|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
298-538 |
7.64e-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: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 298 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 374
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 375 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 454
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 455 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE-----------EKAREALRQ 523
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEleelseelrelESKRSELRR 915
|
250
....*....|....*
gi 129560475 524 QKRKAKASGERYHVE 538
Cdd:TIGR02168 916 ELEELREKLAQLELR 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
299-530 |
6.79e-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: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 299 AEKKVKMLE-QQRSELLEVNKQW--DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR---------- 365
Cdd:COG1196 209 AEKAERYRElKEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 366 KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspeg 445
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE-------------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 446 AGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQK 525
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
....*
gi 129560475 526 RKAKA 530
Cdd:COG1196 435 EEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
193-529 |
9.57e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 9.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 193 RLASKVHKNEQRTSILQTLcEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEgasgrpgspkmegt 272
Cdd:COG1196 226 EAELLLLKLRELEAELEEL-EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE-------------- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 273 gkkAVAGQQQASVTAGKVPEvvalgaaEKKVKMLEQQRSELLEVNKQWDQHfrsmKQQYEQKITELRQKLADLQKQVTDL 352
Cdd:COG1196 291 ---YELLAELARLEQDIARL-------EERRRELEERLEELEEELAELEEE----LEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 353 EAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtp 432
Cdd:COG1196 357 EAELAEAEE---ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA-- 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 433 psspptafgspegAGALLRKQELVTQNELLKQQVKIfEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 512
Cdd:COG1196 432 -------------ELEEEEEEEEEALEEAAEEEAEL-EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330
....*....|....*..
gi 129560475 513 DEEKAREALRQQKRKAK 529
Cdd:COG1196 498 EAEADYEGFLEGVKAAL 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
335-530 |
3.62e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 335 ITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEK 414
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 415 EIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 494
Cdd:COG1196 275 ELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190
....*....|....*....|....*....|....*.
gi 129560475 495 EKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKA 530
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
333-531 |
4.00e-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: 62.09 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 333 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 412
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 413 EKEIQRLNKALEEAL--SIQTPPSSPPTAFGSPEGAGALLRKQELVTQ-NELLKQQVKIFEEDFQRERSDRERMNEEKEE 489
Cdd:COG4942 96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 129560475 490 LKKQVEKLQAQvtlsNAQLKAFKDEEKAREALRQQKRKAKAS 531
Cdd:COG4942 176 LEALLAELEEE----RAALEALKAERQKLLARLEKELAELAA 213
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
300-519 |
4.40e-10 |
|
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: 62.73 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 300 EKKVKMLEQQRSELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLADLQKQVTDLEAERE----QKQRDFDRKLll 369
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 370 aKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS-IQTPPSspptafgspEGAGA 448
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeIEKLKK---------ENQSY 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 129560475 449 LLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKARE 519
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
329-500 |
5.81e-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: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 329 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 408
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 409 REYQ--EKEI---QRLNKALEEALsiqtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRErm 483
Cdd:COG1579 89 KEYEalQKEIeslKRRISDLEDEI------------------LELMERIEELEEELAELEAELAELEAELEEKKAELD-- 148
|
170
....*....|....*..
gi 129560475 484 nEEKEELKKQVEKLQAQ 500
Cdd:COG1579 149 -EELAELEAELEELEAE 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
294-534 |
4.20e-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: 59.01 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 294 VALGAAEKKVKMLEQQRSELlevnkqwdqhfrsmkqqyEQKITELRQKLADLQKQVTDLEAEREQkqrdFDRKLLLAKSK 373
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQL------------------QQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 374 IemeetdkEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEealsiQTPPSSPPTAFGSPEGAGALLR-- 451
Cdd:COG4942 71 I-------RALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY-----RLGRQPPLALLLSPEDFLDAVRrl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 452 --------------------KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAF 511
Cdd:COG4942 139 qylkylaparreqaeelradLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|...
gi 129560475 512 KDEEKAREALRQQKRKAKASGER 534
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
200-498 |
7.34e-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: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 200 KNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAG 279
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 280 QQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---------------------------- 331
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerleslerriaaterrl 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 332 ---EQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKL-LLAKSKIEME--ETDKEQLTAEAKELRQKVKYLQDQLSPL 405
Cdd:TIGR02168 841 edlEEQIEELSEDIESLAAEIEELEELIEELESELEALLnERASLEEALAllRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 406 TRQRE-YQEK------EIQRLNKALEEALSI--QTPPSSPPTAFGSPEGAgallrKQELvtqnELLKQQVKIF------- 469
Cdd:TIGR02168 921 REKLAqLELRleglevRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEA-----RRRL----KRLENKIKELgpvnlaa 991
|
330 340
....*....|....*....|....*....
gi 129560475 470 EEDFQRERSDRERMNEEKEELKKQVEKLQ 498
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
335-528 |
1.14e-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: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 335 ITELRQKLADLQKQVT------DLEAEREQKQ--------RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQD 400
Cdd:TIGR02168 195 LNELERQLKSLERQAEkaerykELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 401 QLSPLtrqreyqEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDR 480
Cdd:TIGR02168 275 EVSEL-------EEEIEELQKELYALANEI---------------SRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 129560475 481 ERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKA 528
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
327-524 |
2.00e-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: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 327 MKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLS 403
Cdd:COG4913 247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 404 PLTRQREYQ--------EKEIQRLNKALEE-------------ALSIQTPPSspptafgspegAGALLRKQELVTQN-EL 461
Cdd:COG4913 327 ELEAQIRGNggdrleqlEREIERLERELEErerrrarleallaALGLPLPAS-----------AEEFAALRAEAAALlEA 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 129560475 462 LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLkafkdeEKAREALRQQ 524
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL------LALRDALAEA 452
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
452-500 |
3.60e-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: 51.20 E-value: 3.60e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 129560475 452 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 500
Cdd:cd09803 34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
329-538 |
3.89e-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: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 329 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 408
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEEL-----------EEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 409 REYQEKEIQRLNKALEEALSIQTPPSSpptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQrerSDRERMNEEKE 488
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEE--------RLEEAEEELAEAEAEIEELEAQIEQLKEELK---ALREALDELRA 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 129560475 489 ELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERYHVE 538
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
328-530 |
5.41e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 328 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSplTR 407
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 408 QREYQEKeiQRLNKALEEALSIQtppsSPPTAFGSPEGAGALLRKQ-ELVTQNELLKQQVKIFEEDFQRERSDRERMNEE 486
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLGSE----SFSDFLDRLSALSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 129560475 487 KEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKA 530
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
292-531 |
6.51e-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: 6.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 292 EVVALGAAEKKVKMLEQQRSEL-LEVNKQWDQHFRSMKQ--QYEQKITELRQKLADLQKQVTDLEAEREQ-KQRDFDRKL 367
Cdd:COG1196 258 LEAELAELEAELEELRLELEELeLELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAElEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 368 LLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNkALEEALSIQTppsspptafgspEGAG 447
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE-ALRAAAELAA------------QLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 448 ALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRK 527
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
....
gi 129560475 528 AKAS 531
Cdd:COG1196 485 ELAE 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
297-524 |
1.00e-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: 55.46 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 297 GAAEKKVKmLEQQRSELLEVNKQWDQhfrsmkqqYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEM 376
Cdd:TIGR02169 164 GVAEFDRK-KEKALEELEEVEENIER--------LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 377 EETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL-----EEALSIQTppsspptAFGSPEGAGALLR 451
Cdd:TIGR02169 235 LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKE-------KIGELEAEIASLE 307
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 129560475 452 KQElvtqnELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEekaREALRQQ 524
Cdd:TIGR02169 308 RSI-----AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE---LEDLRAE 372
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
190-428 |
1.29e-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: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 190 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgrpgspkm 269
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL------------------- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 270 egTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---EQKITELRQKLADLQ 346
Cdd:COG1196 329 --EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 347 KQVTDLE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL 423
Cdd:COG1196 407 EAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
....*
gi 129560475 424 EEALS 428
Cdd:COG1196 487 AEAAA 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-534 |
5.73e-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: 52.76 E-value: 5.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 184 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgr 263
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL------------- 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 264 pgspkmegTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEqqRSELLEVNKQWDQHFRSMKQQY---EQKITELRQ 340
Cdd:TIGR02169 750 --------EQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVsriEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 341 KLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQ 417
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 418 RLNKALEEA-LSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEkEELKKQVEK 496
Cdd:TIGR02169 900 ELERKIEELeAQIEK----------------KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-EDVQAELQR 962
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 129560475 497 LQAQV-TLSNAQLKAFKDEEKAREALRQ-QKRKAKASGER 534
Cdd:TIGR02169 963 VEEEIrALEPVNMLAIQEYEEVLKRLDElKEKRAKLEEER 1002
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
191-538 |
6.98e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 191 FNRLASKVHKNEQRTSILQTLCEQLRKENEALKA--------------------KLDKGLEQRDQAAERLREENLELKKL 250
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAeekkkadeakkkaeeakkadEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 251 LMSNGNKEGASG---RPGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSM 327
Cdd:PTZ00121 1345 AEAAKAEAEAAAdeaEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 328 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLtR 407
Cdd:PTZ00121 1425 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA-K 1503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 408 QREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 487
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKA 1583
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 129560475 488 EELKKQVEKLQAQVTLSNAQLKAFKDEE--KAREALRQQKRKAKASGERYHVE 538
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVE 1636
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
207-530 |
8.22e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 207 ILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGasgrpgspKMEGTGKKAVAGQQQASVT 286
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE--------ELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 287 AGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsmkqqYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRK 366
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 367 LLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY--QEKEIQRLNKALEEALSIQ---------TPPSS 435
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLliaaallalLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 436 PPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEE 515
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330
....*....|....*
gi 129560475 516 KAREALRQQKRKAKA 530
Cdd:COG4717 347 EELQELLREAEELEE 361
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-494 |
9.64e-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: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 184 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegaSGR 263
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL----------EAR 787
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 264 PGSPKMEGTGKKAVAGQQQASVTAGKVPEV-VALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELR 339
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEVSRIEARLREIeQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 340 QKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLtrqrEYQEKEIQRL 419
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL----EEELSEIEDP 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 420 NKALEEalsiqTPPSSPP---------------TAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEdfqreRSDRERMN 484
Cdd:TIGR02169 940 KGEDEE-----IPEEELSledvqaelqrveeeiRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE-----RKAILERI 1009
|
330
....*....|
gi 129560475 485 EEKEELKKQV 494
Cdd:TIGR02169 1010 EEYEKKKREV 1019
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
328-494 |
1.09e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 328 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIemeetdkEQLTAEAK-ELRQKVKYL-QDQLSPL 405
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA-------QQAIKEAKkEADEIIKELrQLQKGGY 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 406 TRQREYQEKEIQR-LNKALEEALSIQTPPSSPPTAF--------GSPEGAGALLRK---QELVTQNELLKQQVKIfeedf 473
Cdd:PRK00409 602 ASVKAHELIEARKrLNKANEKKEKKKKKQKEKQEELkvgdevkyLSLGQKGEVLSIpddKEAIVQAGIMKMKVPL----- 676
|
170 180
....*....|....*....|.
gi 129560475 474 qrerSDRERMNEEKEELKKQV 494
Cdd:PRK00409 677 ----SDLEKIQKPKKKKKKKP 693
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
300-514 |
3.16e-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: 50.40 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 300 EKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEAEREQKQrdfdrklllakSKIEMEET 379
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 380 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspegagallrkqelvtqn 459
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---------------------------------- 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 129560475 460 elLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 514
Cdd:TIGR04523 466 --LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKK 518
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
460-502 |
3.21e-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: 46.13 E-value: 3.21e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 129560475 460 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 502
Cdd:pfam16516 55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
195-533 |
3.46e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 195 ASKVHKNEQRTSILQTLCEQLRKENEALKAKLD--KGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGT 272
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 273 GKKAVAGQQQASVTAGKVPEvvALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELRQKlADLQKQV 349
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEakkKADEAKKA-AEAKKKA 1512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 350 TDLEAEREQKQRDFDRKlllAKSKIEMEETDKEQLTAEAKELR--QKVKYLQDQlspltRQREYQEKEIQRLNKAL---E 424
Cdd:PTZ00121 1513 DEAKKAEEAKKADEAKK---AEEAKKADEAKKAEEKKKADELKkaEELKKAEEK-----KKAEEAKKAEEDKNMALrkaE 1584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 425 EALSIQTPPSSPPTAFGSPEGAGAL--LRKQE-------LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEE--LKKQ 493
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAeeAKKAEeakikaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkIKAA 1664
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 129560475 494 VEKLQAQVTLSNAQ--LKAFKDEEKAREALRQQKRKAKASGE 533
Cdd:PTZ00121 1665 EEAKKAEEDKKKAEeaKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
296-497 |
3.58e-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: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 296 LGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQ---KITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKS 372
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAA----LEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 373 KIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS--IQTPPSSPPTAFGSPEGAGALL 450
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRafNREWPAETADLDADLESLPEYL 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 129560475 451 RKQELVTQNELLKQQVKIFEedFQRERSDRE------RMNEEKEELKKQVEKL 497
Cdd:COG4913 819 ALLDRLEEDGLPEYEERFKE--LLNENSIEFvadllsKLRRAIREIKERIDPL 869
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-529 |
3.75e-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: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 202 EQRTSILQTLCEQLRKENEALKAKLDKGLEQRDqaaerLREENLELK-KLLMSNGNKEGASgrpgspKMEGTGKKAVAGQ 280
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQA-----LLKEKREYEgYELLKEKEALERQ------KEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 281 QQASVTAgkvpevvalgAAEKKVKMLEQQRSELLEVNKQwdqhfrsMKQQYEQKITELRQKLADLQKQVTDLE---AERE 357
Cdd:TIGR02169 252 ELEKLTE----------EISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLErsiAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 358 QKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspp 437
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE------------ 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 438 tafgspegagallrkqelvTQNELLKQQVKIfeEDFQRERSD----RERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 513
Cdd:TIGR02169 383 -------------------TRDELKDYREKL--EKLKREINElkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEE 441
|
330
....*....|....*..
gi 129560475 514 E-EKAREALRQQKRKAK 529
Cdd:TIGR02169 442 EkEDKALEIKKQEWKLE 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
315-530 |
4.81e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 315 EVNKQWDqhfrSMKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFdrklllAKSKIEMEETDKEQLTAEAKELR 392
Cdd:TIGR02168 197 ELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEELREELEE------LQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 393 QKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEA-LSIQTPPSSPPTAFGSPEGAGALLR--KQELVTQNELLKQQVKIF 469
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLERQLEELEAQLEelESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 129560475 470 EEDfqrersdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKA 530
Cdd:TIGR02168 347 EEL-------KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
300-533 |
5.39e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.74 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 300 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQkladlqkqvtDLEAEREQKQRDFDRKLLLAKSKIEMEET 379
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 380 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQEL---- 455
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 456 -----------VTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFkdeEKAREALRQQ 524
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEE-RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM---EREREMMRQI 581
|
....*....
gi 129560475 525 KRKAKASGE 533
Cdd:pfam17380 582 VESEKARAE 590
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
184-500 |
7.39e-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: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 184 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGR 263
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 264 PGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLA 343
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 344 DLQKQVTDLEAEREQK--------QRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ--E 413
Cdd:pfam02463 835 LEELALELKEEQKLEKlaeeelerLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLleE 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 414 KEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAG----------------ALLRKQELVTQNELLKQQVKIFEEDFQRER 477
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKekeennkeeeeernkrLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
330 340
....*....|....*....|...
gi 129560475 478 SDRERMNEEKEELKKQVEKLQAQ 500
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
190-430 |
1.08e-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: 48.90 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 190 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgrpgspkm 269
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL------------------- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 270 egtgkKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQV 349
Cdd:TIGR02168 350 -----KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 350 TDLEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 428
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
..
gi 129560475 429 IQ 430
Cdd:TIGR02168 497 LQ 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-525 |
1.25e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 186 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRKENEALK-AKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRP 264
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 265 GSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEK-----KVKMLEQQRSEllEVNKQWDQHFRSMKQQYEQKITELR 339
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 340 QKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEI 416
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 417 QRLNKALEEalsiqtppsspptafgSPEGAGALLRKQELVTQNELLK----QQVKIFEEDFQRERSDR---ERMNEEKEE 489
Cdd:PTZ00121 1678 EEAKKAEED----------------EKKAAEALKKEAEEAKKAEELKkkeaEEKKKAEELKKAEEENKikaEEAKKEAEE 1741
|
330 340 350
....*....|....*....|....*....|....*.
gi 129560475 490 LKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQK 525
Cdd:PTZ00121 1742 DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
300-529 |
1.77e-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: 48.09 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 300 EKKVKMLEQQRSELlevnkqwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK------ 373
Cdd:TIGR04523 186 QKNIDKIKNKLLKL--------ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlnq 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 374 -IEMEETDKEQLTAEAKELRQ---KVKYLQDQLSPLTRQRE--YQEKEiQRLNKALEEALSIQtppsspptafgspegag 447
Cdd:TIGR04523 258 lKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlNNQKE-QDWNKELKSELKNQ----------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 448 allRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQvtlSNAQLKAFKDEEKAR 518
Cdd:TIGR04523 320 ---EKKLEEIQNQIsqnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEIKNLESQI 393
|
250
....*....|.
gi 129560475 519 EALRQQKRKAK 529
Cdd:TIGR04523 394 NDLESKIQNQE 404
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
332-527 |
1.83e-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: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 332 EQKITELRQKLADLQKQVTDLEAEREQKQRDFD--RKLLLAKSKIEM---EETDKEQLTAEAKELRQKVKYL---QDQLS 403
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEyswDEIDVASAEREIAELEAELERLdasSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 404 PLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERM 483
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIG------------RLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 129560475 484 NEEKEELKKQV-EKLQAQvtLSNAQLKAFKDEEKAREALRQQKRK 527
Cdd:COG4913 757 AALGDAVERELrENLEER--IDALRARLNRAEEELERAMRAFNRE 799
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
192-496 |
2.65e-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: 47.32 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 192 NRLASKVHKNEQRTSILQTLCEQLRKENEALkakldkgleqrDQAAERLREENLELKKLLMSNGNKEGASgrpgSPKMEG 271
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELL-----------EKEIERLKETIIKNNSEIKDLTNQDSVK----ELIIKN 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 272 TGKKAVAGQQQASVTAGKVPEVVAlgAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTD 351
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQ--NLEQKQKELKSKEKELKKLNEE--------KKELEEKVKDLTKKISSLKEKIEK 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 352 LEAE---REQKQRDFDRKLL-----LAKSKIEME-----------ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 412
Cdd:TIGR04523 529 LESEkkeKESKISDLEDELNkddfeLKKENLEKEideknkeieelKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 413 EKEIQRLNKALEEAlsiqtppsspptafgSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKK 492
Cdd:TIGR04523 609 EKKISSLEKELEKA---------------KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
....
gi 129560475 493 QVEK 496
Cdd:TIGR04523 674 KIDD 677
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
306-530 |
2.91e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 306 LEQQRSELLEVNKQWDQhfrsmKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQ 383
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEE-----KEEKDlhERLNGLESELAELDEEIERYEEQREQARETRDE----ADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 384 LTaeakELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEaLSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLK 463
Cdd:PRK02224 253 LE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 129560475 464 Q-------QVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLkafKDEEKAREALRQQKRKAKA 530
Cdd:PRK02224 328 DrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV---EDRREEIEELEEEIEELRE 398
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-534 |
3.19e-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: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 339 RQKLADLQKQVTDLEAEREQkqrdfdrklllakskiemeetdkeqLTAEAKELRQKVKYLQDQLSPLTRQREYQ------ 412
Cdd:COG4913 609 RAKLAALEAELAELEEELAE-------------------------AEERLEALEAELDALQERREALQRLAEYSwdeidv 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 413 ---EKEIQRLNKALEEALSiqtppsspptafGSPEgagalLRKqelvtqnelLKQQVKIFEEDFQRERSDRERMNEEKEE 489
Cdd:COG4913 664 asaEREIAELEAELERLDA------------SSDD-----LAA---------LEEQLEELEAELEELEEELDELKGEIGR 717
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 129560475 490 LKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGER 534
Cdd:COG4913 718 LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
190-449 |
3.20e-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: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 190 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmsngnkegasgrpgspKM 269
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----------------AE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 270 EGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQrsellevnkqwdQHFRSMKQQYEQKITELRQKLADLQKQV 349
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL------------QYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 350 TDLEAEREQKQRDfdrklllakskIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 429
Cdd:COG4942 167 AELEAERAELEAL-----------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|
gi 129560475 430 QTPPSSPPTAFGSPEGAGAL 449
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 ... |
193-529 |
3.58e-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: 47.27 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 193 RLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKegasgrpgspkMEGT 272
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER-----------IDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 273 GKKAVAGQQQASVTAGKvpevvalgaaEKKVKMLEQQRSELLEVNKQWDQhfrSMKQQYEQKITELRQKLADLQKQVTDL 352
Cdd:pfam02463 243 QELLRDEQEEIESSKQE----------IEKEEEKLAQVLKENKEEEKEKK---LQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 353 EAEREQKQRDfDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQreyQEKEIQRLNKALEEALSIQTP 432
Cdd:pfam02463 310 VDDEEKLKES-EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL---QEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 433 PSSPPTAFGSpEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 512
Cdd:pfam02463 386 LSSAAKLKEE-ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330
....*....|....*..
gi 129560475 513 DEEKAREALRQQKRKAK 529
Cdd:pfam02463 465 LELKKSEDLLKETQLVK 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
300-500 |
3.61e-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: 46.94 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 300 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLqKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEET 379
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 380 DKEQLTAEAKELRQKVKYLQDQLSpltrqREYQEKEIQRLNKALEEALSIQTppsspptafgspegagALLRKQelvtqn 459
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEELKQTQK----------------SLKKKQ------ 584
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 129560475 460 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 500
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
321-535 |
3.74e-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: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 321 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREqkqrDFDRKLLLAkskiemeetdkeQLTAEAKELRQKVKYLQD 400
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALE----EFRQKNGLV------------DLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 401 QLSPLTRQREYQEKEIQRLNKALEEAlsiqtpPSSPPTAFGSPEGAGALLRKQELVTQ-NEL-------------LKQQV 466
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSG------PDALPELLQSPVIQQLRAQLAELEAElAELsarytpnhpdviaLRAQI 300
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 467 KIFEEDFQRE-RSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKdeEKAREaLRQQKRKAKASGERY 535
Cdd:COG3206 301 AALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELP--ELEAE-LRRLEREVEVARELY 367
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
124-529 |
3.97e-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: 47.04 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 124 EFEVVTPEEQNSP-ESSSHANAMALGPLPREDGNLMLHLQRLETTLSVCAEEPDhgqlfthlGRMALEFNRLASKVHKNE 202
Cdd:pfam15921 390 EKELSLEKEQNKRlWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ--------GQMERQMAAIQGKNESLE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 203 QRTSI---LQTLCEQLRKENEALKAK-------------LDKGLEQRDQAAERLREE--------NLELKKL--LMSNGN 256
Cdd:pfam15921 462 KVSSLtaqLESTKEMLRKVVEELTAKkmtlessertvsdLTASLQEKERAIEATNAEitklrsrvDLKLQELqhLKNEGD 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 257 K-EGASGRPGSPKMEGTGKKAVAG---QQQASVTAGKVPEVVALGAAEKKVKMLEQQ----RSELlevnkqwdQHFRSMK 328
Cdd:pfam15921 542 HlRNVQTECEALKLQMAEKDKVIEilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEindrRLEL--------QEFKILK 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 329 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllAKSKIEMEetdKEQLTAEAKELRQKVKYLQDQLSPLTRQ 408
Cdd:pfam15921 614 DKKDAKIRELEARVSDLELEKVKLVNAGSERLR--------AVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 409 REYQEKEIQRLNKALEEAL-SIQTPPSSPPTAFGSPEGAGALLRK-----QELVT----QNELLKQQVKIFEEDFQRERS 478
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLkSAQSELEQTRNTLKSMEGSDGHAMKvamgmQKQITakrgQIDALQSKIQFLEEAMTNANK 762
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 129560475 479 DRERMNEEKEELKKQVEKLQAQVTLSNAQLkafkdeekarEALRQQKRKAK 529
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGEL----------EVLRSQERRLK 803
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
190-509 |
4.36e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 190 EFNRLASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLdkglEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGS 266
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 267 P---------------KMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKK---VKMLEQQRSELLEVNKQWDQHFRSMK 328
Cdd:pfam15921 594 QlekeindrrlelqefKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQLLNEVKTSRNELNSLS 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 329 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSkieMEETD----------KEQLTAEAKE---LRQKV 395
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS---MEGSDghamkvamgmQKQITAKRGQidaLQSKI 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 396 KYLQDQLSPLTRQREYQEKEIQRLNKALeealsiqtppSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQR 475
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLSQEL----------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 129560475 476 ERSDR--ERMNEEKEELKKQ----VEKLQAQVTLSNAQLK 509
Cdd:pfam15921 821 AECQDiiQRQEQESVRLKLQhtldVKELQGPGYTSNSSMK 860
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
295-399 |
4.40e-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: 45.74 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 295 ALGAAEKKVKM-------LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkl 367
Cdd:pfam02841 198 ALTAKEKAIEAerakaeaAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER-- 265
|
90 100 110
....*....|....*....|....*....|..
gi 129560475 368 LLAKSKIEMEETDKEQLTAEAKELRQKVKYLQ 399
Cdd:pfam02841 266 MLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
213-523 |
5.65e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 213 EQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAG---- 288
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL---EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGikdk 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 289 --KVPEVVALGAAEKKvKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLAdlqkQVTDLEAEREQKqrdfdrk 366
Cdd:pfam12128 399 laKIREARDRQLAVAE-DDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLN----QATATPELLLQL------- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 367 lllAKSKIEMEETDKEQLTAEAKELRqkvkyLQDQLSPLTRQREYQEKEIQRLNK-------ALEEALSIQTPPSSPPTA 439
Cdd:pfam12128 467 ---ENFDERIERAREEQEAANAEVER-----LQSELRQARKRRDQASEALRQASRrleerqsALDELELQLFPQAGTLLH 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 440 FGSPEGAG-----------ALLRKQEL------------------------------VTQNELLKQQVKIFEEDFQRERS 478
Cdd:pfam12128 539 FLRKEAPDweqsigkvispELLHRTDLdpevwdgsvggelnlygvkldlkridvpewAASEEELRERLDKAEEALQSARE 618
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 129560475 479 DRERMNEEKEELKKQVEKLQAQVTLSNAQLKafkdeeKAREALRQ 523
Cdd:pfam12128 619 KQAAAEEQLVQANGELEKASREETFARTALK------NARLDLRR 657
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
289-419 |
7.18e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 289 KVPEVVALGAAEKKVKMLEQQRSE--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVtdleaerEQKQ 360
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRL-------LQKE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 129560475 361 RDFDRKLLLAKSKiemeetdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL 419
Cdd:PRK12704 96 ENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
268-544 |
8.21e-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: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 268 KMEGTGKKAVAGQQQASVTAGKVpEVVAlGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQK 347
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSQL-EIIQ-EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 348 QVTDLEAEREQKQR------DFDRKLLLAKSKIEME-ETDKEQltaeAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLN 420
Cdd:pfam15921 357 ELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLEKEQ----NKRLWDRDTGNSITIDHLRRELDDRNMEVQRLE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 421 kaleealsiqtppsspptafgspegagALLRKQELVTQNELLKQQVKI--FEEDFQRERSDRERMNEEKEELKKQVEKLQ 498
Cdd:pfam15921 433 ---------------------------ALLKAMKSECQGQMERQMAAIqgKNESLEKVSSLTAQLESTKEMLRKVVEELT 485
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 129560475 499 A-QVTLSNAQ------LKAFKDEEKAREALRQQKRKAKAS-----GERYHVEPHPEHL 544
Cdd:pfam15921 486 AkKMTLESSErtvsdlTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKNEGDHL 543
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
310-513 |
9.62e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 310 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKqvtdleaeREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 389
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQ--------RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 390 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQTPpsspptAFGSPEGAGALLRKQ---ELVTQNEL--LKQ 464
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQL-QARIQRLAARAP------AWLAAQDALARLREQsgeEFEDSQDVteYMQ 634
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 129560475 465 QVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 513
Cdd:PRK04863 635 QLLERERELTVE---RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
329-533 |
1.29e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 329 QQYEQKIT-------ELRQKLADLQKQVTDLEAerEQKQRDFDRKLLLAKSkiemeetdkeQLTAEAKELRQ---KVKYL 398
Cdd:PRK10929 68 KQYQQVIDnfpklsaELRQQLNNERDEPRSVPP--NMSTDALEQEILQVSS----------QLLEKSRQAQQeqdRAREI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 399 QDQLSPLTRQREyqekEIQRLNKALEEALSIQTPPSSPptafgspegagaLLRKQELVTQNELLKQQVKIFEEDF-QRER 477
Cdd:PRK10929 136 SDSLSQLPQQQT----EARRQLNEIERRLQTLGTPNTP------------LAQAQLTALQAESAALKALVDELELaQLSA 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 129560475 478 SDRERMNEEKEEL-KKQVEKLQAQVTLSNAQLKAFKDEEkAREALRQQKRKAKASGE 533
Cdd:PRK10929 200 NNRQELARLRSELaKKRSQQLDAYLQALRNQLNSQRQRE-AERALESTELLAEQSGD 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
370-534 |
1.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 370 AKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE------------------------ 425
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKlqaeiaeaeaeieerreelgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 426 ALSIQTPPSSPPTAFGSPEGAGALLRKQELVT-----QNELLKQQ---VKIFEEDFQRERSDRERMNEEKEELKKQVEKL 497
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkiadaDADLLEELkadKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 129560475 498 QAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGER 534
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
294-536 |
1.42e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 294 VALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFdRKLLLAKSK 373
Cdd:PHA02562 188 MKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 374 IEMEetdKEQLTAEAKELRQ----------------KVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspp 437
Cdd:PHA02562 267 IKSK---IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK------ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 438 tafgspegagallRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKA 517
Cdd:PHA02562 338 -------------KLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
250
....*....|....*....
gi 129560475 518 RealrqQKRKAKASGERYH 536
Cdd:PHA02562 391 I-----VKTKSELVKEKYH 404
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
186-500 |
1.57e-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: 44.73 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 186 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKaKLDKGLEQRDQAAERLREEnlelkkLLMSNGNKEGASGRPG 265
Cdd:pfam17380 341 RMAMERERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQE------LEAARKVKILEEERQR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 266 SPKMEGTGKKAVAGQQQAsvtagkvpevvalgAAEKKVKMLEQQRSELLEvnkqwdqHFRSMKQQYEQKITELRQKLADL 345
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEE--------------ARQREVRRLEEERAREME-------RVRLEEQERQQQVERLRQQEEER 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 346 QKQVTDLEAEREQKQRdfdrklllakskieMEETDKEQLTAEAKELRQKVkyLQDQlspltRQREYQEKEIQRLNKALEE 425
Cdd:pfam17380 473 KRKKLELEKEKRDRKR--------------AEEQRRKILEKELEERKQAM--IEEE-----RKRKLLEKEMEERQKAIYE 531
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 129560475 426 ALSIQTppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEdfqrERSDRERMNEEKEELKKQVEKLQAQ 500
Cdd:pfam17380 532 EERRRE--------------AEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMRQIVESEKAR 588
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
214-251 |
2.08e-04 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 43.43 E-value: 2.08e-04
10 20 30
....*....|....*....|....*....|....*...
gi 129560475 214 QLRKENEALKAKLDKgLEQRDQAAERLREENLELKKLL 251
Cdd:PRK13922 73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-448 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 196 SKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngNKEGASGRPGSPKMEGTGKK 275
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 276 AVAGQQQASVTAGKVPEVV-------ALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQ 348
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLgsesfsdFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 349 VTDLEAEREQKqrdfdrklllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 428
Cdd:COG3883 163 KAELEAAKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
250 260
....*....|....*....|
gi 129560475 429 IQTPPSSPPTAFGSPEGAGA 448
Cdd:COG3883 225 AAAAAAAAAAAAAAAAAAAA 244
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
282-384 |
2.47e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 282 QASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR 361
Cdd:PRK11448 140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219
|
90 100
....*....|....*....|...
gi 129560475 362 DFDRKlllAKSKIEMEETDKEQL 384
Cdd:PRK11448 220 EITDQ---AAKRLELSEEETRIL 239
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
315-425 |
3.28e-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: 41.03 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 315 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 393
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
|
90 100 110
....*....|....*....|....*....|..
gi 129560475 394 KVKYLQDQLSplTRQREYQEKEIQRLNKALEE 425
Cdd:smart00935 77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
213-487 |
3.59e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 213 EQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAGKVPE 292
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 293 VVALGAAEKKVKMLEQQRSELLEVNKQwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKS 372
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKA--EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 373 KIEMEETDK--EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegagalL 450
Cdd:PTZ00121 1701 AKKAEELKKkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAH------------------L 1762
|
250 260 270
....*....|....*....|....*....|....*..
gi 129560475 451 RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 487
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
201-426 |
3.99e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 201 NEQRTSILQTLcEQLRKENEALKAKLdkglEQRDQAAERLREENlelkKLLMSNGNKEGASGRpgspkmegtgkKAVAGQ 280
Cdd:COG3206 167 ELRREEARKAL-EFLEEQLPELRKEL----EEAEAALEEFRQKN----GLVDLSEEAKLLLQQ-----------LSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 281 QQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEvnkqwDQHFRSMKQQY---EQKITELRQKLAD-------LQKQVT 350
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLaelEAELAELSARYTPnhpdviaLRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 129560475 351 DLEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL---QDQLSPLTRQREYQEKEIQRLNKALEEA 426
Cdd:COG3206 302 ALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
194-538 |
4.71e-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: 43.42 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 194 LASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEgasgrpgspKMEGTG 273
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL---------KKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 274 KKAVAGQQQASVTAGKVPEV-VALGAAEKKVKMLEQQRSeLLEVNKQWDQHFRSMKQQyEQKITELRQKLADLQKQVTDL 352
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETqERINRARKAAPLAAHIKA-VTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 353 EAEREQKQRDFDRKLLLAKSKiEMEETDKEQLTaEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNkalEEALSIQTP 432
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAH-EVATSIREISC-QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ---REQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 433 PSSpptaFGSPEGAGALLRKQELVTQNELLKQQVKIfEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 512
Cdd:TIGR00618 416 TSA----FRDLQGQLAHAKKQQELQQRYAELCAAAI-TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
330 340
....*....|....*....|....*.
gi 129560475 513 DEEKAREALRQQKRKAKASGERYHVE 538
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPA 516
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
308-525 |
5.23e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 308 QQRSELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLADLQKQVTDLEAEREQKQRDfdrkllLAKSKIEMEETDK 381
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 382 EQL-TAEAKELRQKVKYLQDQLspltrqreyqekeiQRLNKALEEA----LSIQTPPSSPPTA---------------FG 441
Cdd:PRK11281 116 ETLsTLSLRQLESRLAQTLDQL--------------QNAQNDLAEYnsqlVSLQTQPERAQAAlyansqrlqqirnllKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 442 SPEGAGALL--RKQELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQAqvTLSNAQ 507
Cdd:PRK11281 182 GKVGGKALRpsQRVLLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQE--AINSKR 254
|
250
....*....|....*...
gi 129560475 508 LKAFkdEEKAREALRQQK 525
Cdd:PRK11281 255 LTLS--EKTVQEAQSQDE 270
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
213-485 |
5.46e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 213 EQLRKENEALKAKLDKGLEQRDQAaERLREENLELKKLLmsngnkegasgrpgspkmegtgkkAVAGQQQASVTAgkvpE 292
Cdd:PRK11281 52 KLLEAEDKLVQQDLEQTLALLDKI-DRQKEETEQLKQQL------------------------AQAPAKLRQAQA----E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 293 VVALGAAEKKVKmleQQRSELLEVnkqwdqhfrsmkQQYEQKITELRQKLADLQKQVTDLEA---------EREQK---- 359
Cdd:PRK11281 103 LEALKDDNDEET---RETLSTLSL------------RQLESRLAQTLDQLQNAQNDLAEYNSqlvslqtqpERAQAalya 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 360 --QRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVKYLQ------DQLSPL-TRQREYQEKEIQRLNK---ALE 424
Cdd:PRK11281 168 nsQRLQQIRNLLKGGKVGgkaLRPSQRVLLQAEQALLNAQNDLQRkslegnTQLQDLlQKQRDYLTARIQRLEHqlqLLQ 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 129560475 425 EALSIQTPPSSPPTA--FGSPEGAGAllrkqelVTQNELLKQqvkifEEDFQRERSDR-----ERMNE 485
Cdd:PRK11281 248 EAINSKRLTLSEKTVqeAQSQDEAAR-------IQANPLVAQ-----ELEINLQLSQRllkatEKLNT 303
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
214-395 |
5.93e-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: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 214 QLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGrpgspkmEGTGKKAVAGQQQASVTAGKvpEV 293
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-------EVEARIKKYEEQLGNVRNNK--EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 294 VALgaaEKKVKMLEQQRSELlevnkqwdqhfrsmkqqyEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK 373
Cdd:COG1579 92 EAL---QKEIESLKRRISDL------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 129560475 374 IEMEETDKEQLTAEAKELRQKV 395
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
332-529 |
7.01e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 332 EQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEEtDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY 411
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEE-KIRELEERIEELKKEIEELEEKVKELKELKEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 412 qEKEIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKifeeDFQRERSDRERMNEEKEELK 491
Cdd:PRK03918 292 -AEEYIKLSEFYEEYLD----------------------ELREIEKRLSRLEEEIN----GIEERIKELEEKEERLEELK 344
|
170 180 190
....*....|....*....|....*....|....*...
gi 129560475 492 KQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAK 529
Cdd:PRK03918 345 KKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLT 382
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
306-427 |
7.10e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 306 LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAeREQKQRDFDRKLLLAKSKIEMEETDKEQLT 385
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPELE 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 386 AEAKELRQKVKYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEEAL 427
Cdd:COG0542 492 KELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEEEL 547
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
315-425 |
8.02e-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: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 315 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQK 394
Cdd:pfam03938 19 AAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKK---------------------EQELQQL 77
|
90 100 110
....*....|....*....|....*....|.
gi 129560475 395 VKYLQDQLSplTRQREYQEKEIQRLNKALEE 425
Cdd:pfam03938 78 QQKAQQELQ--KKQQELLQPIQDKINKAIKE 106
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
197-502 |
8.61e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 197 KVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmSNGNKEgasgrpgSPKMEGTGKKa 276
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI-KSLKKE-------LEKLEELKKK- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 277 vagqqqasvtagkvpevvaLGAAEKKVKMLEQQRSELLevNKQWDQHFRSMKqQYEQKITELR---QKLADLQKQVTDLE 353
Cdd:PRK03918 558 -------------------LAELEKKLDELEEELAELL--KELEELGFESVE-ELEERLKELEpfyNEYLELKDAEKELE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 354 aEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQkvKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqtpp 433
Cdd:PRK03918 616 -REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEK----- 687
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 129560475 434 sspptafgspegagallRKQELVTQNELLKQQVKIFEEdFQRERSDRERMNEEKEELKKQVEKLQAQVT 502
Cdd:PRK03918 688 -----------------RREEIKKTLEKLKEELEEREK-AKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
196-425 |
9.38e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 9.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 196 SKVHKNEQRTSILQTLCEQLRKENEALKAKLdKGLEQR-DQAAERLREENLELKKLlmsngnkEGASGRpgSPKMEGTGK 274
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSK-RKLEEKiRELEERIEELKKEIEEL-------EEKVKE--LKELKEKAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 275 KAVAgqqqasVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEA 354
Cdd:PRK03918 294 EYIK------LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE--------LEEKEERLEELKKKLKELEKRLEELEE 359
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 129560475 355 EREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE 425
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
306-526 |
9.81e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 306 LEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKE 382
Cdd:COG4372 40 LDKLQEELEQLREELEQ-AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQaelAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 383 QLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL----EEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQ 458
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLeslqEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 129560475 459 NELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKR 526
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
302-424 |
1.02e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 302 KVKMLEQQRSELLEVNKQWDQHF----RSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEME 377
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 129560475 378 ETDKEQLTAEAKELRQkvkylqdQLSPLTRQREYQEKEIQRLNKALE 424
Cdd:pfam00038 95 LNLRTSAENDLVGLRK-------DLDEATLARVDLEAKIESLKEELA 134
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
304-426 |
1.02e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 304 KMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllaksKIEMEEtdkEQ 383
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE-----------RIERLE---RE 449
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 129560475 384 LTAEAKELRQKVKylqdqlspltRQREYQ--EKEIQRLNKALEEA 426
Cdd:COG2433 450 LSEARSEERREIR----------KDREISrlDREIERLERELEEE 484
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
298-399 |
1.15e-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: 41.41 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 298 AAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkLLLAKSKiEME 377
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
|
90 100
....*....|....*....|..
gi 129560475 378 ETDKEQLTAEAKELRQKVKYLQ 399
Cdd:cd16269 270 ALLEEGFKEQAELLQEEIRSLK 291
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-501 |
1.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 186 RMALEFNRLASKVHKNEQRTSilqtlCEQLRKENEALKAKLDKGLEQRDQAAERLREEnlELKKllmSNGNKEGASGRPG 265
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKK-----ADEAKKAEEAKKADEAKKAEEKKKADELKKAE--ELKK---AEEKKKAEEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 266 SPKMEGTGKKAVAGQQqasVTAGKVPEVVALGAAEKKVKM-----LEQQRSELLEVNKQwdQHFRSMKQQYEQKITELRQ 340
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKAeeakkAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 341 KLADLQK--QVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQR 418
Cdd:PTZ00121 1648 KAEELKKaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 419 LNKALEEAlsiqtppsspptafgsPEGAGALLRKQELVTQNELLKQQVK--IFEEDFQRERSDRERMNEEKEELKKQVEK 496
Cdd:PTZ00121 1728 NKIKAEEA----------------KKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
....*
gi 129560475 497 LQAQV 501
Cdd:PTZ00121 1792 RRMEV 1796
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
330-565 |
1.49e-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: 41.25 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 330 QYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKskiemeetDKEQLTAEAKELRQKVKYLQDQLSPLTRQR 409
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQ--------DYDGATAQLRAAQAAVKAAQAQLAQAQIDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 410 EYQEkeiqrlnkaleealsiqtppsspPTAfgsPEGAGAllrKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEE 489
Cdd:pfam00529 127 ARRR-----------------------VLA---PIGGIS---RESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 129560475 490 LKKQVEKLQAQVTLSNAQLKAfkDEEKAREALRQQKRKAKASGERYHVEPHPEhlcGAypYAYPPMPAM--VPHHGFE 565
Cdd:pfam00529 178 NQAEVRSELSGAQLQIAEAEA--ELKLAKLDLERTEIRAPVDGTVAFLSVTVD---GG--TVSAGLRLMfvVPEDNLL 248
|
|
| Speriolin_N |
pfam15058 |
Speriolin N terminus; This family represents the N-terminus of the sperm centrosome protein ... |
14-149 |
1.64e-03 |
|
Speriolin N terminus; This family represents the N-terminus of the sperm centrosome protein speriolin.
Pssm-ID: 434426 [Multi-domain] Cd Length: 196 Bit Score: 40.03 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 14 GSVPSGEASAAFERLVKENSRLKEKMqgikmlgELLEESQMEATRLRQKAEELV--KDNELLPPPSPSLGSFDPLAELTG 91
Cdd:pfam15058 3 LLTPYEGLRHQIERLVRENEELKKQV-------RLLRENQELKRALGEACAGRCgrQQRGVFLPPVPAYASEPCSPGPGG 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 129560475 92 KD-SNVTASPTAPAcPSDKPAPVQKPPSSGTSSEFEVVTPEEQNSPESSSHANAMALGP 149
Cdd:pfam15058 76 RAlAPLAGMPDTPQ-QSAEEGSLVDPLTSSLEDLLSGHAPLSQEDCQACQTTDPVAAPP 133
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-425 |
1.79e-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: 41.58 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 165 ETTLSVCAEEPDHGQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREEN 244
Cdd:TIGR02168 730 ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 245 LELKKLLMSNGNKEGASGRPgSPKMEGTGKKAVAGQQQASVTAGKVPEVVAlgAAEKKVKMLEQQRSELLEVNKQWDQHF 324
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAA--EIEELEELIEELESELEALLNERASLE 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 325 RSMK-------------QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKL--LLAKSKIEMEETDKEQ------ 383
Cdd:TIGR02168 887 EALAllrseleelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEAEALEnkiedd 966
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 129560475 384 ----------------------LTA--EAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE 425
Cdd:TIGR02168 967 eeearrrlkrlenkikelgpvnLAAieEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
384-504 |
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: 40.90 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 384 LTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQTPPSSPPTAFgspegAGALLRKQELVTQNELL 462
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQL-----ATERSARREAEAELERL 119
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 129560475 463 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQVTLS 504
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQLTSK 158
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
197-518 |
1.90e-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: 41.25 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 197 KVHKNEQRTSILqtLCEQLRKENEaLKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMegtgkka 276
Cdd:pfam05483 234 EINDKEKQVSLL--LIQITEKENK-MKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKM------- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 277 vagQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQH-----------------FRSMKQQYEQKITELR 339
Cdd:pfam05483 304 ---SLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHsfvvtefeattcsleelLRTEQQRLEKNEDQLK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 340 QKLADLQKQVTDLEAE---REQKQRDFD--RKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL-----------QDQLS 403
Cdd:pfam05483 381 IITMELQKKSSELEEMtkfKNNKEVELEelKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarekeihdlEIQLT 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 404 PLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFgspegagaLLRKQELVTQNELLKQQVKIFEEDFQRERSDRERM 483
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKL--------LLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
330 340 350
....*....|....*....|....*....|....*
gi 129560475 484 NEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAR 518
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK 567
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
295-410 |
2.42e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.81 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 295 ALGAAEKKVKMLEQ----QRSELLEVNKQWDQHfRSMKQQYEQKITELRQKLADLQKQVTD-LEAEREQKQRDFDRKLLL 369
Cdd:COG1842 17 LLDKAEDPEKMLDQairdMEEDLVEARQALAQV-IANQKRLERQLEELEAEAEKWEEKARLaLEKGREDLAREALERKAE 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 129560475 370 AKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQRE 410
Cdd:COG1842 96 LEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKD 136
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
184-358 |
2.63e-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: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 184 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGR 263
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 264 PGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNkqwdqhFRSMkQQYEqkitELRQKLA 343
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVN------LLAI-EEYE----ELEERYD 798
|
170
....*....|....*
gi 129560475 344 DLQKQVTDLEAEREQ 358
Cdd:COG1196 799 FLSEQREDLEEARET 813
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
301-497 |
2.63e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 301 KKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQK------ITELRQKLADLQKQ----VTDLEAERE------------- 357
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRqqteVLSPEEEKElvekikelekele 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 358 --QKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAlsiqtppss 435
Cdd:COG1340 151 kaKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA--------- 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 129560475 436 pptafgspEGAGALLRKQELVTQNELLKQQVKIFEedfQRERSDRERMNEEKEELKKQVEKL 497
Cdd:COG1340 222 --------QEKADELHEEIIELQKELRELRKELKK---LRKKQRALKREKEKEELEEKAEEI 272
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
295-421 |
2.66e-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: 40.48 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 295 ALGAAEKKVKMLEQQRSELL-EVNKQwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR-KLLLAKS 372
Cdd:pfam00529 59 ALDSAEAQLAKAQAQVARLQaELDRL--QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrRVLAPIG 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 129560475 373 KIEMEETDKEQltAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 421
Cdd:pfam00529 137 GISRESLVTAG--ALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR 183
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
327-535 |
2.80e-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: 41.11 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 327 MKQQYEQKITELRQKLADLQKQVTDLEAEREQkqrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL-------- 398
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLklneerid 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 399 ---------QDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptAFGSPEGAGALLRKQELVTQNELLKQQVKIF 469
Cdd:pfam02463 241 llqellrdeQEEIESSKQEIEKEEEKLAQVLKENKEEEKEK--------KLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 129560475 470 EEdfQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERY 535
Cdd:pfam02463 313 EE--KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
334-523 |
2.82e-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: 39.50 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 334 KITELRQKLADLQKQVTDLEAErEQKQRDFDRKLLLAKSKIEMEETDKEQL----TAEAKELRQKVKYLQDQLSPLTRQR 409
Cdd:pfam15619 12 KIKELQNELAELQSKLEELRKE-NRLLKRLQKRQEKALGKYEGTESELPQLiarhNEEVRVLRERLRRLQEKERDLERKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 410 EYQEKEIQRLNKALE--EALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQR-----ERSDRER 482
Cdd:pfam15619 91 KEKEAELLRLRDQLKrlEKLSEDK----------------NLAEREELQKKLEQLEAKLEDKDEKIQDlerklELENKSF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 129560475 483 MNEEKEELKKQVEklqAQVTLSNAQLKAFKDEEKAREALRQ 523
Cdd:pfam15619 155 RRQLAAEKKKHKE---AQEEVKILQEEIERLQQKLKEKERE 192
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
307-528 |
2.92e-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: 40.98 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 307 EQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKL----ADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEME----- 377
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpswqs 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 378 ------------ETDKEQLTAEAKELRQKVKY-LQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPE 444
Cdd:pfam12128 355 elenleerlkalTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLE 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 445 -GAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDR--ERMNEEKEELKKQVEKLQaqvtlsNAQLKAFKDEEKAREAL 521
Cdd:pfam12128 435 fNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDEriERAREEQEAANAEVERLQ------SELRQARKRRDQASEAL 508
|
....*..
gi 129560475 522 RQQKRKA 528
Cdd:pfam12128 509 RQASRRL 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
186-523 |
2.94e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 186 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKglEQRDQAAERLREENLELKKLLMSNG---NKEGASG 262
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ--LENELEAAALEERLKEARLLLLIAAallALLGLGG 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 263 RPGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSelLEvNKQWDQHFRSMKQQYEQKITELR--- 339
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE--LE-EEELEELLAALGLPPDLSPEELLell 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 340 ---QKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEET--DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ-- 412
Cdd:COG4717 344 driEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQAEEYQELKEELEELEEQLEELLGELEELle 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 413 -------EKEIQRLNKALEEalsiqtppsspptafgspegagalLRKQELVTQNEL--LKQQVKIFEED--FQRERSDRE 481
Cdd:COG4717 424 aldeeelEEELEELEEELEE------------------------LEEELEELREELaeLEAELEQLEEDgeLAELLQELE 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 129560475 482 RMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE------EKAREALRQ 523
Cdd:COG4717 480 ELKAELRELAEEWAALKLALELLEEAREEYREErlppvlERASEYFSR 527
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
306-540 |
3.44e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 306 LEQQRSELLEVNKQWDQHFRSMKQ------QYEQKITELRQKLADLQKQVTDLEAER---EQKQRDFDRKLLLAKSKIEM 376
Cdd:COG4372 68 LEQARSELEQLEEELEELNEQLQAaqaelaQAQEELESLQEEAEELQEELEELQKERqdlEQQRKQLEAQIAELQSEIAE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 377 EETDKEQLTAEAKELRQKVKYLQDQLSPLTRQrEYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSP----EGAGALLRK 452
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEA-EAEQALDELLKEANRNAEKEEELAEAEKLIESLPrelaEELLEAKDS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 453 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASG 532
Cdd:COG4372 227 LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAA 306
|
....*...
gi 129560475 533 ERYHVEPH 540
Cdd:COG4372 307 LSLIGALE 314
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
295-419 |
3.48e-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: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 295 ALGAAEKKVKMLEQQRSELlevnkqwDQHFRSMKQQYEQ----KITELRQKLADLQKQVtdleAEREQKQRDFDRKLLLA 370
Cdd:COG4913 303 ELARLEAELERLEARLDAL-------REELDELEAQIRGnggdRLEQLEREIERLEREL----EERERRRARLEALLAAL 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 371 KSKIEMEETD-----------KEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL 419
Cdd:COG4913 372 GLPLPASAEEfaalraeaaalLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
306-427 |
4.29e-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: 39.96 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 306 LEQQRSELLEVNKQWD----QHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLL-------AKSKI 374
Cdd:pfam14643 243 VEEWWASLEALNEQLDqyhdQCMTKLRAEYEEVWQECLARVQKLKQELLDYKVCSEEEAEALVNEEFLplvgklqRDAED 322
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 129560475 375 EMEETDK--EQLtaeAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAL 427
Cdd:pfam14643 323 ELEKLDKflEEL---AKQTEAQSEDLFKFFREAAQLWDVHQTELAKQELELEKKL 374
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
310-513 |
4.76e-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: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 310 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKQVTDLEAEREQkQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 389
Cdd:COG3096 490 RSQAWQTARELLRRYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERL-LEEFCQRIGQQLDAAEELEELLAELEAQLE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 390 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIF 469
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQD----------------ALERLREQSGEALADSQEVTAA 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 129560475 470 -EEDFQRERS---DRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 513
Cdd:COG3096 632 mQQLLEREREatvERDELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
364-510 |
4.79e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 39.04 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 364 DRKLLLAKSKIEMEETDKE------QLTAEAKELRQKVKYLQDQlspltrQREYQEKEIQRLNKAlEEALSIQtppsspp 437
Cdd:COG1842 23 DPEKMLDQAIRDMEEDLVEarqalaQVIANQKRLERQLEELEAE------AEKWEEKARLALEKG-REDLARE------- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 129560475 438 tafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKA 510
Cdd:COG1842 89 ----------ALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKV 151
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
288-414 |
5.09e-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: 39.64 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 288 GKVPE-VVALGAAEKKVKML-EQQRSelleVNKQwdqHFRSMkQQYEQKITELRQKLADLQKQVTDLEAEREQKqRDFDR 365
Cdd:smart00435 245 GNVAEkILAYNRANREVAILcNHQRT----VSKT---HEKSM-EKLQEKIKALKYQLKRLKKMILLFEMISDLK-RKLKS 315
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 129560475 366 KLLLAKSKIEME-ETDKEQLTAEAKELRQkVKYLQDQLSPLTRQREYQEK 414
Cdd:smart00435 316 KFERDNEKLDAEvKEKKKEKKKEEKKKKQ-IERLEERIEKLEVQATDKEE 364
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
306-403 |
6.78e-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: 36.78 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 306 LEQQRSELLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKE 382
Cdd:pfam13863 1 LLEKKREMFLVQLALDA----KREEIERLEELLKQREEELEKKEQELKEDLIKFDkflKENDAKRRRALKKAEEETKLKK 76
|
90 100
....*....|....*....|.
gi 129560475 383 QLTAEAKELRQKVKYLQDQLS 403
Cdd:pfam13863 77 EKEKEIKKLTAQIEELKSEIS 97
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
333-538 |
7.35e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 333 QKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllakskiemEETDKEQLTAEAKELRQKVKYLQDQLS--PLTRQRE 410
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE---------------LEEELEELEAELEELREELEKLEKLLQllPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 411 YQEKEIQRLNKALEEALSiqtppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRErmNEEKEEL 490
Cdd:COG4717 136 ALEAELAELPERLEELEE-------------------RLEELRELEEELEELEAELAELQEELEELLEQLS--LATEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 129560475 491 KKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERYHVE 538
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
298-524 |
7.43e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 298 AAEKKVKMLEQQRSELLEVNKQWDQHFRSMK--QQYEQKITELRQKLADLQKQvtdLEAEREqkqrdfdrkllLAKSKIE 375
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKVQEHQMELKylKQYKEKACEIRDQITSKEAQ---LESSRE-----------IVKSYEN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 376 MEETDKEQLTaEAKELRQKVKYLQDQLSPLtrqrEYQEKEIQRLNKALEEALSiqtppsspPTAFGSPEgagallrkqEL 455
Cdd:TIGR00606 246 ELDPLKNRLK-EIEHNLSKIMKLDNEIKAL----KSRKKQMEKDNSELELKME--------KVFQGTDE---------QL 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 129560475 456 VTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKqvEKLQAQVTLSNAQLKAFKDEE--KAREALRQQ 524
Cdd:TIGR00606 304 NDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQ--EKTELLVEQGRLQLQADRHQEhiRARDSLIQS 372
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
192-527 |
7.60e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 192 NRLASKVHKNEQRTSILQTLCEQLRKENE--ALKAKLDKGLEQRDQAAERLREEnLELKKLLMSNGNKEGASGRPGSPKM 269
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEElrAQEAVLEETQERINRARKAAPLA-AHIKAVTQIEQQAQRIHTELQSKMR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 270 EGTG---KKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRS--ELLEVNKQWDQHFRSMKQQYE---QKITELRQK 341
Cdd:TIGR00618 322 SRAKllmKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKTtltQKLQSLCKE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 342 LADLQKQVTDLEAeREQKQRDFDRKLLLAKSKIEMEETDKEQLTA--------------EAKELRQKVKYLQDQLSPLT- 406
Cdd:TIGR00618 402 LDILQREQATIDT-RTSAFRDLQGQLAHAKKQQELQQRYAELCAAaitctaqceklekiHLQESAQSLKEREQQLQTKEq 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 407 ---RQREYQEKEIQRLNKALEE---------------ALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKI 468
Cdd:TIGR00618 481 ihlQETRKKAVVLARLLELQEEpcplcgscihpnparQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 469 FEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKA-FKDEEKAREALRQQKRK 527
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKlSEAEDMLACEQHALLRK 620
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
382-521 |
7.87e-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: 38.89 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 382 EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqtppsspptafgspeGAGALLRKQELVTQNEL 461
Cdd:cd22656 124 DDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLT----------------DEGGAIARKEIKDLQKE 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 129560475 462 LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE-EKAREAL 521
Cdd:cd22656 188 LEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALiGPAIPAL 248
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
332-540 |
7.94e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 332 EQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY 411
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQ----LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 412 QEKEIQRLNKALEEALSIQtppSSPPTAFGSPEGagallRKQELVTQNELLKQQVKIFEEDFQRERSDrermnEEKEELK 491
Cdd:COG4372 120 LQKERQDLEQQRKQLEAQI---AELQSEIAEREE-----ELKELEEQLESLQEELAALEQELQALSEA-----EAEQALD 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 129560475 492 KQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERYHVEPH 540
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
295-428 |
8.44e-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: 38.37 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 295 ALGAAEKKVKMLEQQ----RSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADLQKQVTDLEAERE----QKQRDFDRK 366
Cdd:COG1579 25 RLKELPAELAELEDElaalEARLEAAKTELED-LEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealQKEIESLKR 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 129560475 367 LLLAKSKIEMEETDK-EQLTAEAKELRQKVKYLQDQLSPLTRQRE----YQEKEIQRLNKALEEALS 428
Cdd:COG1579 104 RISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAA 170
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
300-500 |
8.50e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 300 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQyeqkITELRQKLADLQKQVTDLEAEREQKQrdfDRKLLLAKSKIEMEET 379
Cdd:pfam01576 137 EEDILLLEDQNSKLSKERKLLEERISEFTSN----LAEEEEKAKSLSKLKNKHEAMISDLE---ERLKKEEKGRQELEKA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 380 dKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspEGAgallRKQELVTQN 459
Cdd:pfam01576 210 -KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEE------------------ETA----QKNNALKKI 266
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 129560475 460 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 500
Cdd:pfam01576 267 RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTE 307
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
283-539 |
8.84e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 283 ASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDqhfrSMKQQYEQ---KITELRQKLADLQKQVTDLEAEREQK 359
Cdd:COG3883 2 LALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELD----ALQAELEElneEYNELQAELEALQAEIDKLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 360 QRDFDRKlllakskiemeetdKEQLTAEAKELRQK---VKYLQ-----DQLSPLTRQREYQEKEIQRLNKALEEALSiqt 431
Cdd:COG3883 78 EAEIEER--------------REELGERARALYRSggsVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKA--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 129560475 432 ppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAF 511
Cdd:COG3883 141 -------------------DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
250 260
....*....|....*....|....*...
gi 129560475 512 KDEEKAREALRQQKRKAKASGERYHVEP 539
Cdd:COG3883 202 EAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| |
