|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
245-485 |
7.52e-12 |
|
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: 68.54 E-value: 7.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 245 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 321
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 322 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 401
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 402 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE-----------EKAREALRQ 470
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEleelseelrelESKRSELRR 915
|
250
....*....|....*
gi 356874788 471 QKRKAKASGERYHVE 485
Cdd:TIGR02168 916 ELEELREKLAQLELR 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
246-477 |
5.20e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 246 AEKKVKMLE-QQRSELLEVNKQW--DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR---------- 312
Cdd:COG1196 209 AEKAERYRElKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 313 KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspeg 392
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-------------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 393 AGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQK 472
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
....*
gi 356874788 473 RKAKA 477
Cdd:COG1196 435 EEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
140-476 |
7.60e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 140 RLASKVHKNEQRTSILQTLcEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEgasgrpgspkmegt 219
Cdd:COG1196 226 EAELLLLKLRELEAELEEL-EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE-------------- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 220 gkkAVAGQQQASVTAGKVPEvvalgaaEKKVKMLEQQRSELLEVNKQWDQHfrsmKQQYEQKITELRQKLADLQKQVTDL 299
Cdd:COG1196 291 ---YELLAELARLEQDIARL-------EERRRELEERLEELEEELAELEEE----LEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 300 EAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtp 379
Cdd:COG1196 357 EAELAEAEE---ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA-- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 380 psspptafgspegAGALLRKQELVTQNELLKQQVKIfEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 459
Cdd:COG1196 432 -------------ELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330
....*....|....*..
gi 356874788 460 DEEKAREALRQQKRKAK 476
Cdd:COG1196 498 EAEADYEGFLEGVKAAL 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
282-477 |
2.88e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 282 ITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEK 361
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 362 EIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 441
Cdd:COG1196 275 ELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190
....*....|....*....|....*....|....*.
gi 356874788 442 EKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKA 477
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
280-478 |
3.94e-10 |
|
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: 61.70 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 280 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 359
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 360 EKEIQRLNKALEEAL--SIQTPPSSPPTAFGSPEGAGALLRKQELVTQ-NELLKQQVKIFEEDFQRERSDRERMNEEKEE 436
Cdd:COG4942 96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 356874788 437 LKKQVEKLQAQvtlsNAQLKAFKDEEKAREALRQQKRKAKAS 478
Cdd:COG4942 176 LEALLAELEEE----RAALEALKAERQKLLARLEKELAELAA 213
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
276-447 |
5.97e-10 |
|
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: 59.94 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 276 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 355
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 356 REYQ--EKEI---QRLNKALEEALsiqtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRErm 430
Cdd:COG1579 89 KEYEalQKEIeslKRRISDLEDEI------------------LELMERIEELEEELAELEAELAELEAELEEKKAELD-- 148
|
170
....*....|....*..
gi 356874788 431 nEEKEELKKQVEKLQAQ 447
Cdd:COG1579 149 -EELAELEAELEELEAE 164
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
247-466 |
1.20e-09 |
|
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: 61.19 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 247 EKKVKMLEQQRSELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLADLQKQVTDLEAERE----QKQRDFDRKLll 316
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 317 aKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS-IQTPPSspptafgspEGAGA 395
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeIEKLKK---------ENQSY 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356874788 396 LLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKARE 466
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
241-481 |
4.00e-09 |
|
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: 58.62 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 241 VALGAAEKKVKMLEQQRSELlevnkqwdqhfrsmkqqyEQKITELRQKLADLQKQVTDLEAEREQkqrdFDRKLLLAKSK 320
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQL------------------QQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 321 IemeetdkEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEealsiQTPPSSPPTAFGSPEGAGALLR-- 398
Cdd:COG4942 71 I-------RALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY-----RLGRQPPLALLLSPEDFLDAVRrl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 399 --------------------KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAF 458
Cdd:COG4942 139 qylkylaparreqaeelradLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|...
gi 356874788 459 KDEEKAREALRQQKRKAKASGER 481
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
147-445 |
7.19e-09 |
|
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: 58.91 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 147 KNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAG 226
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 227 QQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---------------------------- 278
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerleslerriaaterrl 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 279 ---EQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKL-LLAKSKIEMEE--TDKEQLTAEAKELRQKVKYLQDQLSPL 352
Cdd:TIGR02168 841 edlEEQIEELSEDIESLAAEIEELEELIEELESELEALLnERASLEEALALlrSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 353 TRQRE-YQEK------EIQRLNKALEEALSI--QTPPSSPPTAFGSPEGAGALLRKqelvtqnelLKQQVKIF------- 416
Cdd:TIGR02168 921 REKLAqLELRleglevRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRRLKR---------LENKIKELgpvnlaa 991
|
330 340
....*....|....*....|....*....
gi 356874788 417 EEDFQRERSDRERMNEEKEELKKQVEKLQ 445
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
282-475 |
1.07e-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: 58.53 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 282 ITELRQKLADLQKQVT------DLEAEREQKQ--------RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQD 347
Cdd:TIGR02168 195 LNELERQLKSLERQAEkaerykELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 348 QLSPLtrqreyqEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDR 427
Cdd:TIGR02168 275 EVSEL-------EEEIEELQKELYALANEI---------------SRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 356874788 428 ERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKA 475
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
274-471 |
1.77e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 274 MKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLS 350
Cdd:COG4913 247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 351 PLTRQREYQ--------EKEIQRLNKALEE-------------ALSIQTPPSspptafgspegAGALLRKQELVTQN-EL 408
Cdd:COG4913 327 ELEAQIRGNggdrleqlEREIERLERELEErerrrarleallaALGLPLPAS-----------AEEFAALRAEAAALlEA 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356874788 409 LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLkafkdeEKAREALRQQ 471
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL------LALRDALAEA 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-485 |
3.66e-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: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 276 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 355
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEEL-----------EEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 356 REYQEKEIQRLNKALEEALSIQTPPSSpptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQrerSDRERMNEEKE 435
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEE--------RLEEAEEELAEAEAEIEELEAQIEQLKEELK---ALREALDELRA 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 356874788 436 ELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERYHVE 485
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
399-447 |
4.72e-08 |
|
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: 50.81 E-value: 4.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 356874788 399 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 447
Cdd:cd09803 34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-478 |
5.17e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 253 LEQQRSELLEVNKQWDQH------FRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQ-KQRDFDRKLLLAKSKIEMEE 325
Cdd:COG1196 269 LEELRLELEELELELEEAqaeeyeLLAELARLEQDIARLEERRRELEERLEELEEELAElEEELEELEEELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 326 TDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNkALEEALSIQTppsspptafgspEGAGALLRKQELVTQ 405
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-ALRAAAELAA------------QLEELEEAEEALLER 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356874788 406 NELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKAS 478
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
275-477 |
7.16e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 7.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 275 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSplTR 354
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 355 QREYQEKeiQRLNKALEEALSIQtppsSPPTAFGSPEGAGALLRKQ-ELVTQNELLKQQVKIFEEDFQRERSDRERMNEE 433
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLGSE----SFSDFLDRLSALSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 356874788 434 KEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKA 477
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
244-471 |
9.22e-08 |
|
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: 55.46 E-value: 9.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 244 GAAEKKVKmLEQQRSELLEVNKQWDQhfrsmkqqYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEM 323
Cdd:TIGR02169 164 GVAEFDRK-KEKALEELEEVEENIER--------LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 324 EETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL-----EEALSIQTppsspptAFGSPEGAGALLR 398
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKE-------KIGELEAEIASLE 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356874788 399 KQElvtqnELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEekaREALRQQ 471
Cdd:TIGR02169 308 RSI-----AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE---LEDLRAE 372
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
137-375 |
1.07e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 137 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgrpgspkm 216
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL------------------- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 217 egTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---EQKITELRQKLADLQ 293
Cdd:COG1196 329 --EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 294 KQVTDLE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL 370
Cdd:COG1196 407 EAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
....*
gi 356874788 371 EEALS 375
Cdd:COG1196 487 AEAAA 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-481 |
4.53e-07 |
|
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: 53.15 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 131 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgr 210
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL------------- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 211 pgspkmegTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEqqRSELLEVNKQWDQHFRSMKQQY---EQKITELRQ 287
Cdd:TIGR02169 750 --------EQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVsriEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 288 KLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQ 364
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 365 RLNKALEEA-LSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEkEELKKQVEK 443
Cdd:TIGR02169 900 ELERKIEELeAQIEK----------------KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQR 962
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 356874788 444 LQAQV-TLSNAQLKAFKDEEKAREALRQ-QKRKAKASGER 481
Cdd:TIGR02169 963 VEEEIrALEPVNMLAIQEYEEVLKRLDElKEKRAKLEEER 1002
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
131-441 |
7.84e-07 |
|
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: 52.38 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 131 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegaSGR 210
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL----------EAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 211 PGSPKMEGTGKKAVAGQQQASVTAGKVPEV-VALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELR 286
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 287 QKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLtrqrEYQEKEIQRL 366
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL----EEELSEIEDP 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 367 NKALEEalsiqTPPSSPP---------------TAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEdfqreRSDRERMN 431
Cdd:TIGR02169 940 KGEDEE-----IPEEELSledvqaelqrveeeiRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE-----RKAILERI 1009
|
330
....*....|
gi 356874788 432 EEKEELKKQV 441
Cdd:TIGR02169 1010 EEYEKKKREV 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
154-477 |
8.67e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 154 ILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGasgrpgspKMEGTGKKAVAGQQQASVT 233
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE--------ELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 234 AGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsmkqqYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRK 313
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 314 LLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY--QEKEIQRLNKALEEALSIQ---------TPPSS 382
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLliaaallalLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 383 PPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEE 462
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330
....*....|....*
gi 356874788 463 KAREALRQQKRKAKA 477
Cdd:COG4717 347 EELQELLREAEELEE 361
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
275-441 |
9.56e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 275 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIemeetdkEQLTAEAK-ELRQKVKYL-QDQLSPL 352
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA-------QQAIKEAKkEADEIIKELrQLQKGGY 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 353 TRQREYQEKEIQR-LNKALEEALSIQTPPSSPPTAF--------GSPEGAGALLRK---QELVTQNELLKQQVKIfeedf 420
Cdd:PRK00409 602 ASVKAHELIEARKrLNKANEKKEKKKKKQKEKQEELkvgdevkyLSLGQKGEVLSIpddKEAIVQAGIMKMKVPL----- 676
|
170 180
....*....|....*....|.
gi 356874788 421 qrerSDRERMNEEKEELKKQV 441
Cdd:PRK00409 677 ----SDLEKIQKPKKKKKKKP 693
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-485 |
1.09e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 138 FNRLASKVHKNEQRTSILQTLCEQLRKENEALKA--------------------KLDKGLEQRDQAAERLREENLELKKL 197
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAeekkkadeakkkaeeakkadEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 198 LMSNGNKEGASG---RPGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSM 274
Cdd:PTZ00121 1345 AEAAKAEAEAAAdeaEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 275 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLtR 354
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA-K 1503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 355 QREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 434
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 356874788 435 EELKKQVEKLQAQVTLSNAQLKAFKDEE--KAREALRQQKRKAKASGERYHVE 485
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVE 1636
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
243-444 |
3.16e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 243 LGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQ---KITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKS 319
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAA----LEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 320 KIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS--IQTPPSSPPTAFGSPEGAGALL 397
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRafNREWPAETADLDADLESLPEYL 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 356874788 398 RKQELVTQNELLKQQVKIFEedFQRERSDRE------RMNEEKEELKKQVEKL 444
Cdd:COG4913 819 ALLDRLEEDGLPEYEERFKE--LLNENSIEFvadllsKLRRAIREIKERIDPL 869
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-476 |
3.27e-06 |
|
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: 50.45 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 149 EQRTSILQTLCEQLRKENEALKAKLDKGLEQRDqaaerLREENLELK-KLLMSNGNKEGASgrpgspKMEGTGKKAVAGQ 227
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQA-----LLKEKREYEgYELLKEKEALERQ------KEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 228 QQASVTAgkvpevvalgAAEKKVKMLEQQRSELLEVNKQwdqhfrsMKQQYEQKITELRQKLADLQKQVTDLE---AERE 304
Cdd:TIGR02169 252 ELEKLTE----------EISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLErsiAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 305 QKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspp 384
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE------------ 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 385 tafgspegagallrkqelvTQNELLKQQVKIfeEDFQRERSD----RERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 460
Cdd:TIGR02169 383 -------------------TRDELKDYREKL--EKLKREINElkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
330
....*....|....*..
gi 356874788 461 E-EKAREALRQQKRKAK 476
Cdd:TIGR02169 442 EkEDKALEIKKQEWKLE 458
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
407-449 |
4.15e-06 |
|
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: 45.36 E-value: 4.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 356874788 407 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 449
Cdd:pfam16516 55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-477 |
4.58e-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: 49.67 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 262 EVNKQWDqhfrSMKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFdrklllAKSKIEMEETDKEQLTAEAKELR 339
Cdd:TIGR02168 197 ELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEELREELEE------LQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 340 QKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEA-LSIQTPPSSPPTAFGSPEGAGALLR--KQELVTQNELLKQQVKIF 416
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLERQLEELEAQLEelESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356874788 417 EEDfqrersdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKA 477
Cdd:TIGR02168 347 EEL-------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
142-480 |
6.90e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 142 ASKVHKNEQRTSILQTLCEQLRKENEALKAKLD--KGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGT 219
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 220 GKKAVAGQQQASVTAGKVPEvvALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELRQKlADLQKQV 296
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEakkKADEAKKA-AEAKKKA 1512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 297 TDLEAEREQKQRDFDRKlllAKSKIEMEETDKEQLTAEAKELR--QKVKYLQDQlspltRQREYQEKEIQRLNKAL---E 371
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKK---AEEAKKADEAKKAEEKKKADELKkaEELKKAEEK-----KKAEEAKKAEEDKNMALrkaE 1584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 372 EALSIQTPPSSPPTAFGSPEGAGAL--LRKQE-------LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEE--LKKQ 440
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAeeAKKAEeakikaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkIKAA 1664
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 356874788 441 VEKLQAQVTLSNAQ--LKAFKDEEKAREALRQQKRKAKASGE 480
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEeaKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
131-447 |
6.92e-06 |
|
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: 49.20 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 131 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGR 210
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 211 PGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLA 290
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 291 DLQKQVTDLEAEREQK--------QRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ--E 360
Cdd:pfam02463 835 LEELALELKEEQKLEKlaeeelerLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLleE 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 361 KEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAG----------------ALLRKQELVTQNELLKQQVKIFEEDFQRER 424
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKekeennkeeeeernkrLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
330 340
....*....|....*....|...
gi 356874788 425 SDRERMNEEKEELKKQVEKLQAQ 447
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
247-461 |
7.68e-06 |
|
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: 48.86 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 247 EKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEAEREQKQrdfdrklllakSKIEMEET 326
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 327 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspegagallrkqelvtqn 406
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---------------------------------- 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 356874788 407 elLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 461
Cdd:TIGR04523 466 --LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
247-480 |
8.12e-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: 48.97 E-value: 8.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 247 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQkladlqkqvtDLEAEREQKQRDFDRKLLLAKSKIEMEET 326
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 327 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQEL---- 402
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 403 -----------VTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFkdeEKAREALRQQ 471
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEE-RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM---EREREMMRQI 581
|
....*....
gi 356874788 472 KRKAKASGE 480
Cdd:pfam17380 582 VESEKARAE 590
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
137-377 |
1.09e-05 |
|
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: 48.51 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 137 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgrpgspkm 216
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL------------------- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 217 egtgkKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQV 296
Cdd:TIGR02168 350 -----KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 297 TDLEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 375
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
..
gi 356874788 376 IQ 377
Cdd:TIGR02168 497 LQ 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
279-474 |
1.69e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 279 EQKITELRQKLADLQKQVTDLEAEREQKQRDFD--RKLLLAKSKIEM---EETDKEQLTAEAKELRQKVKYL---QDQLS 350
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEyswDEIDVASAEREIAELEAELERLdasSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 351 PLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERM 430
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIG------------RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 356874788 431 NEEKEELKKQV-EKLQAQvtLSNAQLKAFKDEEKAREALRQQKRK 474
Cdd:COG4913 757 AALGDAVERELrENLEER--IDALRARLNRAEEELERAMRAFNRE 799
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
133-472 |
2.22e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 133 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRKENEALK-AKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRP 211
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 212 GSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEK-----KVKMLEQQRSEllEVNKQWDQHFRSMKQQYEQKITELR 286
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 287 QKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEI 363
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 364 QRLNKALEEalsiqtppsspptafgSPEGAGALLRKQELVTQNELLK----QQVKIFEEDFQRERSDR---ERMNEEKEE 436
Cdd:PTZ00121 1678 EEAKKAEED----------------EKKAAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAEEENKikaEEAKKEAEE 1741
|
330 340 350
....*....|....*....|....*....|....*.
gi 356874788 437 LKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQK 472
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
253-477 |
2.55e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 253 LEQQRSELLEVNKQWDQhfrsmKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQ 330
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEE-----KEEKDlhERLNGLESELAELDEEIERYEEQREQARETRDE----ADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 331 LTaeakELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEaLSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLK 410
Cdd:PRK02224 253 LE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 356874788 411 Q-------QVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLkafKDEEKAREALRQQKRKAKA 477
Cdd:PRK02224 328 DrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV---EDRREEIEELEEEIEELRE 398
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
268-482 |
2.79e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 268 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREqkqrDFDRKLLLAkskiemeetdkeQLTAEAKELRQKVKYLQD 347
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALE----EFRQKNGLV------------DLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 348 QLSPLTRQREYQEKEIQRLNKALEEAlsiqtpPSSPPTAFGSPEGAGALLRKQELVTQ-NEL-------------LKQQV 413
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSG------PDALPELLQSPVIQQLRAQLAELEAElAELsarytpnhpdviaLRAQI 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 414 KIFEEDFQRE-RSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKdeEKAREaLRQQKRKAKASGERY 482
Cdd:COG3206 301 AALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELP--ELEAE-LRRLEREVEVARELY 367
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
286-481 |
2.85e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 286 RQKLADLQKQVTDLEAEREQkqrdfdrklllakskiemeetdkeqLTAEAKELRQKVKYLQDQLSPLTRQREYQ------ 359
Cdd:COG4913 609 RAKLAALEAELAELEEELAE-------------------------AEERLEALEAELDALQERREALQRLAEYSwdeidv 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 360 ---EKEIQRLNKALEEALSiqtppsspptafGSPEgagalLRKqelvtqnelLKQQVKIFEEDFQRERSDRERMNEEKEE 436
Cdd:COG4913 664 asaEREIAELEAELERLDA------------SSDD-----LAA---------LEEQLEELEAELEELEEELDELKGEIGR 717
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 356874788 437 LKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGER 481
Cdd:COG4913 718 LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
137-396 |
3.05e-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: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 137 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmsngnkegasgrpgspKM 216
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----------------AE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 217 EGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQrsellevnkqwdQHFRSMKQQYEQKITELRQKLADLQKQV 296
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL------------QYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 297 TDLEAEREQKQRDfdrklllakskIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 376
Cdd:COG4942 167 AELEAERAELEAL-----------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|
gi 356874788 377 QTPPSSPPTAFGSPEGAGAL 396
Cdd:COG4942 236 AAAAAERTPAAGFAALKGKL 255
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
140-476 |
4.28e-05 |
|
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: 46.50 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 140 RLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKegasgrpgspkMEGT 219
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER-----------IDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 220 GKKAVAGQQQASVTAGKvpevvalgaaEKKVKMLEQQRSELLEVNKQWDQhfrSMKQQYEQKITELRQKLADLQKQVTDL 299
Cdd:pfam02463 243 QELLRDEQEEIESSKQE----------IEKEEEKLAQVLKENKEEEKEKK---LQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 300 EAEREQKQRDfDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQreyQEKEIQRLNKALEEALSIQTP 379
Cdd:pfam02463 310 VDDEEKLKES-EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL---QEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 380 PSSPPTAFGSpEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 459
Cdd:pfam02463 386 LSSAAKLKEE-ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330
....*....|....*..
gi 356874788 460 DEEKAREALRQQKRKAK 476
Cdd:pfam02463 465 LELKKSEDLLKETQLVK 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
247-476 |
4.91e-05 |
|
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: 46.17 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 247 EKKVKMLEQQRSELLEvnkqwDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK------ 320
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLK-----LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlnq 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 321 -IEMEETDKEQLTAEAKELRQ---KVKYLQDQLSPLTRQRE--YQEKEiQRLNKALEEALSIQtppsspptafgspegag 394
Cdd:TIGR04523 258 lKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlNNQKE-QDWNKELKSELKNQ----------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 395 allRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQvtlSNAQLKAFKDEEKAR 465
Cdd:TIGR04523 320 ---EKKLEEIQNQIsqnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEIKNLESQI 393
|
250
....*....|.
gi 356874788 466 EALRQQKRKAK 476
Cdd:TIGR04523 394 NDLESKIQNQE 404
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
242-346 |
4.95e-05 |
|
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: 45.36 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 242 ALGAAEKKVKM-------LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkl 314
Cdd:pfam02841 198 ALTAKEKAIEAerakaeaAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER-- 265
|
90 100 110
....*....|....*....|....*....|..
gi 356874788 315 LLAKSKIEMEETDKEQLTAEAKELRQKVKYLQ 346
Cdd:pfam02841 266 MLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
236-366 |
5.80e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 236 KVPEVVALGAAEKKVKMLEQQRSE--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVtdleaerEQKQ 307
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRL-------LQKE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 356874788 308 RDFDRKLLLAKSKiemeetdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL 366
Cdd:PRK12704 96 ENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
160-470 |
6.98e-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: 45.98 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 160 EQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAG---- 235
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL---EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGikdk 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 236 --KVPEVVALGAAEKKvKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLAdlqkQVTDLEAEREQKqrdfdrk 313
Cdd:pfam12128 399 laKIREARDRQLAVAE-DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLN----QATATPELLLQL------- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 314 lllAKSKIEMEETDKEQLTAEAKELRqkvkyLQDQLSPLTRQREYQEKEIQRLNK-------ALEEALSIQTPPSSPPTA 386
Cdd:pfam12128 467 ---ENFDERIERAREEQEAANAEVER-----LQSELRQARKRRDQASEALRQASRrleerqsALDELELQLFPQAGTLLH 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 387 FGSPEGAG-----------ALLRKQEL------------------------------VTQNELLKQQVKIFEEDFQRERS 425
Cdd:pfam12128 539 FLRKEAPDweqsigkvispELLHRTDLdpevwdgsvggelnlygvkldlkridvpewAASEEELRERLDKAEEALQSARE 618
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 356874788 426 DRERMNEEKEELKKQVEKLQAQVTLSNAQLKafkdeeKAREALRQ 470
Cdd:pfam12128 619 KQAAAEEQLVQANGELEKASREETFARTALK------NARLDLRR 657
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
137-456 |
7.22e-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: 45.88 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 137 EFNRLASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLdkglEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGS 213
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 214 P---------------KMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKK---VKMLEQQRSELLEVNKQWDQHFRSMK 275
Cdd:pfam15921 594 QlekeindrrlelqefKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQLLNEVKTSRNELNSLS 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 276 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSkieMEETD----------KEQLTAEAKE---LRQKV 342
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS---MEGSDghamkvamgmQKQITAKRGQidaLQSKI 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 343 KYLQDQLSPLTRQREYQEKEIQRLNKALeealsiqtppSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQR 422
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLSQEL----------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 356874788 423 ERSDR--ERMNEEKEELKKQ----VEKLQAQVTLSNAQLK 456
Cdd:pfam15921 821 AECQDiiQRQEQESVRLKLQhtldVKELQGPGYTSNSSMK 860
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
71-476 |
7.60e-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: 45.88 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 71 EFEVVTPEEQNSP-ESSSHANAMALGPLPREDGNLMLHLQRLETTLSVCAEEPDhgqlfthlGRMALEFNRLASKVHKNE 149
Cdd:pfam15921 390 EKELSLEKEQNKRlWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ--------GQMERQMAAIQGKNESLE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 150 QRTSI---LQTLCEQLRKENEALKAK-------------LDKGLEQRDQAAERLREE--------NLELKKL--LMSNGN 203
Cdd:pfam15921 462 KVSSLtaqLESTKEMLRKVVEELTAKkmtlessertvsdLTASLQEKERAIEATNAEitklrsrvDLKLQELqhLKNEGD 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 204 K-EGASGRPGSPKMEGTGKKAVAG---QQQASVTAGKVPEVVALGAAEKKVKMLEQQ----RSELlevnkqwdQHFRSMK 275
Cdd:pfam15921 542 HlRNVQTECEALKLQMAEKDKVIEilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEindrRLEL--------QEFKILK 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 276 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllAKSKIEMEetdKEQLTAEAKELRQKVKYLQDQLSPLTRQ 355
Cdd:pfam15921 614 DKKDAKIRELEARVSDLELEKVKLVNAGSERLR--------AVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 356 REYQEKEIQRLNKALEEAL-SIQTPPSSPPTAFGSPEGAGALLRK-----QELVT----QNELLKQQVKIFEEDFQRERS 425
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLkSAQSELEQTRNTLKSMEGSDGHAMKvamgmQKQITakrgQIDALQSKIQFLEEAMTNANK 762
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 356874788 426 DRERMNEEKEELKKQVEKLQAQVTLSNAQLkafkdeekarEALRQQKRKAK 476
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGEL----------EVLRSQERRLK 803
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
247-447 |
7.74e-05 |
|
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: 45.78 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 247 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLqKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEET 326
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 327 DKEQLTAEAKELRQKVKYLQDQLSpltrqREYQEKEIQRLNKALEEALSIQTppsspptafgspegagALLRKQelvtqn 406
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQK----------------SLKKKQ------ 584
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 356874788 407 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 447
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
139-443 |
7.88e-05 |
|
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: 45.78 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 139 NRLASKVHKNEQRTSILQTLCEQLRKENEALkakldkgleqrDQAAERLREENLELKKLLMSNGNKEGASgrpgSPKMEG 218
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELL-----------EKEIERLKETIIKNNSEIKDLTNQDSVK----ELIIKN 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 219 TGKKAVAGQQQASVTAGKVPEVVAlgAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTD 298
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQ--NLEQKQKELKSKEKELKKLNEE--------KKELEEKVKDLTKKISSLKEKIEK 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 299 LEAE---REQKQRDFDRKLL-----LAKSKIEME-----------ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 359
Cdd:TIGR04523 529 LESEkkeKESKISDLEDELNkddfeLKKENLEKEideknkeieelKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 360 EKEIQRLNKALEEAlsiqtppsspptafgSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKK 439
Cdd:TIGR04523 609 EKKISSLEKELEKA---------------KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
....
gi 356874788 440 QVEK 443
Cdd:TIGR04523 674 KIDD 677
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
257-460 |
9.69e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 257 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKqvtdleaeREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 336
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQ--------RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 337 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQTPpsspptAFGSPEGAGALLRKQ---ELVTQNEL--LKQ 411
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQL-QARIQRLAARAP------AWLAAQDALARLREQsgeEFEDSQDVteYMQ 634
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 356874788 412 QVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 460
Cdd:PRK04863 635 QLLERERELTVE---RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
276-480 |
1.24e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 276 QQYEQKIT-------ELRQKLADLQKQVTDLEAerEQKQRDFDRKLLLAKSkiemeetdkeQLTAEAKELRQ---KVKYL 345
Cdd:PRK10929 68 KQYQQVIDnfpklsaELRQQLNNERDEPRSVPP--NMSTDALEQEILQVSS----------QLLEKSRQAQQeqdRAREI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 346 QDQLSPLTRQREyqekEIQRLNKALEEALSIQTPPSSPptafgspegagaLLRKQELVTQNELLKQQVKIFEEDF-QRER 424
Cdd:PRK10929 136 SDSLSQLPQQQT----EARRQLNEIERRLQTLGTPNTP------------LAQAQLTALQAESAALKALVDELELaQLSA 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 356874788 425 SDRERMNEEKEEL-KKQVEKLQAQVTLSNAQLKAFKDEEkAREALRQQKRKAKASGE 480
Cdd:PRK10929 200 NNRQELARLRSELaKKRSQQLDAYLQALRNQLNSQRQRE-AERALESTELLAEQSGD 255
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
215-491 |
1.30e-04 |
|
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: 45.11 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 215 KMEGTGKKAVAGQQQASVTAGKVpEVVAlGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQK 294
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQL-EIIQ-EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 295 QVTDLEAEREQKQR------DFDRKLLLAKSKIEME-ETDKEQltaeAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLN 367
Cdd:pfam15921 357 ELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLEKEQ----NKRLWDRDTGNSITIDHLRRELDDRNMEVQRLE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 368 kaleealsiqtppsspptafgspegagALLRKQELVTQNELLKQQVKI--FEEDFQRERSDRERMNEEKEELKKQVEKLQ 445
Cdd:pfam15921 433 ---------------------------ALLKAMKSECQGQMERQMAAIqgKNESLEKVSSLTAQLESTKEMLRKVVEELT 485
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 356874788 446 A-QVTLSNAQ------LKAFKDEEKAREALRQQKRKAKAS-----GERYHVEPHPEHL 491
Cdd:pfam15921 486 AkKMTLESSErtvsdlTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKNEGDHL 543
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
241-483 |
1.57e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 241 VALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFdRKLLLAKSK 320
Cdd:PHA02562 188 MKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 321 IEMEetdKEQLTAEAKELRQ----------------KVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspp 384
Cdd:PHA02562 267 IKSK---IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK------ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 385 tafgspegagallRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKA 464
Cdd:PHA02562 338 -------------KLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
250
....*....|....*....
gi 356874788 465 RealrqQKRKAKASGERYH 483
Cdd:PHA02562 391 I-----VKTKSELVKEKYH 404
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
317-481 |
1.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 317 AKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE------------------------ 372
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKlqaeiaeaeaeieerreelgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 373 ALSIQTPPSSPPTAFGSPEGAGALLRKQELVT-----QNELLKQQ---VKIFEEDFQRERSDRERMNEEKEELKKQVEKL 444
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkiadaDADLLEELkadKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 356874788 445 QAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGER 481
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
161-198 |
1.86e-04 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 43.43 E-value: 1.86e-04
10 20 30
....*....|....*....|....*....|....*...
gi 356874788 161 QLRKENEALKAKLDKgLEQRDQAAERLREENLELKKLL 198
Cdd:PRK13922 73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
229-331 |
2.31e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 229 QASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR 308
Cdd:PRK11448 140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219
|
90 100
....*....|....*....|...
gi 356874788 309 DFDRKlllAKSKIEMEETDKEQL 331
Cdd:PRK11448 220 EITDQ---AAKRLELSEEETRIL 239
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
133-447 |
2.99e-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: 43.96 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 133 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKaKLDKGLEQRDQAAERLREEnlelkkLLMSNGNKEGASGRPG 212
Cdd:pfam17380 341 RMAMERERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQE------LEAARKVKILEEERQR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 213 SPKMEGTGKKAVAGQQQAsvtagkvpevvalgAAEKKVKMLEQQRSELLEvnkqwdqHFRSMKQQYEQKITELRQKLADL 292
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEE--------------ARQREVRRLEEERAREME-------RVRLEEQERQQQVERLRQQEEER 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 293 QKQVTDLEAEREQKQRdfdrklllakskieMEETDKEQLTAEAKELRQKVkyLQDQlspltRQREYQEKEIQRLNKALEE 372
Cdd:pfam17380 473 KRKKLELEKEKRDRKR--------------AEEQRRKILEKELEERKQAM--IEEE-----RKRKLLEKEMEERQKAIYE 531
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 356874788 373 ALSIQTppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEdfqrERSDRERMNEEKEELKKQVEKLQAQ 447
Cdd:pfam17380 532 EERRRE--------------AEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
148-373 |
3.12e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 148 NEQRTSILQTLcEQLRKENEALKAKLdkglEQRDQAAERLREENlelkKLLMSNGNKEGASGRpgspkmegtgkKAVAGQ 227
Cdd:COG3206 167 ELRREEARKAL-EFLEEQLPELRKEL----EEAEAALEEFRQKN----GLVDLSEEAKLLLQQ-----------LSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 228 QQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEvnkqwDQHFRSMKQQY---EQKITELRQKLAD-------LQKQVT 297
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLaelEAELAELSARYTPnhpdviaLRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356874788 298 DLEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL---QDQLSPLTRQREYQEKEIQRLNKALEEA 373
Cdd:COG3206 302 ALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
143-395 |
3.17e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 143 SKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngNKEGASGRPGSPKMEGTGKK 222
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 223 AVAGQQQASVTAGKVPEVV-------ALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQ 295
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLgsesfsdFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 296 VTDLEAEREQKqrdfdrklllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 375
Cdd:COG3883 163 KAELEAAKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
250 260
....*....|....*....|
gi 356874788 376 IQTPPSSPPTAFGSPEGAGA 395
Cdd:COG3883 225 AAAAAAAAAAAAAAAAAAAA 244
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
262-372 |
4.45e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 40.64 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 262 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 340
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
|
90 100 110
....*....|....*....|....*....|..
gi 356874788 341 KVKYLQDQLSplTRQREYQEKEIQRLNKALEE 372
Cdd:smart00935 77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
160-434 |
4.93e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 160 EQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAGKVPE 239
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 240 VVALGAAEKKVKMLEQQRSELLEVNKQwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKS 319
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKA--EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 320 KIEMEETDK--EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegagalL 397
Cdd:PTZ00121 1701 AKKAEELKKkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH------------------L 1762
|
250 260 270
....*....|....*....|....*....|....*..
gi 356874788 398 RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 434
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
279-476 |
5.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 279 EQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEEtDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY 358
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE-KIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 359 qEKEIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKifeeDFQRERSDRERMNEEKEELK 438
Cdd:PRK03918 292 -AEEYIKLSEFYEEYLD----------------------ELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELK 344
|
170 180 190
....*....|....*....|....*....|....*...
gi 356874788 439 KQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAK 476
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT 382
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
253-374 |
5.37e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 253 LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAeREQKQRDFDRKLLLAKSKIEMEETDKEQLT 332
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPELE 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 333 AEAKELRQKVKYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEEAL 374
Cdd:COG0542 492 KELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEEEL 547
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
255-472 |
5.66e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 255 QQRSELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLADLQKQVTDLEAEREQKQRDfdrkllLAKSKIEMEETDK 328
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 329 EQL-TAEAKELRQKVKYLQDQLspltrqreyqekeiQRLNKALEEA----LSIQTPPSSPPTA---------------FG 388
Cdd:PRK11281 116 ETLsTLSLRQLESRLAQTLDQL--------------QNAQNDLAEYnsqlVSLQTQPERAQAAlyansqrlqqirnllKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 389 SPEGAGALL--RKQELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQAqvTLSNAQ 454
Cdd:PRK11281 182 GKVGGKALRpsQRVLLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQE--AINSKR 254
|
250
....*....|....*...
gi 356874788 455 LKAFkdEEKAREALRQQK 472
Cdd:PRK11281 255 LTLS--EKTVQEAQSQDE 270
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
160-432 |
5.81e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 160 EQLRKENEALKAKLDKGLEQRDQAaERLREENLELKKLLmsngnkegasgrpgspkmegtgkkAVAGQQQASVTAgkvpE 239
Cdd:PRK11281 52 KLLEAEDKLVQQDLEQTLALLDKI-DRQKEETEQLKQQL------------------------AQAPAKLRQAQA----E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 240 VVALGAAEKKVKmleQQRSELLEVnkqwdqhfrsmkQQYEQKITELRQKLADLQKQVTDLEA---------EREQK---- 306
Cdd:PRK11281 103 LEALKDDNDEET---RETLSTLSL------------RQLESRLAQTLDQLQNAQNDLAEYNSqlvslqtqpERAQAalya 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 307 --QRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVKYLQ------DQLSPL-TRQREYQEKEIQRLNK---ALE 371
Cdd:PRK11281 168 nsQRLQQIRNLLKGGKVGgkaLRPSQRVLLQAEQALLNAQNDLQRkslegnTQLQDLlQKQRDYLTARIQRLEHqlqLLQ 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356874788 372 EALSIQTPPSSPPTA--FGSPEGAGAllrkqelVTQNELLKQqvkifEEDFQRERSDR-----ERMNE 432
Cdd:PRK11281 248 EAINSKRLTLSEKTVqeAQSQDEAAR-------IQANPLVAQ-----ELEINLQLSQRllkatEKLNT 303
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
161-342 |
6.05e-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: 41.83 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 161 QLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGrpgspkmEGTGKKAVAGQQQASVTAGKvpEV 240
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EVEARIKKYEEQLGNVRNNK--EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 241 VALgaaEKKVKMLEQQRSELlevnkqwdqhfrsmkqqyEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK 320
Cdd:COG1579 92 EAL---QKEIESLKRRISDL------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 356874788 321 IEMEETDKEQLTAEAKELRQKV 342
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-449 |
6.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 144 KVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmSNGNKEgasgrpgSPKMEGTGKKa 223
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI-KSLKKE-------LEKLEELKKK- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 224 vagqqqasvtagkvpevvaLGAAEKKVKMLEQQRSELLevNKQWDQHFRSMKqQYEQKITELR---QKLADLQKQVTDLE 300
Cdd:PRK03918 558 -------------------LAELEKKLDELEEELAELL--KELEELGFESVE-ELEERLKELEpfyNEYLELKDAEKELE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 301 aEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQkvKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqtpp 380
Cdd:PRK03918 616 -REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEK----- 687
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 356874788 381 sspptafgspegagallRKQELVTQNELLKQQVKIFEEdFQRERSDRERMNEEKEELKKQVEKLQAQVT 449
Cdd:PRK03918 688 -----------------RREEIKKTLEKLKEELEEREK-AKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-372 |
6.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 143 SKVHKNEQRTSILQTLCEQLRKENEALKAKLdKGLEQR-DQAAERLREENLELKKLlmsngnkEGASGRpgSPKMEGTGK 221
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSK-RKLEEKiRELEERIEELKKEIEEL-------EEKVKE--LKELKEKAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 222 KAVAgqqqasVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEA 301
Cdd:PRK03918 294 EYIK------LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--------LEEKEERLEELKKKLKELEKRLEELEE 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356874788 302 EREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE 372
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
251-373 |
7.28e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 251 KMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllaksKIEMEEtdkEQ 330
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE-----------RIERLE---RE 449
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 356874788 331 LTAEAKELRQKVKylqdqlspltRQREYQ--EKEIQRLNKALEEA 373
Cdd:COG2433 450 LSEARSEERREIR----------KDREISrlDREIERLERELEEE 484
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
141-485 |
9.28e-04 |
|
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: 42.26 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 141 LASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEgasgrpgspKMEGTG 220
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL---------KKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 221 KKAVAGQQQASVTAGKVPEV-VALGAAEKKVKMLEQQRSeLLEVNKQWDQHFRSMKQQyEQKITELRQKLADLQKQVTDL 299
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETqERINRARKAAPLAAHIKA-VTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 300 EAEREQKQRDFDRKLLLAKSKiEMEETDKEQLTaEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNkalEEALSIQTP 379
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAH-EVATSIREISC-QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ---REQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 380 PSSpptaFGSPEGAGALLRKQELVTQNELLKQQVKIfEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 459
Cdd:TIGR00618 416 TSA----FRDLQGQLAHAKKQQELQQRYAELCAAAI-TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
330 340
....*....|....*....|....*.
gi 356874788 460 DEEKAREALRQQKRKAKASGERYHVE 485
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPA 516
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
262-372 |
1.02e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.48 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 262 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQK 341
Cdd:pfam03938 19 AAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKK---------------------EQELQQL 77
|
90 100 110
....*....|....*....|....*....|.
gi 356874788 342 VKYLQDQLSplTRQREYQEKEIQRLNKALEE 372
Cdd:pfam03938 78 QQKAQQELQ--KKQQELLQPIQDKINKAIKE 106
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
249-371 |
1.07e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 249 KVKMLEQQRSELLEVNKQWDQHF----RSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEME 324
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 356874788 325 ETDKEQLTAEAKELRQkvkylqdQLSPLTRQREYQEKEIQRLNKALE 371
Cdd:pfam00038 95 LNLRTSAENDLVGLRK-------DLDEATLARVDLEAKIESLKEELA 134
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
245-346 |
1.28e-03 |
|
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: 41.02 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 245 AAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkLLLAKSKiEME 324
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
|
90 100
....*....|....*....|..
gi 356874788 325 ETDKEQLTAEAKELRQKVKYLQ 346
Cdd:cd16269 270 ALLEEGFKEQAELLQEEIRSLK 291
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-473 |
1.57e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 253 LEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKE 329
Cdd:COG4372 40 LDKLQEELEQLREELEQ-AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQaelAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 330 QLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL----EEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQ 405
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLeslqEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356874788 406 NELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKR 473
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
277-512 |
1.83e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 277 QYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKskiemeetDKEQLTAEAKELRQKVKYLQDQLSPLTRQR 356
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQ--------DYDGATAQLRAAQAAVKAAQAQLAQAQIDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 357 EYQEkeiqrlnkaleealsiqtppsspPTAfgsPEGAGAllrKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEE 436
Cdd:pfam00529 127 ARRR-----------------------VLA---PIGGIS---RESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356874788 437 LKKQVEKLQAQVTLSNAQLKAfkDEEKAREALRQQKRKAKASGERYHVEPHPEhlcGAypYAYPPMPAM--VPHHGFE 512
Cdd:pfam00529 178 NQAEVRSELSGAQLQIAEAEA--ELKLAKLDLERTEIRAPVDGTVAFLSVTVD---GG--TVSAGLRLMfvVPEDNLL 248
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-372 |
1.84e-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: 41.20 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 112 ETTLSVCAEEPDHGQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREEN 191
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 192 LELKKLLMSNGNKEGASGRPgSPKMEGTGKKAVAGQQQASVTAGKVPEVVAlgAAEKKVKMLEQQRSELLEVNKQWDQHF 271
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAA--EIEELEELIEELESELEALLNERASLE 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 272 RSMK-------------QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKL--LLAKSKIEMEETDKEQ------ 330
Cdd:TIGR02168 887 EALAllrseleelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEAEALEnkiedd 966
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356874788 331 ----------------------LTA--EAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE 372
Cdd:TIGR02168 967 eeearrrlkrlenkikelgpvnLAAieEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
331-451 |
1.89e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 331 LTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQTPPSSPPTAFgspegAGALLRKQELVTQNELL 409
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQL-----ATERSARREAEAELERL 119
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 356874788 410 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQVTLS 451
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQLTSK 158
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
133-448 |
1.96e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 133 RMALEFNRLASKVHKNEQRTSilqtlCEQLRKENEALKAKLDKGLEQRDQAAERLREEnlELKKllmSNGNKEGASGRPG 212
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKK-----ADEAKKAEEAKKADEAKKAEEKKKADELKKAE--ELKK---AEEKKKAEEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 213 SPKMEGTGKKAVAGQQqasVTAGKVPEVVALGAAEKKVKM-----LEQQRSELLEVNKQwdQHFRSMKQQYEQKITELRQ 287
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKAeeakkAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 288 KLADLQK--QVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQR 365
Cdd:PTZ00121 1648 KAEELKKaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 366 LNKALEEAlsiqtppsspptafgsPEGAGALLRKQELVTQNELLKQQVK--IFEEDFQRERSDRERMNEEKEELKKQVEK 443
Cdd:PTZ00121 1728 NKIKAEEA----------------KKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
....*
gi 356874788 444 LQAQV 448
Cdd:PTZ00121 1792 RRMEV 1796
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
293-576 |
2.27e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.77 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 293 QKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE 372
Cdd:NF033838 203 EEKIKQAKAKVESKKAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKEND 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 373 ALSIQTPP--SSPPTAFGSPEGAGALLRKQELVTQNELLKQ----------------QVKIFEEDFQRERSDRERMNEEK 434
Cdd:NF033838 283 AKSSDSSVgeETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQkeedrrnyptntyktlELEIAESDVKVKEAELELVKEEA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 435 EELKKQVEKLQAQVTLSNAQLKAFK------DEEKAREALRQQKRKAKASGERYHVEPHPEhlcgayPYAYPPMPAmvph 508
Cdd:NF033838 363 KEPRNEEKIKQAKAKVESKKAEATRlekiktDRKKAEEEAKRKAAEEDKVKEKPAEQPQPA------PAPQPEKPA---- 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 356874788 509 hgfedwsqiryPPPPMAMEHPPPLPNSRLFHLPEYTWRLPcggvRNPNQSSQVMDPPTARPTEPESPK 576
Cdd:NF033838 433 -----------PKPEKPAEQPKAEKPADQQAEEDYARRSE----EEYNRLTQQQPPKTEKPAQPSTPK 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
131-305 |
2.33e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 131 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGR 210
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 211 PGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNkqwdqhFRSMkQQYEqkitELRQKLA 290
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVN------LLAI-EEYE----ELEERYD 798
|
170
....*....|....*
gi 356874788 291 DLQKQVTDLEAEREQ 305
Cdd:COG1196 799 FLSEQREDLEEARET 813
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
242-357 |
2.45e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 242 ALGAAEKKVKMLEQ----QRSELLEVNKQWDQHfRSMKQQYEQKITELRQKLADLQKQVTD-LEAEREQKQRDFDRKLLL 316
Cdd:COG1842 17 LLDKAEDPEKMLDQairdMEEDLVEARQALAQV-IANQKRLERQLEELEAEAEKWEEKARLaLEKGREDLAREALERKAE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 356874788 317 AKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQRE 357
Cdd:COG1842 96 LEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKD 136
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
242-368 |
2.70e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.10 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 242 ALGAAEKKVKMLEQQRSELL-EVNKQwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR-KLLLAKS 319
Cdd:pfam00529 59 ALDSAEAQLAKAQAQVARLQaELDRL--QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrRVLAPIG 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 356874788 320 KIEMEETDKEQltAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 368
Cdd:pfam00529 137 GISRESLVTAG--ALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR 183
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
144-465 |
2.98e-03 |
|
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: 40.48 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 144 KVHKNEQRTSILQTLCEQLRKENEALKAKLD--KGLEQRDQAAERLREENLELKKLLMSNGNKEGASgrpgspKMEGTGK 221
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEdiKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEA------QMEELNK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 222 KAVAgqqqasvTAGKVPEVVALGAAEKKVKMLEQQRselLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEA 301
Cdd:pfam05483 343 AKAA-------HSFVVTEFEATTCSLEELLRTEQQR---LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKK 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 302 EREQKQRDFDRKLLLAKSKIEMEETDKEqLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPS 381
Cdd:pfam05483 413 ILAEDEKLLDEKKQFEKIAEELKGKEQE-LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 382 SPPTAFgspegagaLLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 461
Cdd:pfam05483 492 AHCDKL--------LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDE 563
|
....
gi 356874788 462 EKAR 465
Cdd:pfam05483 564 VKCK 567
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
274-482 |
3.04e-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: 40.73 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 274 MKQQYEQKITELRQKLADLQKQVTDLEAEREQkqrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL-------- 345
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLklneerid 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 346 ---------QDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptAFGSPEGAGALLRKQELVTQNELLKQQVKIF 416
Cdd:pfam02463 241 llqellrdeQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK--------KLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 356874788 417 EEdfQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERY 482
Cdd:pfam02463 313 EE--KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
242-366 |
3.11e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 242 ALGAAEKKVKMLEQQRSELlevnkqwDQHFRSMKQQYEQ----KITELRQKLADLQKQVtdleAEREQKQRDFDRKLLLA 317
Cdd:COG4913 303 ELARLEAELERLEARLDAL-------REELDELEAQIRGnggdRLEQLEREIERLEREL----EERERRRARLEALLAAL 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 318 KSKIEMEETD-----------KEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL 366
Cdd:COG4913 372 GLPLPASAEEfaalraeaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
133-470 |
3.34e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 133 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKglEQRDQAAERLREENLELKKLLMSNG---NKEGASG 209
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ--LENELEAAALEERLKEARLLLLIAAallALLGLGG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 210 RPGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSelLEvNKQWDQHFRSMKQQYEQKITELR--- 286
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE--LE-EEELEELLAALGLPPDLSPEELLell 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 287 ---QKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEET--DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ-- 359
Cdd:COG4717 344 driEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELle 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 360 -------EKEIQRLNKALEEalsiqtppsspptafgspegagalLRKQELVTQNEL--LKQQVKIFEED--FQRERSDRE 428
Cdd:COG4717 424 aldeeelEEELEELEEELEE------------------------LEEELEELREELaeLEAELEQLEEDgeLAELLQELE 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 356874788 429 RMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE------EKAREALRQ 470
Cdd:COG4717 480 ELKAELRELAEEWAALKLALELLEEAREEYREErlppvlERASEYFSR 527
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
248-444 |
3.45e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 248 KKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQK------ITELRQKLADLQKQ----VTDLEAERE------------- 304
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRqqteVLSPEEEKElvekikelekele 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 305 --QKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAlsiqtppss 382
Cdd:COG1340 151 kaKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA--------- 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 356874788 383 pptafgspEGAGALLRKQELVTQNELLKQQVKIFEedfQRERSDRERMNEEKEELKKQVEKL 444
Cdd:COG1340 222 --------QEKADELHEEIIELQKELRELRKELKK---LRKKQRALKREKEKEELEEKAEEI 272
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
254-475 |
3.83e-03 |
|
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: 40.21 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 254 EQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKL----ADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEME----- 324
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpswqs 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 325 ------------ETDKEQLTAEAKELRQKVKY-LQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPE 391
Cdd:pfam12128 355 elenleerlkalTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 392 -GAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDR--ERMNEEKEELKKQVEKLQaqvtlsNAQLKAFKDEEKAREAL 468
Cdd:pfam12128 435 fNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDEriERAREEQEAANAEVERLQ------SELRQARKRRDQASEAL 508
|
....*..
gi 356874788 469 RQQKRKA 475
Cdd:pfam12128 509 RQASRRL 515
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
281-470 |
4.39e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 38.73 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 281 KITELRQKLADLQKQVTDLEAErEQKQRDFDRKLLLAKSKIEMEETDKEQL----TAEAKELRQKVKYLQDQLSPLTRQR 356
Cdd:pfam15619 12 KIKELQNELAELQSKLEELRKE-NRLLKRLQKRQEKALGKYEGTESELPQLiarhNEEVRVLRERLRRLQEKERDLERKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 357 EYQEKEIQRLNKALE--EALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQR-----ERSDRER 429
Cdd:pfam15619 91 KEKEAELLRLRDQLKrlEKLSEDK----------------NLAEREELQKKLEQLEAKLEDKDEKIQDlerklELENKSF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 356874788 430 MNEEKEELKKQVEklqAQVTLSNAQLKAFKDEEKAREALRQ 470
Cdd:pfam15619 155 RRQLAAEKKKHKE---AQEEVKILQEEIERLQQKLKEKERE 192
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
257-460 |
4.51e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 257 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKQVTDLEAEREQkQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 336
Cdd:COG3096 490 RSQAWQTARELLRRYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERL-LEEFCQRIGQQLDAAEELEELLAELEAQLE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 337 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIF 416
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQD----------------ALERLREQSGEALADSQEVTAA 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 356874788 417 -EEDFQRERS---DRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 460
Cdd:COG3096 632 mQQLLEREREatvERDELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
253-374 |
5.07e-03 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 39.57 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 253 LEQQRSELLEVNKQWD----QHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLL-------AKSKI 321
Cdd:pfam14643 243 VEEWWASLEALNEQLDqyhdQCMTKLRAEYEEVWQECLARVQKLKQELLDYKVCSEEEAEALVNEEFLplvgklqRDAED 322
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 356874788 322 EMEETDK--EQLtaeAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAL 374
Cdd:pfam14643 323 ELEKLDKflEEL---AKQTEAQSEDLFKFFREAAQLWDVHQTELAKQELELEKKL 374
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
311-457 |
5.08e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.65 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 311 DRKLLLAKSKIEMEETDKE------QLTAEAKELRQKVKYLQDQlspltrQREYQEKEIQRLNKAlEEALSIQtppsspp 384
Cdd:COG1842 23 DPEKMLDQAIRDMEEDLVEarqalaQVIANQKRLERQLEELEAE------AEKWEEKARLALEKG-REDLARE------- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 356874788 385 tafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKA 457
Cdd:COG1842 89 ----------ALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKV 151
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
235-361 |
5.82e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 39.25 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 235 GKVPE-VVALGAAEKKVKML-EQQRSelleVNKQwdqHFRSMkQQYEQKITELRQKLADLQKQVTDLEAEREQKqRDFDR 312
Cdd:smart00435 245 GNVAEkILAYNRANREVAILcNHQRT----VSKT---HEKSM-EKLQEKIKALKYQLKRLKKMILLFEMISDLK-RKLKS 315
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 356874788 313 KLLLAKSKIEME-ETDKEQLTAEAKELRQkVKYLQDQLSPLTRQREYQEK 361
Cdd:smart00435 316 KFERDNEKLDAEvKEKKKEKKKEEKKKKQ-IERLEERIEKLEVQATDKEE 364
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
253-487 |
5.98e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 253 LEQQRSELLEVNKQWDQHFRSMKQ------QYEQKITELRQKLADLQKQVTDLEAER---EQKQRDFDRKLLLAKSKIEM 323
Cdd:COG4372 68 LEQARSELEQLEEELEELNEQLQAaqaelaQAQEELESLQEEAEELQEELEELQKERqdlEQQRKQLEAQIAELQSEIAE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 324 EETDKEQLTAEAKELRQKVKYLQDQLSPLTRQrEYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSP----EGAGALLRK 399
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEA-EAEQALDELLKEANRNAEKEEELAEAEKLIESLPrelaEELLEAKDS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 400 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASG 479
Cdd:COG4372 227 LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
....*...
gi 356874788 480 ERYHVEPH 487
Cdd:COG4372 307 LSLIGALE 314
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
280-485 |
7.17e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 280 QKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllAKSKIEMEETDKEQLTAEAKELRQkvkylQDQLSPLTRQREYQ 359
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE--------LEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 360 EKEIQRLNKALEEALSiqtppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRErmNEEKEELKK 439
Cdd:COG4717 138 EAELAELPERLEELEE-------------------RLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEELQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 356874788 440 QVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERYHVE 485
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
242-375 |
8.54e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.98 E-value: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 242 ALGAAEKKVKMLEQQ----RSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADLQKQVTDLEAERE----QKQRDFDRK 313
Cdd:COG1579 25 RLKELPAELAELEDElaalEARLEAAKTELED-LEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 356874788 314 LLLAKSKIEMEETDK-EQLTAEAKELRQKVKYLQDQLSPLTRQRE----YQEKEIQRLNKALEEALS 375
Cdd:COG1579 104 RISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAA 170
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| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
253-350 |
8.65e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 36.39 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 253 LEQQRSELLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKE 329
Cdd:pfam13863 1 LLEKKREMFLVQLALDA----KREEIERLEELLKQREEELEKKEQELKEDLIKFDkflKENDAKRRRALKKAEEETKLKK 76
|
90 100
....*....|....*....|.
gi 356874788 330 QLTAEAKELRQKVKYLQDQLS 350
Cdd:pfam13863 77 EKEKEIKKLTAQIEELKSEIS 97
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
329-468 |
9.52e-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: 38.50 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356874788 329 EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqtppsspptafgspeGAGALLRKQELVTQNEL 408
Cdd:cd22656 124 DDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLT----------------DEGGAIARKEIKDLQKE 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 356874788 409 LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE-EKAREAL 468
Cdd:cd22656 188 LEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALiGPAIPAL 248
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