|
Name |
Accession |
Description |
Interval |
E-value |
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
348-549 |
1.35e-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: 63.63 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 348 QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQ 427
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 428 EKEIQRLNKALEEAL--SIQASPSSPPAAFGSPEGVGGHLR----------------------KQELVTQNELLKQQVKI 483
Cdd:COG4942 96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRrlqylkylaparreqaeelradLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564371823 484 FEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRKAKASGER 549
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
313-545 |
1.95e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 313 TAEKKVKLleQQRMELLEVNKQW--DQHFRTMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDR---------- 380
Cdd:COG1196 211 KAERYREL--KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 381 KLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspeg 460
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 461 vgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQK 540
Cdd:COG1196 359 ----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
....*
gi 564371823 541 RKAKA 545
Cdd:COG1196 435 EEEEE 439
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-553 |
1.16e-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: 61.61 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 314 AEKKVKLLEQQRMELLEVNKQWDQHFRTMKQQYEQK---ITELRQKLVDLQKQVTELEAEREQ---KQRDFDRKLLLAKS 387
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeLEELSRQISALRKDLARLEAEVEQleeRIAQLSKELTELEA 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 388 KIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEaLSIqaspssppAAFGSPEGVGGHL-R 466
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNE--------EAANLRERLESLErR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 467 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEE-----------EKAKEA 535
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEleelseelrelESKRSE 912
|
250
....*....|....*...
gi 564371823 536 LKQQKRKAKASGERYHVE 553
Cdd:TIGR02168 913 LRRELEELREKLAQLELR 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
314-544 |
4.34e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 314 AEKKVKLLEQQRMEL-LEVNKQWDQHFRTMKQ--QYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdRKLLLAKSKIE 390
Cdd:COG1196 265 LEAELEELRLELEELeLELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELE----EELEELEEELE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 391 MEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEALSIQAspssppaafgspegvgghlrkQEL 470
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA---------------------ELA 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564371823 471 VTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRKAK 544
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
347-545 |
9.62e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 347 EQKITELRQKLVDLQKQVTELEAEREQ-------KQRDFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSP 419
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 420 LMRQREYQEKEIQRLNKALEEALSiqaspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMN 499
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564371823 500 EEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRKAKA 545
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
228-562 |
3.36e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 228 EQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLLMnsnckeglcgqpsspKTEGAGKKGVAGQQQASMTASKVPE 307
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRL---------------ELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 308 AgafgtaEKKVKLLEQQRMELLEVNKQWDQhfrtMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQ---RDFDRKLLL 384
Cdd:COG1196 300 L------EQDIARLEERRRELEERLEELEE----ELAELEEELEELEEELEELEEELEEAEEELEEAEaelAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 385 AKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEALSiqaspssppaafgspegvggh 464
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE--------------------- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 465 lRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRKAK 544
Cdd:COG1196 429 -ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
330
....*....|....*...
gi 564371823 545 ASGERYHVEPHPEHLCGA 562
Cdd:COG1196 508 EGVKAALLLAGLRGLAGA 525
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
343-534 |
6.72e-08 |
|
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: 55.80 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 343 KQQYEQKITELRQ---KLVDLQKQVTELEAERE----QKQRDFDRKLllaKSKIEMEETDKEQLTTEAKELRQKVKYLQD 415
Cdd:TIGR04523 266 KKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL---KSELKNQEKKLEEIQNQISQNNKIISQLNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 416 QLSPLMRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspEGVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDR 495
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKK--------ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQI 414
|
170 180 190
....*....|....*....|....*....|....*....
gi 564371823 496 ERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKE 534
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-543 |
8.37e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 350 ITELRQKLVDLQKQVT------ELEAEREQKQ--------RDFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQD 415
Cdd:TIGR02168 195 LNELERQLKSLERQAEkaerykELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 416 QLSPLmrqreyqEKEIQRLNKALEEALSIQASPSSppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDR 495
Cdd:TIGR02168 275 EVSEL-------EEEIEELQKELYALANEISRLEQ---------------QKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 564371823 496 ERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRKA 543
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
344-516 |
1.62e-07 |
|
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: 52.62 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 344 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQ 423
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 424 REYQ--EKEIQRLNKAL----EEALSIQAspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRE- 496
Cdd:COG1579 89 KEYEalQKEIESLKRRIsdleDEILELME-------------------RIEELEEELAELEAELAELEAELEEKKAELDe 149
|
170 180
....*....|....*....|...
gi 564371823 497 ---RMNEEKEELKKQVEKLQAQV 516
Cdd:COG1579 150 elaELEAELEELEAEREELAAKI 172
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
467-515 |
1.76e-07 |
|
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: 49.27 E-value: 1.76e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 564371823 467 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 515
Cdd:cd09803 34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
207-513 |
4.46e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 207 NRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLLMNSNCKE----GLCGQPSSP 282
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqieQLKEELKAL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 283 KTEGAGKKGVAGQQQasmtaskvpeaGAFGTAEKKVKLLEQQRMELLEVNKQWDQHFRTMKQQ---YEQKITELRQKLVD 359
Cdd:TIGR02168 802 REALDELRAELTLLN-----------EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDiesLAAEIEELEELIEE 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 360 LQKQVTELEAEREQKQRDfdrkLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALE 439
Cdd:TIGR02168 871 LESELEALLNERASLEEA----LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 440 EALSI--QASPSSPPAAFGSPEGVGGHLRKqelvtqnelLKQQVKIF-------EEDFQRERSDRERMNEEKEELKKQVE 510
Cdd:TIGR02168 947 EEYSLtlEEAEALENKIEDDEEEARRRLKR---------LENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
...
gi 564371823 511 KLQ 513
Cdd:TIGR02168 1018 TLE 1020
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
205-545 |
5.72e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 205 EFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKSLEQRDQAAERLREEntELKRLLMNSNCKEGLCGQPSSPKT 284
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 285 EGAGKKGVAGQQQASMTASKVPEAGAFGTAEKKVKLLEQQRMELLEVNKQWDQhfrtMKQQYEQKITELRQKLVDLQKQV 364
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE----KKKEEAKKKADAAKKKAEEKKKA 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 365 TELE--AEREQKQRDFDRKLLLAKSKIEmEETDKEQLTTEAKELRQKVKylQDQLSPLMRQREYQEKEIQRLNKALEEAL 442
Cdd:PTZ00121 1394 DEAKkkAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 443 SIQASPSSPPAAFGSPEG---VGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK---EELKKQVEKLQAQV 516
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADE 1550
|
330 340
....*....|....*....|....*....
gi 564371823 517 TLTTAQLRTLKEEEKAKEALKQQKRKAKA 545
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
209-553 |
7.42e-07 |
|
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: 52.66 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 209 LASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLLMNSNCKEglcgqpsspKTEGAG 288
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQL---------KKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 289 KKGVAGQQQASMTASKVPEAG-AFGTAEKKVKLLEQQRmELLEVNKQWDQHFRTMKQQyEQKITELRQKLVDLQKQVTEL 367
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETQeRINRARKAAPLAAHIK-AVTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 368 EAEREQKQRDFDRKLLLAKSKiEMEETDKEQLTtEAKELRQKVKYLQDQLsplmrqrEYQEKEIQRLNKALEEALSIQAS 447
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAH-EVATSIREISC-QQHTLTQHIHTLQQQK-------TTLTQKLQSLCKELDILQREQAT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 448 PSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIfEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLK 527
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI-TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
330 340
....*....|....*....|....*.
gi 564371823 528 EEEKAKEALKQQKRKAKASGERYHVE 553
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPA 516
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
174-531 |
8.41e-07 |
|
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: 52.43 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 174 LHLQRLETTLSVCAEEPDhsqlfthlGRMALEFNRLASKVHKNEQRTSI---LQTLCEQLRQENEALKAK---------- 240
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQ--------GQMERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKVVEELTAKkmtlessert 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 241 ---LDKSLEQRDQAAERLREENT-----------ELKRLLMNSNCKEGLCGQPSSPKTEGAGKKGVAG---QQQASMT-- 301
Cdd:pfam15921 498 vsdLTASLQEKERAIEATNAEITklrsrvdlklqELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEilrQQIENMTql 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 302 -ASKVPEAGAFGTAEKKV-KLLEQQRMELlevnkqwdQHFRTMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRdfd 379
Cdd:pfam15921 578 vGQHGRTAGAMQVEKAQLeKEINDRRLEL--------QEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR--- 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 380 rklllAKSKIEMEetdKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEAL-SIQASPSSPPAAFGSP 458
Cdd:pfam15921 647 -----AVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLkSAQSELEQTRNTLKSM 718
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 459 EGVGGHLRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEE 529
Cdd:pfam15921 719 EGSDGHAMKVAMGMQKQItakrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ 798
|
..
gi 564371823 530 EK 531
Cdd:pfam15921 799 ER 800
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
341-549 |
1.22e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 341 TMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPL 420
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 421 MRqreyqekeiqrlnkaleeALSIQASPSSPPAAFGSPEGVGGHLRKQELVT-----QNELLKQQ---VKIFEEDFQRER 492
Cdd:COG3883 92 AR------------------ALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkiadaDADLLEELkadKAELEAKKAELE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 564371823 493 SDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRKAKASGER 549
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
344-553 |
1.26e-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: 51.98 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 344 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllakskiemeETDKEQLTTEAKELRQKVKYLQDQLSPLMRQ 423
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEEL-----------EEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 424 REYQEKEIQRLNKALEEALSIQASPSSppaafgspEGVGGHLRKQELVTQNELLKQQVKIFEEDFQrerSDRERMNEEKE 503
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEE--------RLEEAEEELAEAEAEIEELEAQIEQLKEELK---ALREALDELRA 810
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564371823 504 ELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRKAKASGERYHVE 553
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
347-545 |
1.64e-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: 51.61 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 347 EQKITELRQKLVDLQKQVTELEAEREQKQRDfdRKLLLAKSKIEMEEtdkeqLTTEAKELRQKVKYLQDQLSPLMRQREY 426
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYE-----LLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 427 QEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFE---EDFQRER----SDRERMN 499
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErelEDAEERLakleAEIDKLL 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564371823 500 EEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRKAKA 545
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
199-509 |
2.05e-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: 51.22 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 199 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLD---KSLEQRDQAAERLREENTELKRLLMNSNCKEgL 275
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSHSRIPE-I 796
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 276 CGQPSSPKTEGAGKKGVAGQQQASMTASKVPEAgafgTAEKKVKLLEQQRMEL---LEVNKQWDQHFRTMKQQYEQKITE 352
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKE----YLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 353 LRQKLVDLQKQVTELEAEREqkqrDFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLS---PLMRQREYQEK 429
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERD----ELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEEIPE 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 430 EIQRLNKALEEALSIQASPSS-PPAAFGSPEGVgghlrKQELVTQNELLKQQVKIFEEdfqreRSDRERMNEEKEELKKQ 508
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRAlEPVNMLAIQEY-----EEVLKRLDELKEKRAKLEEE-----RKAILERIEEYEKKKRE 1018
|
.
gi 564371823 509 V 509
Cdd:TIGR02169 1019 V 1019
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
208-549 |
2.21e-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: 51.13 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 208 RLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLL-MNSNCKEGLCGQPSSPKTEG 286
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLkLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 287 AGKKGVAGQQQASMTASKVpeagafgTAEKKVKLLEQQRMELLEVNKQWDQHfRTMKQQYEQKITELRQKLVDLQKQVTE 366
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLK-------ENKEEEKEKKLQEEELKLLAKEEEEL-KSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 367 LEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEALSIQA 446
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 447 SPSSPpaafgspegvgGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTL 526
Cdd:pfam02463 406 EAQLL-----------LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
330 340
....*....|....*....|...
gi 564371823 527 KEEEKAKEALKQQKRKAKASGER 549
Cdd:pfam02463 475 KETQLVKLQEQLELLLSRQKLEE 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
215-528 |
2.94e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 215 KNEQRTSILQTLCEQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLLMNsnckeglcgqpsspktegagkkgvag 294
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD-------------------------- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 295 qqqasmtaskvpeagaFGTAEKKVKLLEQQRMELLEVNKQwdqhfrtmkqqYEQKITELRQKLVDLQKQVTELEAEREQK 374
Cdd:TIGR02168 735 ----------------LARLEAEVEQLEERIAQLSKELTE-----------LEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 375 QRDFDRklllAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEALSIQASPSSPPAA 454
Cdd:TIGR02168 788 EAQIEQ----LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 455 FGSP-----EGVGGHL-RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKE 528
Cdd:TIGR02168 864 LEELieeleSELEALLnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE 943
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
325-551 |
3.95e-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: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 325 RMELLEVnKQWDQHFRTMKQQYEQkITELRQKLVDLQKQVTELE------AEREQKQRDFD---------------RKLL 383
Cdd:COG4913 214 REYMLEE-PDTFEAADALVEHFDD-LERAHEALEDAREQIELLEpirelaERYAAARERLAeleylraalrlwfaqRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 384 LAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQ--------EKEIQRLNKALEEalsiqaspssppaaf 455
Cdd:COG4913 292 LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEE--------------- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 456 gspegvgghlRKQELVTQNELLKQ---QVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKA 532
Cdd:COG4913 357 ----------RERRRARLEALLAAlglPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
250 260
....*....|....*....|
gi 564371823 533 KEA-LKQQKRKAKASGERYH 551
Cdd:COG4913 424 LEAeIASLERRKSNIPARLL 443
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-443 |
5.45e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 205 EFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLlmnsnckeglcgqpsspkt 284
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL------------------- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 285 egAGKKGVAGQQQASMTASKVPEAGAFGTAEKKVKLLEQQRMELLEVNKQWDQHFRTMKQQY---EQKITELRQKLVDLQ 361
Cdd:COG1196 329 --EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 362 KQVTELE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKAL 438
Cdd:COG1196 407 EAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
....*
gi 564371823 439 EEALS 443
Cdd:COG1196 487 AEAAA 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-549 |
8.32e-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: 49.30 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 184 SVCAEEPDHSQLFTH-LGRMALEFNRLASKVHKNEQRTSILQtlceQLRQENEALKAKLDKSLEQRDQAAERLREENTEL 262
Cdd:TIGR02169 667 LFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELS----QELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 263 KRLLmnSNCKEGLcgqpSSPKTEGAGKKGVAGQQQASMtaskvpeagafgtAEKKVKLLEQQRMELLEVNKQWDQHFRTM 342
Cdd:TIGR02169 743 EEDL--SSLEQEI----ENVKSELKELEARIEELEEDL-------------HKLEEALNDLEARLSHSRIPEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 343 KQQY---EQKITELRQKLVDLQKQVTELEAEREQKQ---RDFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQ 416
Cdd:TIGR02169 804 EEEVsriEARLREIEQKLNRLTLEKEYLEKEIQELQeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 417 LSPLMRQREYQEKEIQRLNKALEEaLSIQASPSsppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRE 496
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEE-LEAQIEKK--------------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 564371823 497 RMNEEkEELKKQVEKLQAQV-TLTTAQLRTLKEEEKAKEALKQ-QKRKAKASGER 549
Cdd:TIGR02169 949 EELSL-EDVQAELQRVEEEIrALEPVNMLAIQEYEEVLKRLDElKEKRAKLEEER 1002
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
475-517 |
1.17e-05 |
|
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: 44.20 E-value: 1.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 564371823 475 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 517
Cdd:pfam16516 55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
201-553 |
1.95e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 201 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRQENEALK-AKLDKSLEQRDQAAERLREENTELKRLLMNSNCKEGLCGQP 279
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 280 SSPKTEGAGKKGVAGQQQASMTASKVPEAGAFGTAEK-----KVKLLEQQRMEllEVNKQWDQHFRTMKQQYEQKITELR 354
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 355 QKLVDLQKQVTELEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEI 431
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 432 QRLNKALEEalsiqaspssppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEK 511
Cdd:PTZ00121 1678 EEAKKAEED-----------------------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 564371823 512 LQAQVTLTTAQLRTLKEEEKAKEALKQQKRKAKASGERYHVE 553
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
336-550 |
4.56e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 336 DQHFRTMKQQYEQKITELRQKLVDLQKQVTELEAEREQ-KQR----DFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKV 410
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 411 KYLQDQL-------SPLMRQREYQE--KEIQRLNKALEEaLSIQASPSSPPAafgspegvgghlrkQELVTQNELLKQQV 481
Cdd:COG3206 243 AALRAQLgsgpdalPELLQSPVIQQlrAQLAELEAELAE-LSARYTPNHPDV--------------IALRAQIAALRAQL 307
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564371823 482 KifeedfQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKakeALKQQKRKAKASGERY 550
Cdd:COG3206 308 Q------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA---ELRRLEREVEVARELY 367
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
315-548 |
4.81e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 315 EKKVKLLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQklvdlqkqvtELEAEREQKQRDFDRKLLLAKSKIEMEET 394
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 395 DKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQEL---- 470
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 471 -----------VTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKkqveKLQAQVTLTTAQLRTLKEEEKAKEALKQQ 539
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR----RIQEQMRKATEERSRLEAMEREREMMRQI 581
|
....*....
gi 564371823 540 KRKAKASGE 548
Cdd:pfam17380 582 VESEKARAE 590
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
315-539 |
5.60e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 315 EKKVKLLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQKLVDLqKQVTELEAEREQKQRDFDRKLLLAKSKIEMEET 394
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 395 DKEQLTTEAKELRQKVKYLQDQLSplmrqREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvggHLRKQELVTQN 474
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEEL----------------------KQTQKSLKKKQ 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564371823 475 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEeekAKEALKQQ 539
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS---KKNKLKQE 646
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
315-546 |
6.33e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 315 EKKVKLLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQKLVDLQKQVTELE---AEREQKQRDFDRKLLLAKSKIEM 391
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLErsiAEKERELEDAEERLAKLEAEIDK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 392 EETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEALSIQASpssppaafgspegvgghlRKQEL- 470
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------------YREKLe 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564371823 471 VTQNEL--LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAqvTLTTAQLRTLKEEEKAKEaLKQQKRKAKAS 546
Cdd:TIGR02169 396 KLKREIneLKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEE--EKEDKALEIKKQEWKLEQ-LAADLSKYEQE 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
321-545 |
8.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 321 LEQQRMELLEVNKQWDQhfrtmkqqYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLT 400
Cdd:COG4717 134 LEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 401 TEAKELRQKVKYLQDQLSPLMRQREY--QEKEIQRLNKALEEALSIQASPSS-------PPAAFGSPEGVGGH--LRKQE 469
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAAllallglGGSLLSLILTIAGVlfLVLGL 285
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564371823 470 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRKAKA 545
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
320-529 |
8.43e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 320 LLEQQRMELLEVNKQWDQhfrtmKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKE 397
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-----KEEKDlhERLNGLESELAELDEEIERYEEQREQARETRDE----ADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 398 QLTTEAKELRQkvkyLQDQLSPLMRQREYQEKEIQRLNKALEEaLSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELL 477
Cdd:PRK02224 252 ELETLEAEIED----LRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564371823 478 KQ-------QVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEE 529
Cdd:PRK02224 327 RDrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
344-544 |
8.52e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 344 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSK-------IEMEETDKEQLTTEAKELRQ---KVKYL 413
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlnqlKDEQNKIKKQLSEKQKELEQnnkKIKEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 414 QDQLSPLmrqreyqEKEIQRLNKALEEALSiqaspssppaafgspEGVGGHLRKQE---LVTQNEL---------LKQQV 481
Cdd:TIGR04523 287 EKQLNQL-------KSEISDLNNQKEQDWN---------------KELKSELKNQEkklEEIQNQIsqnnkiisqLNEQI 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564371823 482 KIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQvtlTTAQLRTLKEEEKAKEALKQQKRKAK 544
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEIKNLESQINDLESKIQNQE 404
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
229-266 |
1.11e-04 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 44.58 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|....*...
gi 564371823 229 QLRQENEALKAKLDKsLEQRDQAAERLREENTELKRLL 266
Cdd:PRK13922 73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
315-537 |
1.11e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.40 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 315 EKKVKLLEQQRMELLEVNKQWDQHFRTMKQQY---EQKITELRQKLVDLQKQVTELEAE---------------REQKQR 376
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldntrESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 377 DFDRKLLLAKSKIEMEETDKE---------QLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKAL----EEALS 443
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKElkskekelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdleDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 444 IQASPSsppaaFGSPEGVGGHLRKQ--EL-VTQNELLKQQVKIFEEDFQRErsdrermnEEKEELKKQVEKLQAQVTLTT 520
Cdd:TIGR04523 550 DDFELK-----KENLEKEIDEKNKEieELkQTQKSLKKKQEEKQELIDQKE--------KEKKDLIKEIEEKEKKISSLE 616
|
250
....*....|....*..
gi 564371823 521 AQLRTLKEEEKAKEALK 537
Cdd:TIGR04523 617 KELEKAKKENEKLSSII 633
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
313-529 |
1.12e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 313 TAEKKVKLLEQQRMELLEVNKQWDQ--HFRTMKQQY-----EQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllA 385
Cdd:COG4913 246 DAREQIELLEPIRELAERYAAARERlaELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLDA----L 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 386 KSKIEMEETDKEQLTTEAKELrqkvkyLQDQLSPLMRQREYQEKEIQRLNKALEealSIQASPSSPPAAFGSpegvgghl 465
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQ------LEREIERLERELEERERRRARLEALLA---ALGLPLPASAEEFAA-------- 384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564371823 466 RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEE 529
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
187-527 |
1.23e-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: 45.11 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 187 AEEPDHSQLFTHLGRMALEFNRLASKVHKNEQRTSIlqtlcEQLRQENEALKAKLDKSLE----QRDQAAERLREENTEL 262
Cdd:pfam17380 327 AEMDRQAAIYAEQERMAMERERELERIRQEERKREL-----ERIRQEEIAMEISRMRELErlqmERQQKNERVRQELEAA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 263 KRLlmnsnckeglcgqpsspKTEGAGKKGVAGQQQASMTASKVPEAGAfgtAEKKVKLLEQQRMELLEvnkqwdqHFRTM 342
Cdd:pfam17380 402 RKV-----------------KILEEERQRKIQQQKVEMEQIRAEQEEA---RQREVRRLEEERAREME-------RVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 343 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRdfdrklllakskieMEETDKEQLTTEAKELRQKVkyLQDQlsplmR 422
Cdd:pfam17380 455 EQERQQQVERLRQQEEERKRKKLELEKEKRDRKR--------------AEEQRRKILEKELEERKQAM--IEEE-----R 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 423 QREYQEKEIQRLNKALEEALSIQASPSSPpaafgspegvgghlRKQELVTQNELLKQQVKIFEEdfqrERSDRERMNEEK 502
Cdd:pfam17380 514 KRKLLEKEMEERQKAIYEEERRREAEEER--------------RKQQEMEERRRIQEQMRKATE----ERSRLEAMERER 575
|
330 340
....*....|....*....|....*.
gi 564371823 503 EELKKQVEKLQAQVTL-TTAQLRTLK 527
Cdd:pfam17380 576 EMMRQIVESEKARAEYeATTPITTIK 601
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
228-502 |
1.40e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 228 EQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLLMNSNCKegLCGQPSSPKTEGAGKkgvagQQQASMTASKVPE 307
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK--LYEEEKKMKAEEAKK-----AEEAKIKAEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 308 AGAFGTAEKKVKLLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFD--RKLLLA 385
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeaKKAEEL 1707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 386 KSKIEMEETDKEQLTTEAKELRQKVKYLQdqlsplmRQREYQEKEIQRLNKALEEALSIQaspssppaafgspegvggHL 465
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAK-------KEAEEDKKKAEEAKKDEEEKKKIA------------------HL 1762
|
250 260 270
....*....|....*....|....*....|....*..
gi 564371823 466 RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 502
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
335-528 |
1.80e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 335 WDQHFRTMKQQYEQKIteLRQKLVDLQKQVTELEaEREQKQRDFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQ 414
Cdd:PRK04863 495 WDVARELLRRLREQRH--LAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 415 DQLSPLMRQREYQEKEIQRLnKALEEALSIQASP--SSPPAAFGSPEGVGGHLRKQELVTQnelLKQQVKIFEEDFQREr 492
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQL-QARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTE---YMQQLLERERELTVE- 646
|
170 180 190
....*....|....*....|....*....|....*.
gi 564371823 493 sdRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKE 528
Cdd:PRK04863 647 --RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
205-439 |
1.97e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 205 EFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLLmnsNCKEGLcgqpsspkt 284
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK---EELESL--------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 285 EGAGKKGVAGQQQASmtaskvpeagafGTAEKKVKLLEQQRMELLEVNKQwdqhfrtmKQQYEQKITELRQKLVDLQKQV 364
Cdd:TIGR02168 357 EAELEELEAELEELE------------SRLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564371823 365 TELEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPL---MRQREYQEKEIQRLNKALE 439
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAeqaLDAAERELAQLQARLDSLE 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-543 |
2.68e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 330 EVNKQWDqhfrTMKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFdrklllAKSKIEMEETDKEQLTTEAKELR 407
Cdd:TIGR02168 197 ELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEELREELEE------LQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 408 QKVKYLQDQLSPL-MRQREYQEK------EIQRLNKALEEalsIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQ 480
Cdd:TIGR02168 267 EKLEELRLEVSELeEEIEELQKElyalanEISRLEQQKQI---LRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564371823 481 VKIFEedfqrersDRERMNEEKEELKKQVEKLQAQVTLTTAqLRTLKEEEKAKEALKQQKRKA 543
Cdd:TIGR02168 344 EKLEE--------LKEELESLEAELEELEAELEELESRLEE-LEEQLETLRSKVAQLELQIAS 397
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
323-559 |
3.75e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 323 QQRMELLEVNKQWDQHFRTMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQR------DFDRKLLLAKSKIEME-ETD 395
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 396 KEQltteAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLnKALEEALSIQASpssppaafgspegvgGHLRKQELVTQNE 475
Cdd:pfam15921 397 KEQ----NKRLWDRDTGNSITIDHLRRELDDRNMEVQRL-EALLKAMKSECQ---------------GQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 476 llkqqvkifEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRT-------LKEEEKAKEALKQQKRKAKAS-- 546
Cdd:pfam15921 457 ---------NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltasLQEKERAIEATNAEITKLRSRvd 527
|
250
....*....|....*.
gi 564371823 547 ---GERYHVEPHPEHL 559
Cdd:pfam15921 528 lklQELQHLKNEGDHL 543
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
314-414 |
5.53e-04 |
|
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: 42.27 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 314 AEKKVK--LLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRklLLAKSKIEM 391
Cdd:pfam02841 207 EAERAKaeAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER--MLEHKLQEQ 274
|
90 100
....*....|....*....|...
gi 564371823 392 EETDKEQLTTEAKELRQKVKYLQ 414
Cdd:pfam02841 275 EELLKEGFKTEAESLQKEIQDLK 297
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
199-515 |
6.25e-04 |
|
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: 43.04 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 199 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLLMNSNCKEGLCGQ 278
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 279 PSSPKTEGAGKKGVAGQQQASMTASKVPEAGAFGTAEKKVKLLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQKLV 358
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 359 DLQKQVTELEAEREQK--------QRDFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKE 430
Cdd:pfam02463 835 LEELALELKEEQKLEKlaeeelerLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 431 --------IQRLNKALEEALSIQASPSSPPAAFGSPEG----------VGGHLRKQELVTQNELLKQQVKIFEEDFQRER 492
Cdd:pfam02463 915 keneieerIKEEAEILLKYEEEPEELLLEEADEKEKEEnnkeeeeernKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
330 340
....*....|....*....|...
gi 564371823 493 SDRERMNEEKEELKKQVEKLQAQ 515
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
315-542 |
6.32e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 315 EKKVKLLEQQRMELLEVNKQwdqhfrtmKQQYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdrklllakSKIEMEET 394
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 395 DKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKaleealsiqaspssppaafgspegvgghlRKQELVTQN 474
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN-----------------------------TRESLETQL 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564371823 475 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKEALKQQKRK 542
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
343-509 |
6.50e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 343 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEmEETdkEQLTTEAKELRQKVKYLQDQLSPLMR 422
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-QAI--KEAKKEADEIIKELRQLQKGGYASVK 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 423 QREYQEKeIQRLNKALEEALSIQASPSSPPAAFgspeGVGGHLR---------------KQELVTQNELLKQQVKIfeed 487
Cdd:PRK00409 606 AHELIEA-RKRLNKANEKKEKKKKKQKEKQEEL----KVGDEVKylslgqkgevlsipdDKEAIVQAGIMKMKVPL---- 676
|
170 180
....*....|....*....|..
gi 564371823 488 fqrerSDRERMNEEKEELKKQV 509
Cdd:PRK00409 677 -----SDLEKIQKPKKKKKKKP 693
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
207-460 |
9.19e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 207 NRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKSLEQRDQAAERLREENTELKRLlmnsncKEGLcgqpsspkteg 286
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER------REEL----------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 287 agKKGVAGQQQASMTASKVP---EAGAFGTAEKKVKLLEQqrmeLLEVNKQWDQHFRTMKQQYEQKITELRQKLVDLQKQ 363
Cdd:COG3883 89 --GERARALYRSGGSVSYLDvllGSESFSDFLDRLSALSK----IADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 364 VTELEAEREQKQrdfdrklllakskiemeeTDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEALS 443
Cdd:COG3883 163 KAELEAAKAELE------------------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
250
....*....|....*..
gi 564371823 444 IQASPSSPPAAFGSPEG 460
Cdd:COG3883 225 AAAAAAAAAAAAAAAAA 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
347-539 |
9.22e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 347 EQKITELRQKLVDLQKQVTELEAEREQKQRDFD----RKLLLAK------SKIEMEETDKEQLTTEA------------K 404
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDalqeRREALQRlaeyswDEIDVASAEREIAELEAelerldassddlA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 405 ELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVtQNELLKQQVKIF 484
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF-AAALGDAVEREL 767
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564371823 485 EEDFQRERSD-RERMNEEKEELKKQVEKLQAQ-----VTLTT---------AQLRTLKE------EEKAKEALKQQ 539
Cdd:COG4913 768 RENLEERIDAlRARLNRAEEELERAMRAFNREwpaetADLDAdleslpeylALLDRLEEdglpeyEERFKELLNEN 843
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
314-447 |
9.56e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 314 AEKKVKLLEQQRmeLLEVNKQWDQhfrtMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllaKSKIEMEE 393
Cdd:PRK12704 47 AKKEAEAIKKEA--LLEAKEEIHK----LRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR----EEELEKKE 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 564371823 394 TDKEQLTTEAKELRQKVKYLQD-QLSPLMRQREYQEKEI-QRLNKALEEALSIQAS 447
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEeQLQELERISGLTAEEAkEILLEKVEEEARHEAA 172
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
306-399 |
1.01e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 306 PEAGAFGTAEKK--VKLLEQQRMELLEVNKQWDQHFRTMKQ----------QYEQKITELRQKLVDLQKQVTELEAEREQ 373
Cdd:PRK11448 137 PEDPENLLHALQqeVLTLKQQLELQAREKAQSQALAEAQQQelvaleglaaELEEKQQELEAQLEQLQEKAAETSQERKQ 216
|
90 100
....*....|....*....|....*.
gi 564371823 374 KQRDFDRKlllAKSKIEMEETDKEQL 399
Cdd:PRK11448 217 KRKEITDQ---AAKRLELSEEETRIL 239
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
448-546 |
1.79e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.48 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 448 PSSPPAAFGSPEGVGGHLrkQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLK 527
Cdd:PRK11448 127 WDFKPGPFVPPEDPENLL--HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ 204
|
90
....*....|....*....
gi 564371823 528 EEEKAKEALKQQKRKAKAS 546
Cdd:PRK11448 205 EKAAETSQERKQKRKEITD 223
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
314-551 |
2.01e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 314 AEKKVKLLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDF-DRKLLLAKSKIEME 392
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALnKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 393 ETDKE---------------QLTTEAK---ELRQKVKYLQDQLSPLMrqrEYQEKEIQRLNKALEEALSIqaspssppaa 454
Cdd:PHA02562 273 QFQKVikmyekggvcptctqQISEGPDritKIKDKLKELQHSLEKLD---TAIDELEEIMDEFNEQSKKL---------- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 455 fgspegvgghlrkQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKe 534
Cdd:PHA02562 340 -------------LELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI- 391
|
250
....*....|....*..
gi 564371823 535 alkqQKRKAKASGERYH 551
Cdd:PHA02562 392 ----VKTKSELVKEKYH 404
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
380-549 |
2.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 380 RKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQ---------EKEIQRLNKALEEALSiqaspss 450
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLDA------- 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 451 ppaafGSPEgvgghLRKqelvtqnelLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTTAQLRTLKEEE 530
Cdd:COG4913 683 -----SSDD-----LAA---------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
170
....*....|....*....
gi 564371823 531 KAKEALKQQKRKAKASGER 549
Cdd:COG4913 744 RLELRALLEERFAAALGDA 762
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
343-545 |
2.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 343 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRkllLAKSKIEMEETDKE--QLTTEAKELRQKVKYLQDQLSPL 420
Cdd:PRK03918 188 TENIEELIKEKEKELEEVLREINEISSELPELREELEK---LEKEVKELEELKEEieELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 421 MRQREYQEKEIQRLNKALEEALSIQASPSSPPAAfgspegvgGHLRKQELVTQNELLKQQVKIFEE--DFQRERSDRERM 498
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKELKELKEKAEEYIKL--------SEFYEEYLDELREIEKRLSRLEEEinGIEERIKELEEK 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 564371823 499 NEEKEELKKQVEKLQAQVTLTTAQLRTLkEEEKAKEALKQQKRKAKA 545
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLT 382
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
223-538 |
2.59e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 223 LQTLCEQLRQENEALKAKLdKSLEQRDQAAERLREENtelKRLLMNSNCKEglCGQP--SSPKTEGAGKKGVAGQQ---- 296
Cdd:PRK02224 410 AEDFLEELREERDELRERE-AELEATLRTARERVEEA---EALLEAGKCPE--CGQPveGSPHVETIEEDRERVEEleae 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 297 ------QASMTASKVPEAGAFGTAEKKVKLLEQQRMELLEvnkqwdqhfrtMKQQYEQKITELRQKLVDLQKQVTELEAE 370
Cdd:PRK02224 484 ledleeEVEEVEERLERAEDLVEAEDRIERLEERREDLEE-----------LIAERRETIEEKRERAEELRERAAELEAE 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 371 REQKQRDFDRKLLLAKSKIEmEETDKEQLTTEAKELRQKVKYLQDQLSplmrQREYQEKEIQRLNKALEEALSIQaspss 450
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLERIRTLLA----AIADAEDEIERLREKREALAELN----- 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 451 ppaafgspegvggHLRKQELVTQNELLKQQVKIFEED-FQRERSDRER-------MNEEKEELKKQVEKLQAQ---VTLT 519
Cdd:PRK02224 623 -------------DERRERLAEKRERKRELEAEFDEArIEEAREDKERaeeyleqVEEKLDELREERDDLQAEigaVENE 689
|
330
....*....|....*....
gi 564371823 520 TAQLRTLKEEEKAKEALKQ 538
Cdd:PRK02224 690 LEELEELRERREALENRVE 708
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
323-516 |
2.79e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 40.59 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 323 QQRMELLEVNKQWDQHFRtmKQQyeQKITELRQKLVDLQKQVTELEAEREQKQRDFDrklLLAKSKIEMEE--TDKEQLT 400
Cdd:pfam15066 311 EEDMALNEVLQKLKHTNR--KQQ--MQIQDLQCSNLYLEKKVKELQMKITKQQVFVD---IINKLKENVEEliEDKYNVI 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 401 TEAKELRQKVKYLQDQLSPLMRQRE----------------------YQEK---EIQRLNKALEEALSIQASPSSPPAAF 455
Cdd:pfam15066 384 LEKNDINKTLQNLQEILANTQKHLQesrkeketlqlelkkikvnyvhLQERyitEMQQKNKSVSQCLEMDKTLSKKEEEV 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564371823 456 GSPEGVGGHLRKqelVTQN--ELLKQQVKIFEEDF---QRERSDRERMN-EEKEELKKQVEKLQAQV 516
Cdd:pfam15066 464 ERLQQLKGELEK---ATTSalDLLKREKETREQEFlslQEEFQKHEKENlEERQKLKSRLEKLVAQV 527
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
330-440 |
2.85e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 330 EVNKQWDQHFRTMKQQYEQKITELRQKLVDLQKQVTEL-EAEREQKQRDFDRKlllakskiemeetdkeqltteAKELRQ 408
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
|
90 100 110
....*....|....*....|....*....|..
gi 564371823 409 KVKYLQDQLSplMRQREYQEKEIQRLNKALEE 440
Cdd:smart00935 77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
342-550 |
3.01e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 342 MKQQYEQKITELRQKLVDLQKQvTELEAEREQKQrdfdrKLLLAKskiemEETDKEQLTTEaKELRQKVKYLQDQLSPLM 421
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE-AKKEAEAIKKE-----ALLEAK-----EEIHKLRNEFE-KELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 422 RQREYQEKEIQRLNKaleealsiqaspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEdfqrersdrermneE 501
Cdd:PRK12704 93 QKEENLDRKLELLEK-----------------------------REEELEKKEKELEQKQQELEK--------------K 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 502 KEELKK----QVEKLQAQVTLTTAQ-----LRTLKEEEKAKEA--LKQQKRKAKASGERY 550
Cdd:PRK12704 130 EEELEElieeQLQELERISGLTAEEakeilLEKVEEEARHEAAvlIKEIEEEAKEEADKK 189
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
343-534 |
3.27e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 343 KQQYEQKITELRQkLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMR 422
Cdd:pfam15921 306 EQARNQNSMYMRQ-LSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 423 QREYQEKEIQrLNKALEEALSIQASPSSPPAafgspegvgGHLRKqELVTQN---ELLKQQVKIFEEDFQRERSDRERMN 499
Cdd:pfam15921 385 DLHKREKELS-LEKEQNKRLWDRDTGNSITI---------DHLRR-ELDDRNmevQRLEALLKAMKSECQGQMERQMAAI 453
|
170 180 190
....*....|....*....|....*....|....*
gi 564371823 500 EEKEELKKQVEKLQAQVTLTTAQLRTLKEEEKAKE 534
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKK 488
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
323-540 |
3.60e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 323 QQRMELLEVNKQWDQHFRTMKQQYEQ------KITELRQKLVDLQKQVTELEAEREQKQRDfdrkllLAKSKIEMEETDK 396
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 397 EQLTTEA-KELRQKVKYLQDQL-----------SPLMRQREYQE----------KEIQRLNKALeEALSIQASPSSPPaa 454
Cdd:PRK11281 116 ETLSTLSlRQLESRLAQTLDQLqnaqndlaeynSQLVSLQTQPEraqaalyansQRLQQIRNLL-KGGKVGGKALRPS-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 455 fgspegvgghlRKQELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQAQVTlttaQ 522
Cdd:PRK11281 193 -----------QRVLLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQEAIN----S 252
|
250
....*....|....*...
gi 564371823 523 LRTLKEEEKAKEALKQQK 540
Cdd:PRK11281 253 KRLTLSEKTVQEAQSQDE 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
342-441 |
3.67e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 342 MKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllaKSKIEMEEtdkEQLTTEAKELRQKVKylqdqlsplm 421
Cdd:COG2433 400 EKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIERLE---RELSEARSEERREIR---------- 462
|
90 100
....*....|....*....|..
gi 564371823 422 RQREYQ--EKEIQRLNKALEEA 441
Cdd:COG2433 463 KDREISrlDREIERLERELEEE 484
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
344-526 |
3.71e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 344 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETdkEQLTTEAKELRQKVKYLQDQLSP---- 419
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI--QQLRAQLAELEAELAELSARYTPnhpd 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 420 ---LMRQREYQEKEIQRLNKALEEALSIQASpssppaafgspegvGGHLRKQELVTQNELLKQQVKIFEEDfQRERSDRE 496
Cdd:COG3206 293 viaLRAQIAALRAQLQQEAQRILASLEAELE--------------ALQAREASLQAQLAQLEARLAELPEL-EAELRRLE 357
|
170 180 190
....*....|....*....|....*....|....
gi 564371823 497 R---MNEEK-EELKKQVEKLQAQVTLTTAQLRTL 526
Cdd:COG3206 358 ReveVARELyESLLQRLEEARLAEALTVGNVRVI 391
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
198-549 |
4.53e-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: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 198 HLGRMaLEFNRLASKVhknEQRTSILQTLCEQLRQENEALKAkldkSLEQRDQAAERLREENTELKRLlmnsnckeglcg 277
Cdd:COG3096 335 HLNLV-QTALRQQEKI---ERYQEDLEELTERLEEQEEVVEE----AAEQLAEAEARLEAAEEEVDSL------------ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 278 qpsspktegagKKGVAGQQQASMTASKvpEAGAFGTAekkVKLLEQQRmELLEVN-------KQWDQHFRTMKQQYEQKI 350
Cdd:COG3096 395 -----------KSQLADYQQALDVQQT--RAIQYQQA---VQALEKAR-ALCGLPdltpenaEDYLAAFRAKEQQATEEV 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 351 TELRQKLVDlqkqvteLEAEREQkqrdFDRKL-LLAKSKIEME-----ETDKEQLTT--EAKELRQKVKYLQDQLSPLmR 422
Cdd:COG3096 458 LELEQKLSV-------ADAARRQ----FEKAYeLVCKIAGEVErsqawQTARELLRRyrSQQALAQRLQQLRAQLAEL-E 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 423 QREYQEKEIQRLNKALEEALSIQASpssppaafgSPEGVGGHLrkQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 502
Cdd:COG3096 526 QRLRQQQNAERLLEEFCQRIGQQLD---------AAEELEELL--AELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI 594
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564371823 503 EELKKQ----------VEKLQAQVTLT-------TAQLRTLKEEEKAKEALKQQKRKAKASGER 549
Cdd:COG3096 595 KELAARapawlaaqdaLERLREQSGEAladsqevTAAMQQLLEREREATVERDELAARKQALES 658
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
320-543 |
4.92e-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: 40.21 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 320 LLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQKL----VDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEE-- 393
Cdd:pfam12128 273 LIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPsw 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 394 --------------TDKEQLTTEAKE-LRQKVKY-LQDQLSPLMRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGS 457
Cdd:pfam12128 353 qselenleerlkalTGKHQDVTAKYNrRRSKIKEqNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 458 PEGVGGHLRKQELVTQNELLKQQVKIFEEDF-QRERSDR--ERMNEEKEELKKQVEKLQAQVTlttaQLRTLKeeEKAKE 534
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATATPELLlQLENFDEriERAREEQEAANAEVERLQSELR----QARKRR--DQASE 506
|
....*....
gi 564371823 535 ALKQQKRKA 543
Cdd:pfam12128 507 ALRQASRRL 515
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
336-451 |
6.10e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 336 DQHFRTMKQQY---EQKITELRQKL-------VDLQKQVTELEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTTEAKE 405
Cdd:COG3206 262 SPVIQQLRAQLaelEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQ 338
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 564371823 406 LRQKVKYL---QDQLSPLMRQREYQEKEIQRLNKALEEALSIQASPSSP 451
Cdd:COG3206 339 LEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
314-414 |
6.25e-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: 39.10 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 314 AEKKVKLLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRkLLLAKSKiEMEE 393
Cdd:cd16269 203 ERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQEA 270
|
90 100
....*....|....*....|.
gi 564371823 394 TDKEQLTTEAKELRQKVKYLQ 414
Cdd:cd16269 271 LLEEGFKEQAELLQEEIRSLK 291
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
330-440 |
6.36e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 37.89 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 330 EVNKQWDQHFRTMKQQYEQKITELRQKLVDLQKQVTEL-EAEREQKQRDFDRKlllakskiemeetdkeqltteAKELRQ 408
Cdd:COG2825 43 AAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLsEEERQKKERELQKK---------------------QQELQR 101
|
90 100 110
....*....|....*....|....*....|..
gi 564371823 409 KVKYLQDQLSplMRQREYQEKEIQRLNKALEE 440
Cdd:COG2825 102 KQQEAQQDLQ--KRQQELLQPILEKIQKAIKE 131
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
150-441 |
6.75e-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: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 150 PETGHHSRNVMELGSPPPEDGNLMLHLQRLETTLSVCAEEpdHSQLFTHLGRMALEFnrLASKVHKNEQRTSILQTLCEQ 229
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE--LALKLTALHALQLTL--TQERVREHALSIRVLPKELLA 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 230 LRQ----ENEALKAKLDKSLEQRDQAAERLREENTELKRllmNSNCKEGLCGQPSSPKTEGAGKKGVAGQQQASMTASkv 305
Cdd:TIGR00618 677 SRQlalqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE---YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ-- 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 306 peagaFGTAEKKVKLLEQQRMELLEVNKQWDQHFRTMKQQYEQKITELRQklvdLQKQVTELEAEREQKQRDFDRKLLLA 385
Cdd:TIGR00618 752 -----ARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREE----DTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 564371823 386 KSKIEMEETDKEQLTTEAKELRQKVKYLQDQLSPLMRQREYQEKEIQRLNKALEEA 441
Cdd:TIGR00618 823 CETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
323-528 |
7.87e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.42 E-value: 7.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 323 QQRMELLEvNKQWD--QHFRTMKQQYEQKitelRQKLVDLQKQVTELEAEREQKQRDFDRKlllAKSKIEMEEtDKEQLT 400
Cdd:pfam10174 309 QTKLETLT-NQNSDckQHIEVLKESLTAK----EQRAAILQTEVDALRLRLEEKESFLNKK---TKQLQDLTE-EKSTLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 401 TEAKELRQ-------KVKYLQDQLSPLMRQREYQEKEIQRLNKALEealSIQASPSSPPAAfgspegvgghlrkqeLVTQ 473
Cdd:pfam10174 380 GEIRDLKDmldvkerKINVLQKKIENLQEQLRDKDKQLAGLKERVK---SLQTDSSNTDTA---------------LTTL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564371823 474 NELLKQQVKIFEE-DFQRERSDRERMNE------EKEELKKQVEKLQAQVTLTTAQLRTLKE 528
Cdd:pfam10174 442 EEALSEKERIIERlKEQREREDRERLEEleslkkENKDLKEKVSALQPELTEKESSLIDLKE 503
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
345-557 |
8.25e-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: 38.94 E-value: 8.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 345 QYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKskiemeetDKEQLTTEAKELRQKVKYLQDQLsplmrqr 424
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQ--------DYDGATAQLRAAQAAVKAAQAQL------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564371823 425 eyqekeiqrlnkaleEALSIQASPSSPPAAFGspeGVGGhlrkQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEE 504
Cdd:pfam00529 120 ---------------AQAQIDLARRRVLAPIG---GISR----ESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564371823 505 LKKQVEKLQAQVTLTTAQLRtlKEEEKAKEALKQQKRKAKASGERYHVEPHPE 557
Cdd:pfam00529 178 NQAEVRSELSGAQLQIAEAE--AELKLAKLDLERTEIRAPVDGTVAFLSVTVD 228
|
|
| |
