHRLY---MDMrEKIEHDYW-----QVPRKGVKAR 243
Cdd:pfam12128 533 AGTLLHFLRKEAPDweqsigKVISPEL-LHRTDLDPEVWDGSVGGELNLYgvkLDL-KRIDVPEWaaseeELRERLDKAE 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 244 EVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQE 323
Cdd:pfam12128 611 EALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQ 690
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1039772807 324 REQLIKDHNMMVE---KKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIE 369
Cdd:pfam12128 691 LKQLDKKHQAWLEeqkEQKREARTEKQAYWQVVEGALDAQLALLKAAIA 739
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
281-375 |
3.35e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 281 KEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMvEKKLKEQKALLE---EGFKKKAEEM 357
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKL-EKRLLQKEENLDrklELLEKREEEL 112
|
90
....*....|....*...
gi 1039772807 358 DGEIQQLKHNIEDMKKKQ 375
Cdd:PRK12704 113 EKKEKELEQKQQELEKKE 130
|
|
| GBP |
cd01851 |
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ... |
3-89 |
3.46e-05 |
|
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: 44.62 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 3 TISHDSLEKLHYVTELTElirakSSPNPDGIKNsteFVSFFPDFVWTVRDFMLELKLNGEDITS-----DEYLENALKLI 77
Cdd:cd01851 104 TILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPLEGLDVTEksetlIEELNKIWSSI 175
|
90
....*....|..
gi 1039772807 78 PGLGILVTTYVD 89
Cdd:cd01851 176 RKPFTPITCFVL 187
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
240-375 |
9.40e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 240 VKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEniEQLRRK 319
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA--EALKKE 1697
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039772807 320 LEQER--EQLIKDHNMmvEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 375
Cdd:PTZ00121 1698 AEEAKkaEELKKKEAE--EKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-374 |
9.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 262 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRnkeNIEQLRRKLEQER---EQLIKDHNmmvEKK 338
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK---KAEELKKKEAEEKkkaEELKKAEE---ENK 1729
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039772807 339 LK-EQKALLEEGFKKKAEEM---DGEIQQLKHNIEDMKKK 374
Cdd:PTZ00121 1730 IKaEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKK 1769
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
265-360 |
1.51e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 265 TALTAGQKAIAEERTKKEAAEKEQDL--------LRQKQ---KEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNM 333
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELaelEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPEL 490
|
90 100
....*....|....*....|....*..
gi 1039772807 334 mvEKKLKEQKALLEEGFKKKAEEMDGE 360
Cdd:COG0542 491 --EKELAELEEELAELAPLLREEVTEE 515
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
280-356 |
1.99e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 1.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039772807 280 KKEAAEKEQdlLRQKQKEQQeymeAQEKRNKENIEQLR-RKLEQEREQLIKdhnmmvEKKLKEQKALLEEGFKKKAEE 356
Cdd:PRK09510 71 QKSAKRAEE--QRKKKEQQQ----AEELQQKQAAEQERlKQLEKERLAAQE------QKKQAEEAAKQAALKQKQAEE 136
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
225-375 |
2.04e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 225 REKIEHDYWQVPRKGVKAREVFQSFLQSQAII--ESSILQADTALTAGQKAIAEERTKKEAAEKEQdLLRQKQKEQQEYM 302
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK-VEQLKKKEAEEKK 1647
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039772807 303 EAQEKRNKENIEQLRRKLEQEREQlikdhnmmvEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 375
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAE---------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-375 |
2.14e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 253 QAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRKLEQEREQLIKDHN 332
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ--LEELEEAEEALLERLERLEEELEELEEALA 431
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1039772807 333 MMVEKKLKEQKALLEEgfKKKAEEMDGEIQQLKHNIEDMKKKQ 375
Cdd:COG1196 432 ELEEEEEEEEEALEEA--AEEEAELEEEEEALLELLAELLEEA 472
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
272-374 |
2.15e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 272 KAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEK-RNKENIEQLRRKLEQEReqliKDHNMmveKKLKEQKALLEEgF 350
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAK----KAEEA---KKKAEEAKKADE-A 1475
|
90 100
....*....|....*....|....
gi 1039772807 351 KKKAEEMDgEIQQLKHNIEDMKKK 374
Cdd:PTZ00121 1476 KKKAEEAK-KADEAKKKAEEAKKK 1498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
271-370 |
2.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 271 QKAIAEERTKKEAAEKEQ-DLLRQKQKEQQ---EYMEAQEKRNKENIEQLRRKLEQER----------------EQLIKD 330
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKaEELKKKEAEEKkkaEELKKAEEENKIKAEEAKKEAEEDKkkaeeakkdeeekkkiAHLKKE 1765
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039772807 331 HNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIED 370
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
271-377 |
4.87e-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: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 271 QKAIAEERTK---KEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREqliKDHNMMVEKKLKEQKALLE 347
Cdd:pfam17380 486 RKRAEEQRRKileKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERR---KQQEMEERRRIQEQMRKAT 562
|
90 100 110
....*....|....*....|....*....|
gi 1039772807 348 EGfKKKAEEMDGEIQQLKHNIEDMKKKQWF 377
Cdd:pfam17380 563 EE-RSRLEAMEREREMMRQIVESEKARAEY 591
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
276-363 |
5.03e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 276 EERTKKEAAEKEQDLLRQKQKEQQEYMEaQEKRNKENIEQLRRKLEQEREQLikdhnMMVEKKLKEQKALLEEGFKKKAE 355
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLE-KEEEERLRKEELRRRAEEERARR-----EEEARRLEEERRREEEERQRKAE 82
|
....*...
gi 1039772807 356 EMDGEIQQ 363
Cdd:pfam05672 83 EEAEEREQ 90
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-374 |
5.33e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 262 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMM-VEKKLK 340
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEEAKK 1614
|
90 100 110
....*....|....*....|....*....|....
gi 1039772807 341 EQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKK 374
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
251-357 |
6.33e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 251 QSQAIIESSILQADT----ALTAGQKAIAEERTK--KEAAEKEQDLLRQKQKEQQEymEAQEKRNKENIEQLRRKLEQER 324
Cdd:PRK12704 39 EAKRILEEAKKEAEAikkeALLEAKEEIHKLRNEfeKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKKE 116
|
90 100 110
....*....|....*....|....*....|...
gi 1039772807 325 EQLIKDhnmmvEKKLKEQKALLEEGFKKKAEEM 357
Cdd:PRK12704 117 KELEQK-----QQELEKKEEELEELIEEQLQEL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
237-371 |
6.96e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 237 RKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQL 316
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1039772807 317 RRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDM 371
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
256-375 |
7.97e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 256 IESSILQADTALTAGQKAIAEERTKKEAAEKEqdllRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLikdhnMMV 335
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEAR----LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL-----GNV 85
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039772807 336 eKKLKEQKALLEE--GFKKKAEEMDGEIQQLKHNIEDMKKKQ 375
Cdd:COG1579 86 -RNNKEYEALQKEieSLKRRISDLEDEILELMERIEELEEEL 126
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-374 |
8.12e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 262 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYME-----AQEKRNKENIEQLRRKLEQEREQLIKDHNMMVE 336
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADaakkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110
....*....|....*....|....*....|....*...
gi 1039772807 337 KKLKEQKALLEEgFKKKAEEMDgEIQQLKHNIEDMKKK 374
Cdd:PTZ00121 1371 KKKEEAKKKADA-AKKKAEEKK-KADEAKKKAEEDKKK 1406
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
242-375 |
1.05e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 242 AREVFQsfLQSQAII---ESSILQADTAltagqkaiaeertkKEAAEKEQDLLR-QKQKEQQEYMEAQEKRNK--ENIEQ 315
Cdd:pfam10168 530 PQECLQ--LLSRATQvfrEEYLKKHDLA--------------REEIQKRVKLLKlQKEQQLQELQSLEEERKSlsERAEK 593
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039772807 316 LRRKLE--QEREQLI--KDHNMMveKKLKEQKALL---EEGFKKKAEEMDGEIQQLKHNIEDMKKKQ 375
Cdd:pfam10168 594 LAEKYEeiKDKQEKLmrRCKKVL--QRLNSQLPVLsdaEREMKKELETINEQLKHLANAIKQAKKKM 658
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
262-364 |
2.23e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 40.36 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 262 QADTALTAGQKAIAE--ERTkkeAAEKE-QDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKD--HNMMve 336
Cdd:pfam13779 486 DAERRLRAAQERLSEalERG---ASDEEiAKLMQELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQQdlQRML-- 560
|
90 100
....*....|....*....|....*...
gi 1039772807 337 KKLKEqkaLLEEGFKKKAEEMDGEIQQL 364
Cdd:pfam13779 561 DRIEE---LARSGRRAEAQQMLSQLQQM 585
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
254-329 |
2.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 254 AIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQK----------QKEQQEYMEAQEKRNKENIEQLRRKLEQE 323
Cdd:COG3883 5 ALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAEleelneeyneLQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
....*.
gi 1039772807 324 REQLIK 329
Cdd:COG3883 85 REELGE 90
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
255-375 |
3.36e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 255 IIESSILQAdtaLTAGQKAIAEERTKKEAAEKEQDLLRQKQkEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMM 334
Cdd:PRK00409 521 LIASLEELE---RELEQKAEEAEALLKEAEKLKEELEEKKE-KLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1039772807 335 VEKKLKEQKAlleegfkKKAEEMdgeIQQLKHNIEDMKKKQ 375
Cdd:PRK00409 597 QKGGYASVKA-------HELIEA---RKRLNKANEKKEKKK 627
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
257-374 |
3.55e-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: 39.65 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 257 ESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQK---QKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNM 333
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1039772807 334 MVEKK-----LKEQKALLE---EGFKKKAEEMDGEIQQLKHNIEDMKKK 374
Cdd:TIGR02168 332 LDELAeelaeLEEKLEELKeelESLEAELEELEAELEELESRLEELEEQ 380
|
|
| G_path_suppress |
pfam15991 |
G-protein pathway suppressor; This family of proteins inhibits G-protein- and ... |
277-369 |
4.03e-03 |
|
G-protein pathway suppressor; This family of proteins inhibits G-protein- and mitogen-activated protein kinase-mediated signal transduction.
Pssm-ID: 464961 [Multi-domain] Cd Length: 272 Bit Score: 38.75 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 277 ERTKKEAAEKEQDLLRQKQKEQQEYME--AQEKRNKEniEQLRRK-----LEQEREQLikdhnMMVEKK---LKEQKALL 346
Cdd:pfam15991 5 KMSEQMWRALKRHIMRERERKKQEQEAkmEEERLRRE--REEREKedrmtLEETKEQI-----LKLEKKladLKEEKHQL 77
|
90 100
....*....|....*....|...
gi 1039772807 347 EEGFKKKAEEMDGEIQQLKHNIE 369
Cdd:pfam15991 78 FLQLKKVLHEDETRKRQLKEQSE 100
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
276-358 |
4.04e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 38.00 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 276 EERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKK-LKEQKALLEEGFKKKA 354
Cdd:COG1390 12 LEEAEAEAEEILEEAEEEAEKILEEAEEEAEEIKEEILEKAEREAEREKRRIISSAELEARKElLEAKEELIEEVFEEAL 91
|
....
gi 1039772807 355 EEMD 358
Cdd:COG1390 92 EKLK 95
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
283-375 |
4.45e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 39.02 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 283 AAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLikdhnmmvekKLKEQKALLEEGFKKKAEEMDGEIQ 362
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERL----------KQLEKERLAAQEQKKQAEEAAKQAA 128
|
90
....*....|...
gi 1039772807 363 QLKHNIEDMKKKQ 375
Cdd:PRK09510 129 LKQKQAEEAAAKA 141
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
262-374 |
4.55e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 262 QADTALTAGQKAIAEERtKKEAAEKEQDLLRQKQKEQQEYMEAQEK--RNKENIEQLRRKLEQEREQLIKDHNMMVEKKL 339
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAKKKaeEDKKKADELKKAAAAKKKADEAKKKAEEKKKA 1433
|
90 100 110
....*....|....*....|....*....|....*
gi 1039772807 340 KEQKALLEEgfKKKAEEMDGEIQQlKHNIEDMKKK 374
Cdd:PTZ00121 1434 DEAKKKAEE--AKKADEAKKKAEE-AKKAEEAKKK 1465
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
262-363 |
5.45e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 38.83 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 262 QADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQ---EYMEAQEKRNKENIeQLRRKLEQEREQLIKDHNMMVEKK 338
Cdd:pfam05262 221 ELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKnlpKPADTSSPKEDKQV-AENQKREIEKAQIEIKKNDEEALK 299
|
90 100
....*....|....*....|....*
gi 1039772807 339 LKEQKAlleEGFKKKAEEMDGEIQQ 363
Cdd:pfam05262 300 AKDHKA---FDLKQESKASEKEAED 321
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
275-374 |
5.50e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 275 AEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKA 354
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA 1324
|
90 100
....*....|....*....|
gi 1039772807 355 EEMDGEIQQLKHNIEDMKKK 374
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKA 1344
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
257-373 |
5.61e-03 |
|
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: 38.97 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 257 ESSILQADTALTAGQKAIAEERTKKEA--------AEKEQDLLRQKQKEQQEY-MEAQEKRNKENIE--------QLRRK 319
Cdd:pfam09731 286 NSLIAHAHREIDQLSKKLAELKKREEKhieralekQKEELDKLAEELSARLEEvRAADEAQLRLEFErereeireSYEEK 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039772807 320 LEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKK-----AEEMDGEIQQL---KHNIEDMKK 373
Cdd:pfam09731 366 LRTELERQAEAHEEHLKDVLVEQEIELQREFLQDikekvEEERAGRLLKLnelLANLKGLEK 427
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
266-341 |
5.73e-03 |
|
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130214 [Multi-domain] Cd Length: 147 Bit Score: 37.00 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 266 ALTAGQKAIAE-----ERTKKEAA---EKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEK 337
Cdd:TIGR01144 23 AIETRQKKIADglasaERAKKEAAlaqKKAQVILKEAKDEAQEIIENANKRGSEILEEAKAEAREEREKIKAQARAEIEA 102
|
....
gi 1039772807 338 KLKE 341
Cdd:TIGR01144 103 EKEQ 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
272-374 |
6.09e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 272 KAIAEERTKK-EAAEKEQDLLRQKQKEQQEYMEAQEKRN---KENIEQLRRKLEQERE-QLIKDHNMMVEKKLKEQKALL 346
Cdd:PTZ00121 1335 KKKAEEAKKAaEAAKAEAEAAADEAEAAEEKAEAAEKKKeeaKKKADAAKKKAEEKKKaDEAKKKAEEDKKKADELKKAA 1414
|
90 100
....*....|....*....|....*...
gi 1039772807 347 EEgfKKKAEEMDGEIQQLKhNIEDMKKK 374
Cdd:PTZ00121 1415 AA--KKKADEAKKKAEEKK-KADEAKKK 1439
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
246-363 |
6.75e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.27 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 246 FQSFLQSQAIIeSSILQADTALTAGQKA-IAEERTKKEAAEKEQDLLRQKQKE---QQEYMEAQEKRNKENIEQLRRKLE 321
Cdd:COG3883 114 FSDFLDRLSAL-SKIADADADLLEELKAdKAELEAKKAELEAKLAELEALKAEleaAKAELEAQQAEQEALLAQLSAEEA 192
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1039772807 322 QEREQLikdHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQ 363
Cdd:COG3883 193 AAEAQL---AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
245-348 |
7.20e-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: 38.21 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 245 VFQSFLQSQAiieSSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKEnIEQLRRKLEQER 324
Cdd:COG4942 10 LLALAAAAQA---DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA-LEQELAALEAEL 85
|
90 100
....*....|....*....|....
gi 1039772807 325 EQLIKDHNMMvEKKLKEQKALLEE 348
Cdd:COG4942 86 AELEKEIAEL-RAELEAQKEELAE 108
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
236-352 |
8.21e-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: 38.21 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 236 PRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLR---QKQKEQQEYMEAQEKRNKEN 312
Cdd:COG4942 131 FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERaalEALKAERQKLLARLEKELAE 210
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1039772807 313 IEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKK 352
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
231-356 |
8.29e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 37.90 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 231 DYWQVPRKGVKAREVFQSFLQSQAIIESSI----LQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQE 306
Cdd:TIGR02794 23 LYHSVKPEPGGGAEIIQAVLVDPGAVAQQAnriqQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1039772807 307 KrnKENIEQLRRKLEQEREQLIKdhnmMVEKKLKEQKALLEEGFKKKAEE 356
Cdd:TIGR02794 103 A--AKQAEQAAKQAEEKQKQAEE----AKAKQAAEAKAKAEAEAERKAKE 146
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
272-387 |
9.11e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 38.39 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039772807 272 KAIAEERTKKEaaEKEQDL---------LRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQ 342
Cdd:pfam15818 239 KKINEEITHIQ--EEKQDIiisfqhmqqLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHE 316
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1039772807 343 KALleEGFKKKAEEMDGEIQQLKHNIEDMKKKQwFHFRYYYKRSC 387
Cdd:pfam15818 317 KAL--GTWKKHVEELNGEINEIKNELSSLKETH-IKLQEHYNKLC 358
|
|
| |
