|
Name |
Accession |
Description |
Interval |
E-value |
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
411-507 |
9.43e-23 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 92.74 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 411 EELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHE 490
Cdd:pfam16516 1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80
|
90
....*....|....*..
gi 1251770383 491 EKEQLALQLAILLKENN 507
Cdd:pfam16516 81 EKEQLAAQLEYLQRQNQ 97
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
426-510 |
3.84e-22 |
|
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.
Pssm-ID: 197361 [Multi-domain] Cd Length: 87 Bit Score: 90.87 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 426 LQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKE 505
Cdd:cd09803 3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
....*
gi 1251770383 506 NNDIE 510
Cdd:cd09803 83 NQELK 87
|
|
| NEMO |
pfam11577 |
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ... |
37-103 |
1.39e-16 |
|
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.
Pssm-ID: 431942 [Multi-domain] Cd Length: 67 Bit Score: 74.44 E-value: 1.39e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251770383 37 PEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHE 103
Cdd:pfam11577 1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
|
|
| zf_C2H2_10 |
pfam18414 |
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ... |
558-583 |
1.34e-13 |
|
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.
Pssm-ID: 436483 Cd Length: 26 Bit Score: 64.53 E-value: 1.34e-13
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
224-472 |
6.50e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 224 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVgsEVE 303
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--RLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 304 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTE 383
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 384 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 461
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250
....*....|.
gi 1251770383 462 ETMAVLRAQME 472
Cdd:COG1196 477 AALAELLEELA 487
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-525 |
4.18e-08 |
|
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: 56.60 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 244 LREGNQKVERLEVALREAKERISDFEKKanghsstekqtARRADREKEDKGQESvgsevetlSIQVTSLFKELQEAHTKL 323
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQ-----------AEKAERYKELKAELR--------ELELALLVLRLEELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 324 SEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEK----SRLATLQATHNKL 399
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 400 LQEHNKALKTIEELTKQQAEKVDKmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLET-----------MAVLR 468
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaqlelqIASLN 399
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1251770383 469 AQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQCRH 525
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-466 |
7.74e-08 |
|
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: 55.45 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 219 LSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSStEKQTARRADREKEDKgQESV 298
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELAEAEAE-IEEL 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 299 GSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELnekQELVYSNKKLELQVESMRSEIKME 378
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL---EDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 379 QAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM-----LLQELSEKLELAEQALASKQLQMDEMKQT 453
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRselrrELEELREKLAQLELRLEGLEVRIDNLQER 944
|
250
....*....|...
gi 1251770383 454 LAKQEEDLETMAV 466
Cdd:TIGR02168 945 LSEEYSLTLEEAE 957
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
244-461 |
1.29e-07 |
|
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: 54.68 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 244 LREGNQKVERLEVALREAKERISDFEKKANG----HSSTEKQTAR-RADREKEDKGQESVGSEVETLSIQVTSLFKELQE 318
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 319 AHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQElVYSNKKLELQveSMRSEIKMEQAKTEEEKSRLATLQATHNK 398
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-ELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQIEE 849
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251770383 399 LLQEHNKALKTIEELTKQQAEKVDKmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 461
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-511 |
1.63e-07 |
|
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: 54.68 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 230 AEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGhSSTEKQTARRADREKEDKGQEsvgsevetlsIQv 309
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEE----------LQ- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 310 tslfKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQelvysNKKLELQVESMRSEIKMEQAKteEEKSRL 389
Cdd:TIGR02168 288 ----KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE-----SKLDELAEELAELEEKLEELK--EELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 390 ATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKlelAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRA 469
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1251770383 470 QMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDIEE 511
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
135-472 |
2.42e-06 |
|
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: 50.83 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 135 LEEEVEKLKTQVEQEVEHLKIQVMRLRAEKADLLGIVSELQLKLNSGGSSEDSfVEIRMTEGETEGAMKEMKncptptrt 214
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKE-AEEELEELTAELQELEEK-------- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 215 dpislSNCTEDARSCAEFEELTVSQLLLCLregNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKg 294
Cdd:TIGR02168 269 -----LEELRLEVSELEEEIEELQKELYAL---ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 295 qESVGSEVETLSIQVTSLFKELQEAHTKLSEaelMKKRLQEKCQALERKNsatpSELNEKQELVYSNKKlelQVESMRSE 374
Cdd:TIGR02168 340 -AELEEKLEELKEELESLEAELEELEAELEE---LESRLEELEEQLETLR----SKVAQLELQIASLNN---EIERLEAR 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 375 IKMeqakTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTL 454
Cdd:TIGR02168 409 LER----LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330
....*....|....*...
gi 1251770383 455 AKQEEDLETMAVLRAQME 472
Cdd:TIGR02168 485 AQLQARLDSLERLQENLE 502
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
34-509 |
7.37e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.95 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 34 TFTPEELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERllfemqskevkERLKALTHENERLKEElgk 113
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVEL-----------EELKKILAEDEKLLDE--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 114 fKEKSEKPLEDLTGGyrypralEEEVEKLKTQVEQEVEHLKIQVMRLRAEKADLLGIVSELQLKLnsggsSEDSFVEIRM 193
Cdd:pfam05483 424 -KKQFEKIAEELKGK-------EQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL-----EKEKLKNIEL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 194 TeGETEGAMKEMKNCPTPTRTDPISLSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKAN 273
Cdd:pfam05483 491 T-AHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 274 ghSSTEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEahtklseaelmkkrLQEKCQALERKNSATPSELNE 353
Cdd:pfam05483 570 --KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE--------------LHQENKALKKKGSAENKQLNA 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 354 KQELVysnKKLELQVESMRSEIkmeQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEkVDKMLLQELSEKL 433
Cdd:pfam05483 634 YEIKV---NKLELELASAKQKF---EEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKE-IDKRCQHKIAEMV 706
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1251770383 434 ELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDI 509
Cdd:pfam05483 707 ALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAI 782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-415 |
8.50e-06 |
|
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: 48.90 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 38 EELLQQMKELLVENHQLKEAM---KLNNQAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHENERLKEELGKF 114
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 115 KEKSEKPLEDLTGGYRYPRALEEEVEKLKTQVEQevehLKIQVMRLRAEKADLLGIVSELQLKLNSGGSsedsfveirmt 194
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEEAANLRE----------- 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 195 egetegamkemkncptptrtdpiSLSNCTEDARSCAEFEELTVSQlllcLREGNQKVERLEVALREAKERISDFEKKANG 274
Cdd:TIGR02168 825 -----------------------RLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEA 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 275 H-----SSTEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPS 349
Cdd:TIGR02168 878 LlneraSLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAE 957
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251770383 350 ELNEKQELvySNKKLELQVESMRSEIK---------MEQAktEEEKSRLATLQATHNKLLQEHNKALKTIEELTK 415
Cdd:TIGR02168 958 ALENKIED--DEEEARRRLKRLENKIKelgpvnlaaIEEY--EELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
56-462 |
9.23e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 56 EAMKLNNQAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHENERLKEELGKFKEKSEKPLEDLTGGYRYPRAL 135
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 136 EEEVEKLKTQVE---QEVEHLKIQVMRLRAEKADLLGIVSELQLKLNSggssedsfVEIRMTEGEtegAMKEMKNCPT-- 210
Cdd:PRK02224 390 EEEIEELRERFGdapVDLGNAEDFLEELREERDELREREAELEATLRT--------ARERVEEAE---ALLEAGKCPEcg 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 211 -PTRTDPISLSncTEDARSCAEFEELTVSQLLLCLREGNQKVERLEvALREAKERISDFEKKAnghSSTEKQTARRADRE 289
Cdd:PRK02224 459 qPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERR---EDLEELIAERRETI 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 290 KEDKGQesvgseVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSE---LNEKQELVYSNKKLEL 366
Cdd:PRK02224 533 EEKRER------AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERiesLERIRTLLAAIADAED 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 367 QVESMRSEIKMEQAKTEEEKSRLATLQathnkllqehnkalktieELTKQQAEKVDKMLLQELSEKLELAEQALAskqlQ 446
Cdd:PRK02224 607 EIERLREKREALAELNDERRERLAEKR------------------ERKRELEAEFDEARIEEAREDKERAEEYLE----Q 664
|
410
....*....|....*.
gi 1251770383 447 MDEMKQTLAKQEEDLE 462
Cdd:PRK02224 665 VEEKLDELREERDDLQ 680
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
116-493 |
9.39e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 116 EKSEKPLEDLTGGYRYPRA-LEEEVEKLKTQVEQEVEHLkiqvmrlraEKADLlgIVSELQLKLNSGGSSEDSFVEIRMT 194
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAeLDEEIERYEEQREQARETR---------DEADE--VLEEHEERREELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 195 EGETEGAMKEMKNCPTPTRTDPISLSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANG 274
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAES 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 275 HSSTEKQTARRADREKE-----DKGQESVGSEVETLSIQVTSLFKELQE-------AHTKLSEAELMKKRLQEKCQALER 342
Cdd:PRK02224 347 LREDADDLEERAEELREeaaelESELEEAREAVEDRREEIEELEEEIEElrerfgdAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 343 KNSATPSELNEKQELVYSNKKL-----------ELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKAlktiE 411
Cdd:PRK02224 427 REAELEATLRTARERVEEAEALleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA----E 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 412 ELTKQQAEkvdkmlLQELSEKLELAEQALASKQlqmdemkqtlAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEE 491
Cdd:PRK02224 503 DLVEAEDR------IERLEERREDLEELIAERR----------ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE 566
|
..
gi 1251770383 492 KE 493
Cdd:PRK02224 567 AE 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
279-511 |
9.69e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 279 EKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSEL----NEK 354
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLeeleEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 355 QELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKML-LQELSEKL 433
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEEL 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1251770383 434 ELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQmevycsDFHAERAAREKIHEEKEQLALQLAILLKENNDIEE 511
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEE------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
38-518 |
1.64e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 38 EELLQQMKELLVENHQLK---EAMKLNNQAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHENERLK--EELG 112
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKkkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 113 KFKEKSEKPLEDLtggyRYPRALEEEVEKLKTQVEQEVEHLKIQVMRLRAEKADLLGIVSELQLKLNSGGSSEDSFVEIR 192
Cdd:PTZ00121 1398 KKAEEDKKKADEL----KKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 193 MTEGETEGAMK--EMKNCPTPTRTDPISLSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEK 270
Cdd:PTZ00121 1474 EAKKKAEEAKKadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 271 KANGHSSTEKQTARRADREKEDKGQESVGSEV-----ETLSIQVTSLF--------KELQEAHTKLSEAELMKKRLQEKC 337
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeEARIEEVMKLYeeekkmkaEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 338 QALERKNSAT----PSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQathnklLQEHNKALKTIEEL 413
Cdd:PTZ00121 1634 KVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA------LKKEAEEAKKAEEL 1707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 414 TKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMK-QTLAKQEEDLETMAVLRAQMEVYCSDFHAERAA--REKIHE 490
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAviEEELDE 1787
|
490 500 510
....*....|....*....|....*....|..
gi 1251770383 491 EKEQLALQLAILLKENND----IEEGGSRQSL 518
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDnfanIIEGGKEGNL 1819
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
244-465 |
2.42e-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: 46.68 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 244 LREGNQKVERLEVALREAKERISDFEKKANGHSST-EKQTARRADREKEDKGQESvgsEVETLSIQVTSLFKELQEAHTK 322
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlAALERRIAALARRIRALEQ---ELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 323 LSEaelMKKRLQEKCQALERKNSATPSEL----NEKQELVYSNKKLELQVESMRS---EIKMEQAKTEEEKSRLATLQAT 395
Cdd:COG4942 99 LEA---QKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREqaeELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 396 HNKLLQEHNKALKTIEELTKQQAEkvdkmLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMA 465
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
89-460 |
2.57e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 89 QSKEVKERLKALTHENERLKEELGKFKEKSE----KPLEDLTGGYRYPRALEEE--VEKLKTQVEQEVEHLKIQVMRLRA 162
Cdd:PTZ00121 1195 KAEDARKAEAARKAEEERKAEEARKAEDAKKaeavKKAEEAKKDAEEAKKAEEErnNEEIRKFEEARMAHFARRQAAIKA 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 163 E---KADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGETEGAMKEMKNCPTPTRTDPISLSNCTEDARSCAEFEELTVSQ 239
Cdd:PTZ00121 1275 EearKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEA 1354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 240 LLLCLREGNQKVERLEVALREAKERISDFEKKANghsstEKQTARRADREKEDKGQESvgsevetlsiqvtslfKELQEA 319
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-----EKKKADEAKKKAEEDKKKA----------------DELKKA 1413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 320 HTKLSEAELMKKRLQEKCQALERKNSAtpselNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKL 399
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKA-----EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251770383 400 LQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEED 460
Cdd:PTZ00121 1489 KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
234-522 |
6.31e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 6.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 234 ELTVSQLLLCLREGNQ----KVERLE-------VALREAKERISDFEKKA-NGHSSTEKQTARRADREKE---DKGQESV 298
Cdd:pfam15921 323 ESTVSQLRSELREAKRmyedKIEELEkqlvlanSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKElslEKEQNKR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 299 GSEVET-LSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSnkkLELQVESMRseiKM 377
Cdd:pfam15921 403 LWDRDTgNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS---LTAQLESTK---EM 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 378 EQAKTEEEKSRLATLQATHNKL------LQEHNKALK-TIEELTKQQAeKVDkMLLQELS------EKLELAEQALASKQ 444
Cdd:pfam15921 477 LRKVVEELTAKKMTLESSERTVsdltasLQEKERAIEaTNAEITKLRS-RVD-LKLQELQhlknegDHLRNVQTECEALK 554
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251770383 445 LQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREK-IHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQ 522
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKeINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-419 |
9.86e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.44 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 38 EELLQQMKELLVENHQLKEAMklnnQAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHENERLKEELGKFKEK 117
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQEL----SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 118 SEKPLEDLTggyryprALEEEVEKLKTQV-EQEVEHLKIQVMRLRAEKADLLGIVSELQLKLNSggssedsfveirmTEG 196
Cdd:TIGR02169 767 IEELEEDLH-------KLEEALNDLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-------------LTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 197 ETEGAMKEMKNcptptrtdpisLSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKkanghs 276
Cdd:TIGR02169 827 EKEYLEKEIQE-----------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK------ 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 277 stekqtarraDREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQE 356
Cdd:TIGR02169 890 ----------ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAE 959
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251770383 357 LvysnKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAE 419
Cdd:TIGR02169 960 L----QRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
248-472 |
1.09e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 248 NQKVERLEVALREAKERISDFekkanghsstekqtarradreKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAE 327
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF---------------------RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 328 LMKKRLQekcQALERKNSATPSELNEKQelvysnkklelqVESMRSEIkmeqaktEEEKSRLATLQAThnklLQEHNKAL 407
Cdd:COG3206 240 ARLAALR---AQLGSGPDALPELLQSPV------------IQQLRAQL-------AELEAELAELSAR----YTPNHPDV 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251770383 408 KTIeeltKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQME 472
Cdd:COG3206 294 IAL----RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
69-459 |
2.00e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 69 FEELSAWTEKQKEERLLFEmqskEVKERLKALTHENERLKEELGKFKEKSEKPLEDLTGGYRYPRALEEEVEKLKTQVEQ 148
Cdd:TIGR02169 176 LEELEEVEENIERLDLIID----EKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 149 EVEHLKIQVMRLRAEKADLLGIVSELQLKLNSGGSSEDSFVEIRMTEGETEgamkemkncptptrtdpislsnctedars 228
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE----------------------------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 229 caefeeltVSQLLLCLREGNQKVERLEVALREAKERISdfEKKANGHSSTEKQTARRADREKedkgqesVGSEVETLSIQ 308
Cdd:TIGR02169 303 --------IASLERSIAEKERELEDAEERLAKLEAEID--KLLAEIEELEREIEEERKRRDK-------LTEEYAELKEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 309 VTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTEEEKSR 388
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELADLNAAIAGIEAKINELEEE 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251770383 389 LATLQAthnKLLQEHNKALKTIEELTKQQAEKVDkmllqeLSEKLELAEQALASKQLQMDEMKQTLAKQEE 459
Cdd:TIGR02169 443 KEDKAL---EIKKQEWKLEQLAADLSKYEQELYD------LKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
326-458 |
2.04e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 326 AELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNK 405
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEI---RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1251770383 406 ALKTIEELTKQQAEKvdKMLLQELSEKLELAEQaLASKQLQMDEMKQTLAKQE 458
Cdd:COG2433 460 EIRKDREISRLDREI--ERLERELEEERERIEE-LKRKLERLKELWKLEHSGE 509
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
77-493 |
2.14e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 77 EKQKEerllfemQSKEVKERLKALTHENERLKEELGKFKEKSEKPLEDLTGGYRYPRALEEEVEKLKTQVEQ---EVEHL 153
Cdd:PRK02224 226 EEQRE-------QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeERDDL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 154 KIQVMRLRAEKADLLGIVSELQLKLNSGGSS-EDSFVEIRMTEGETEGAMKEMKNcptptrtdpisLSNCTEDARSCAEF 232
Cdd:PRK02224 299 LAEAGLDDADAEAVEARREELEDRDEELRDRlEECRVAAQAHNEEAESLREDADD-----------LEERAEELREEAAE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 233 EELTVSQLLLCLREGNQKVERLEVALREAKERISDFEkkanghsstekqtarrADREKEDKGQESVGSEVETLSIQVTSL 312
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAP----------------VDLGNAEDFLEELREERDELREREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 313 FKELQEAHTKLSEAElmkkRLQE--KCQALER--KNSATPSELNEKQElvysnKKLELQVEsmRSEIKMEQAKTEEEKSR 388
Cdd:PRK02224 432 EATLRTARERVEEAE----ALLEagKCPECGQpvEGSPHVETIEEDRE-----RVEELEAE--LEDLEEEVEEVEERLER 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 389 LATLQATHNKLLQEHNKAlKTIEELTKQQAEKVDKMLLQ---------ELSEKLELAEQALASKQLQMDEMKQTLAKQEE 459
Cdd:PRK02224 501 AEDLVEAEDRIERLEERR-EDLEELIAERRETIEEKRERaeelreraaELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
410 420 430
....*....|....*....|....*....|....
gi 1251770383 460 DLETMAVLRAQMEVYCSDFHAERAAREKIHEEKE 493
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIADAEDEIERLRE 613
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
244-463 |
3.70e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 244 LREGNQKVERLEVALREAKERISDFEKkanghsstEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKL 323
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNN--------QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 324 sEAELMKKRL--QEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQ 401
Cdd:TIGR04523 348 -KKELTNSESenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251770383 402 EH-------NKALKTIEELTKQQAEKvdKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLET 463
Cdd:TIGR04523 427 EIerlketiIKNNSEIKDLTNQDSVK--ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
272-487 |
3.77e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 272 ANGHSSTEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSEL 351
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 352 N------EKQELVYSNKKLELQVESMRSEIKM-----EQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEK 420
Cdd:COG4942 93 AelraelEAQKEELAELLRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251770383 421 VDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREK 487
Cdd:COG4942 173 RAELeaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
315-472 |
3.88e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 315 ELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTEEEKSRLAtlQA 394
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL---EDLEKEIKRLELEIEEVEARIKKYEEQLG--NV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251770383 395 THNKllqEHNKALKTIEELTKQQAEKVDKMLlqELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLET-MAVLRAQME 472
Cdd:COG1579 86 RNNK---EYEALQKEIESLKRRISDLEDEIL--ELMERIEELEEELAELEAELAELEAELEEKKAELDEeLAELEAELE 159
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
244-462 |
4.14e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 244 LREGNQKVERLEVALREAKERISDFEKkanghsstEKQTARRAD---REKEDKGQESVGSEVETLSIQVTSLFKELQEAH 320
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRR--------EREKAERYQallKEKREYEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 321 tklSEAELMKKRLQEKCQALERKNsATPSELNEKQELVYSNKKLELQ--VESMRSEIKMEQAKTEEEKSRLATLQATHNK 398
Cdd:TIGR02169 251 ---EELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLGEEEQLRVKekIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251770383 399 LLQEHNKALKTIEELTKQQAE-KVDKMLLQE----LSEKLELAEQALASKQLQMDEMKQTLAKQEEDLE 462
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEeRKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-511 |
4.76e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 38 EELLQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHENERLKEELGKFKEK 117
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 118 ---------------SEKPLEDLTGGYRYPRALEEEVEKLKTQVEQEVEHLKIQVMRLRAEKADLLGIVSELQ------- 175
Cdd:TIGR02168 430 leeaelkelqaeleeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvk 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 176 -LKLNS----------------------------GGSSEDSFVEIRMTEGETEGAMKEMK------------NCPTPTRT 214
Cdd:TIGR02168 510 aLLKNQsglsgilgvlselisvdegyeaaieaalGGRLQAVVVENLNAAKKAIAFLKQNElgrvtflpldsiKGTEIQGN 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 215 DPISLSNCTEDARSCAEFEELTVS-QLLLCLREGNQK-VERLEVALREAKERISDFE-----------------KKANGH 275
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLvVDDLDNALELAKKLRPGYRivtldgdlvrpggvitgGSAKTN 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 276 SSTEKQTARRADREKEDKGQES-----------VGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKN 344
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEkiaelekalaeLRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 345 SATPSELNEKQElvysnkklelQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQ-QAEKVDk 423
Cdd:TIGR02168 750 AQLSKELTELEA----------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAElTLLNEE- 818
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 424 mlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAA----REKIHEEKEQLALQL 499
Cdd:TIGR02168 819 --AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllneRASLEEALALLRSEL 896
|
570
....*....|..
gi 1251770383 500 AILLKENNDIEE 511
Cdd:TIGR02168 897 EELSEELRELES 908
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
41-492 |
5.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 41 LQQMKELLVENHQLKEAMKLNNQAMKGRFEELSAWTEKQKE-ERLLFEMQSKEvkERLKALTHENERLKEELGKFKEKSE 119
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGiEERIKELEEKE--ERLEELKKKLKELEKRLEELEERHE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 120 -----KPLEDLTGGYRYPRALE---------EEVEKLKTQVEQEVEHLKIQVMRLRAEKADLLGIVSELQlklnsGGSSE 185
Cdd:PRK03918 363 lyeeaKAKKEELERLKKRLTGLtpeklekelEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK-----KAKGK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 186 DSFVEIRMTEGETEGAMKEMKNCPTPTRTDPISLSNCTEDARscAEFEELtvsqlllclrEGNQKVERLEVALREAKERI 265
Cdd:PRK03918 438 CPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR--KELREL----------EKVLKKESELIKLKELAEQL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 266 SDFEKKANGHSSTEkqtarradREKEDKGQESVGSEVETLSIQVTSLFKELQeahtKLSEAELMKKRLQEKCQALERKNS 345
Cdd:PRK03918 506 KELEEKLKKYNLEE--------LEKKAEEYEKLKEKLIKLKGEIKSLKKELE----KLEELKKKLAELEKKLDELEEELA 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 346 ATPSELNEKQelVYSNKKLELQVESMRS------EIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAE 419
Cdd:PRK03918 574 ELLKELEELG--FESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 420 KVDKM----------LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIH 489
Cdd:PRK03918 652 LEKKYseeeyeelreEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVK 731
|
...
gi 1251770383 490 EEK 492
Cdd:PRK03918 732 KYK 734
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
286-472 |
1.02e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 286 ADREKEDKGQE--SVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysNKK 363
Cdd:COG3883 14 ADPQIQAKQKElsELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 364 LELQVESMRSEIKMEQ---AKTEEE----KSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLE 434
Cdd:COG3883 92 ARALYRSGGSVSYLDVllgSESFSDfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELeaLKAELEAAKA 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1251770383 435 LAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQME 472
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
302-483 |
1.52e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 302 VETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELN-------------EKQELVYSNKKLElQV 368
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiaeleaELERLDASSDDLA-AL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 369 ESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKL--ELAEQALASKQLQ 446
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFaaALGDAVERELREN 770
|
170 180 190
....*....|....*....|....*....|....*..
gi 1251770383 447 MDEMKQTLAKQEEDLETMavLRAQMEVYCSDFHAERA 483
Cdd:COG4913 771 LEERIDALRARLNRAEEE--LERAMRAFNREWPAETA 805
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
314-483 |
1.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 314 KELQEAHTKLSEAElmkKRLQEKCQALERKnsatpSELNEKQElvysnkklelqvesmrSEIKMEQAKTEEEKSRLATLQ 393
Cdd:PRK12704 75 KELRERRNELQKLE---KRLLQKEENLDRK-----LELLEKRE----------------EELEKKEKELEQKQQELEKKE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 394 ATHNKLLQEHNKALKTIEELTKQQAEkvdKMLLQELSEKLElAEQALASKQLQMDemkqtlAKQEEDLETMAVLRAQMEV 473
Cdd:PRK12704 131 EELEELIEEQLQELERISGLTAEEAK---EILLEKVEEEAR-HEAAVLIKEIEEE------AKEEADKKAKEILAQAIQR 200
|
170
....*....|
gi 1251770383 474 YCSDFHAERA 483
Cdd:PRK12704 201 CAADHVAETT 210
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
55-505 |
1.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 55 KEAMKLNNQAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHENERLKEELGKFKEKSEKPLEDLTGGYRYPRA 134
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 135 LEEEVEKLKTQVEQEVEHLKIQVMRLRaEKADLLGIVSELQLKLNSGGSSEDsfvEIRMTEGETEGAMKEMKNCPTPTRT 214
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAK-KKAEEKKKADEAKKKAEEDKKKAD---ELKKAAAAKKKADEAKKKAEEKKKA 1433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 215 DPI-----------SLSNCTEDARSCAEF----EELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANG----- 274
Cdd:PTZ00121 1434 DEAkkkaeeakkadEAKKKAEEAKKAEEAkkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAkkkad 1513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 275 --HSSTEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKlSEAELMKKRLQEKCQALERKNSATPSELN 352
Cdd:PTZ00121 1514 eaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK-KKAEEAKKAEEDKNMALRKAEEAKKAEEA 1592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 353 EKQELV-YSNKKLELQVESMRSE----IKMEQAKTEEEKSR----LATLQATHNKLLQEHNKA-----LKTIEELTKQQA 418
Cdd:PTZ00121 1593 RIEEVMkLYEEEKKMKAEEAKKAeeakIKAEELKKAEEEKKkveqLKKKEAEEKKKAEELKKAeeenkIKAAEEAKKAEE 1672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 419 EKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVycSDFHAERAAREKIHEEKEQLALQ 498
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE--NKIKAEEAKKEAEEDKKKAEEAK 1750
|
....*..
gi 1251770383 499 LAILLKE 505
Cdd:PTZ00121 1751 KDEEEKK 1757
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
362-472 |
2.12e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 362 KKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKAL--KTIEELTKQQAEKVDkmllqelseklELAEQA 439
Cdd:cd22656 131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIarKEIKDLQKELEKLNE-----------EYAAKL 199
|
90 100 110
....*....|....*....|....*....|...
gi 1251770383 440 LAskqlQMDEMKQTLAKQEEDLETMAVLRAQME 472
Cdd:cd22656 200 KA----KIDELKALIADDEAKLAAALRLIADLT 228
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
279-457 |
2.42e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.11 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 279 EKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATP--------SE 350
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaahikavTQ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 351 LNEKQELVY----SNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLL 426
Cdd:TIGR00618 305 IEQQAQRIHtelqSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
|
170 180 190
....*....|....*....|....*....|.
gi 1251770383 427 QELSEKLELAEQALASKQLQMDEMKQTLAKQ 457
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILQREQATIDTR 415
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
63-460 |
5.01e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 63 QAMKGRFEELSAWTEKQKEERLLFEMQSKEVKERLKALTHENERLKEELGKFKEK----------SEKPLEDLTGGY--- 129
Cdd:pfam15921 429 QRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEltakkmtlesSERTVSDLTASLqek 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 130 -RYPRALEEEVEKLKTQVE---QEVEHLKIQVMRLRAEKADllgiVSELQLKLnsggSSEDSFVEI------RMTE---- 195
Cdd:pfam15921 509 eRAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTE----CEALKLQM----AEKDKVIEIlrqqieNMTQlvgq 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 196 -GETEGAMKEMKncptptrtdpISLSNCTEDARscAEFEELTVSQlllclregnqkvERLEVALREAKERISDFE--KKA 272
Cdd:pfam15921 581 hGRTAGAMQVEK----------AQLEKEINDRR--LELQEFKILK------------DKKDAKIRELEARVSDLEleKVK 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 273 NGHSSTEKQTARRADREKEDKgqesVGSEVETLSIQVTSLFKELQ----EAHTKLSEAEL----MKKRLQEKCQALERKN 344
Cdd:pfam15921 637 LVNAGSERLRAVKDIKQERDQ----LLNEVKTSRNELNSLSEDYEvlkrNFRNKSEEMETttnkLKMQLKSAQSELEQTR 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 345 SATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNK---ALKTIEELTKQQAEKV 421
Cdd:pfam15921 713 NTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKlsqELSTVATEKNKMAGEL 792
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1251770383 422 DKMLLQE--LSEKLELAEQALASKQLQMDEMKQTLAKQEED 460
Cdd:pfam15921 793 EVLRSQErrLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
255-464 |
7.39e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 255 EVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQ-------------ESVGSEVETLSIQVT----------- 310
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSAlnrllprlnlladETLADRVEEIREQLDeaeeakrfvqq 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 311 ------------SLFKELQEAHTKLS----EAELMKKRLQEKCQAL----ERKN----SATPSELNEKQELVYSNKKLEL 366
Cdd:PRK04863 916 hgnalaqlepivSVLQSDPEQFEQLKqdyqQAQQTQRDAKQQAFALtevvQRRAhfsyEDAAEMLAKNSDLNEKLRQRLE 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 367 QVESMRSEIKME----QAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQ---QAEKVDKMLLQELSEKL------ 433
Cdd:PRK04863 996 QAEQERTRAREQlrqaQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPadsGAEERARARRDELHARLsanrsr 1075
|
250 260 270
....*....|....*....|....*....|..
gi 1251770383 434 -ELAEQALASKQLQMDEMKQTLAKQEEDLETM 464
Cdd:PRK04863 1076 rNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
69-447 |
8.47e-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: 39.18 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 69 FEELSAWTE--KQKEERLLFEMQSKEVKERLKALTHENERLKEELGKFKEKSEKpledltggyRYPRALEEEVEKLKTQV 146
Cdd:pfam02463 158 IEEEAAGSRlkRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALE---------YYQLKEKLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 147 EQEVEHLKIQVMRLRAEKADllgivsELQLKLNSGGSSEDSFVEIRMTEGETEGAMKEMKNcptptrtdpislsncteda 226
Cdd:pfam02463 229 LDYLKLNEERIDLLQELLRD------EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKL------------------- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 227 rscAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESvgsevETLS 306
Cdd:pfam02463 284 ---QEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKR-----EAEE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 307 IQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEK 386
Cdd:pfam02463 356 EEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251770383 387 SRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQM 447
Cdd:pfam02463 436 EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLE 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
96-385 |
9.24e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.15 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 96 RLKALTHENERLKEELGKFKEKSEKPLEDLtggyrypRALEEEVEKLKTQVEQEVEHLKIQVMRLRAEKADLLGIVSELQ 175
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAEL-------AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 176 LKLNSGGSSEDSFVEIRMTEGETEGAMKEMKncptptrtdpislsncTEDARSCAEFEELT--VSQLLLCLREGNQKVER 253
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELE----------------EELEELEEELEEAEeeLEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 254 LEVALREAKERISDF-------EKKANGHSSTEKQTARRADREKEDkgQESVGSEVETLSIQVTSLFKELQEAHTKLSEA 326
Cdd:COG1196 370 AEAELAEAEEELEELaeelleaLRAAAELAAQLEELEEAEEALLER--LERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1251770383 327 ELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEE 385
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
249-440 |
9.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 249 QKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKgQESVGSEVETLSiqvtslfKELQEAHTKLSEAEL 328
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI-RGNGGDRLEQLE-------REIERLERELEERER 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251770383 329 MKKRLQEKCQALERKNSATPSELNEKQElvysnkklelQVESMRSEIKMEQAKTEEEksrLATLQATHNKLLQEHNKALK 408
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEFAALRA----------EAAALLEALEEELEALEEA---LAEAEAALRDLRRELRELEA 426
|
170 180 190
....*....|....*....|....*....|....*
gi 1251770383 409 TIEELTKQQ---AEKVDKMlLQELSEKLELAEQAL 440
Cdd:COG4913 427 EIASLERRKsniPARLLAL-RDALAEALGLDEAEL 460
|
|
| |
