|
Name |
Accession |
Description |
Interval |
E-value |
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
346-547 |
1.50e-11 |
|
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: 66.33 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 346 QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQ 425
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 426 EKEIQRLNKALEEAL--SIQASPSSPPAAFGSPEGVGGHLR----------------------KQELVTQNELLKQQVKI 481
Cdd:COG4942 96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRrlqylkylaparreqaeelradLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755539259 482 FEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 547
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-543 |
6.47e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 311 AAEKKVKLleQQRMELLEVNKQW--DQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDR---------- 378
Cdd:COG1196 211 KAERYREL--KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 379 KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspeg 458
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 459 vgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQK 538
Cdd:COG1196 359 ----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
....*
gi 755539259 539 RKAKA 543
Cdd:COG1196 435 EEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
345-543 |
1.46e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 345 EQKITELRQKLVDLQKQVTELEAEREQ-------KQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSP 417
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 418 LTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMN 497
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 755539259 498 EEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKA 543
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-547 |
8.55e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 311 AAEKKVKLLEQQRMEL-LEVNKQWDQHFRSMKQ--QYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdRKLLLAKSKI 387
Cdd:COG1196 264 ELEAELEELRLELEELeLELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELE----EELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 388 EMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspegvgghlRKQE 467
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----------------------AAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 468 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 547
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-541 |
3.84e-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: 60.07 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 348 ITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEK 427
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 428 EIQRLNKALEEALSIQASPSSPPAAFGSpegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 507
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQ--------QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190
....*....|....*....|....*....|....
gi 755539259 508 EKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKA 541
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-532 |
1.04e-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: 58.49 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 313 EKKVKLLEQQRMELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLVDLQKQVTELEAERE----QKQRDFDRKLll 382
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 383 aKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspEGVGGH 462
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK--------ENQSYK 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 463 LRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKE 532
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-557 |
1.95e-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: 57.76 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 226 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnssckeglcgqpsspkpegagKKGVAGQQQASVMASKVpe 305
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----------------------RKELEELSRQISALRKD-- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 306 agaFGAAEKKVKLLEQQRMELLEVNKQwdqhfrsmkqqYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKS 385
Cdd:TIGR02168 735 ---LARLEAEVEQLEERIAQLSKELTE-----------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 386 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEgvgghlrk 465
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI-------- 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 466 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASG 545
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
330
....*....|..
gi 755539259 546 ERYHMEPHPEHV 557
Cdd:TIGR02168 949 YSLTLEEAEALE 960
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-511 |
2.20e-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: 57.37 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 213 KNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGAGKKGVAG 292
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 293 QQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQY------------------------EQKI 348
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerleslerriaatERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 349 TELRQKLVDLQKQVTELEAEREQKQRDFDR------KLLLAKSKIEME----ETDKEQLTAEAKELRQKVRYLQDQLSPL 418
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEEleseleALLNERASLEEAlallRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 419 TRQRE-YQEK------EIQRLNKALEEALSI--QASPSSPPAAFGSPEGVGGHLRKqelvtqnelLKQQVKIF------- 482
Cdd:TIGR02168 921 REKLAqLELRleglevRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRRLKR---------LENKIKELgpvnlaa 991
|
330 340
....*....|....*....|....*....
gi 755539259 483 EEDFQRERSDRERMNEEKEELKKQVEKLQ 511
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-560 |
2.61e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 206 RLASKVHKNEQRTSILQTLcEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLmnssckeglcgqpsspkpega 285
Cdd:COG1196 226 EAELLLLKLRELEAELEEL-EAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 286 gkkGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWdqhfrsmkqqyEQKITELRQKLVDLQKQVTEL 365
Cdd:COG1196 284 ---EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-----------EEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 366 EAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAs 445
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 446 pssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 525
Cdd:COG1196 429 ------------------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330 340 350
....*....|....*....|....*....|....*
gi 755539259 526 EEEKAKEALKQQKRKAKASGERYHMEPHPEHVCGA 560
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
342-513 |
3.58e-08 |
|
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: 54.55 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 342 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQ 421
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 422 REYQ--EKEIQRLNKAL----EEALSIQAspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDREr 495
Cdd:COG1579 89 KEYEalQKEIESLKRRIsdleDEILELME-------------------RIEELEEELAELEAELAELEAELEEKKAELD- 148
|
170
....*....|....*...
gi 755539259 496 mnEEKEELKKQVEKLQAQ 513
Cdd:COG1579 149 --EELAELEAELEELEAE 164
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
465-513 |
1.21e-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: 49.66 E-value: 1.21e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755539259 465 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 513
Cdd:cd09803 34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
340-549 |
1.73e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 340 MKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS 416
Cdd:COG4913 247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 417 PLTRQREYQ--------EKEIQRLNKALEEalsiqaspssppaafgspegvgghlRKQELVTQNELLKQ---QVKIFEED 485
Cdd:COG4913 327 ELEAQIRGNggdrleqlEREIERLERELEE-------------------------RERRRARLEALLAAlglPLPASAEE 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755539259 486 FQRErsdRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEA-LKQQKRKAKASGERYH 549
Cdd:COG4913 382 FAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeIASLERRKSNIPARLL 443
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-551 |
2.14e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 345 EQKITELRQKLVDLQKQVTELEAEREQKQRDfdRKLLLAKSKIEMEEtdkeqLTAEAKELRQKVRYLQDQLSPLTRQREY 424
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYE-----LLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 425 QEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFE---EDFQRER----SDRERMN 497
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErelEDAEERLakleAEIDKLL 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 755539259 498 EEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERYHME 551
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-548 |
2.95e-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: 53.91 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 342 QQYEQKITELRQKLVDLQKQVTELEAER---EQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPL 418
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 419 TRQREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQrerSDRERMNE 498
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEA----------------------EEELAEAEAEIEELEAQIEQLKEELK---ALREALDE 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 755539259 499 EKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERY 548
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
341-547 |
3.68e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 341 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSplTR 420
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 421 QREYQEKeiQRLNKALEEALSiqaspSSPPAAFgspegvgghLRKQELVT-----QNELLKQQ---VKIFEEDFQRERSD 492
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLG-----SESFSDF---------LDRLSALSkiadaDADLLEELkadKAELEAKKAELEAK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 755539259 493 RERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 547
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
334-548 |
2.29e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 334 DQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQ-KQR----DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKV 408
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 409 RYLQDQL--SPLTRQREYQEKEIQRLNKALEEA------LSIQASPSSPPAafgspegvgghlrkQELVTQNELLKQQVK 480
Cdd:COG3206 243 AALRAQLgsGPDALPELLQSPVIQQLRAQLAELeaelaeLSARYTPNHPDV--------------IALRAQIAALRAQLQ 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755539259 481 ifeedfQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKakeALKQQKRKAKASGERY 548
Cdd:COG3206 309 ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA---ELRRLEREVEVARELY 367
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
206-547 |
3.01e-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: 50.74 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 206 RLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGA 285
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 286 GKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNkqwdqhfRSMKQQYEQKITELRQKLVDLQKQVTEL 365
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-------KSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 366 EAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAS 445
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 446 PSSPpaafgspegvgGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 525
Cdd:pfam02463 407 AQLL-----------LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|..
gi 755539259 526 EEEKAKEALKQQKRKAKASGER 547
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEE 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-441 |
3.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 166 EDSNLKLHLQRLETTLSVCAEEpdHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQ 245
Cdd:COG1196 233 KLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 246 RDLAAERLREENTELKKLlmnssckeglcgqpsspkpegAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRME 325
Cdd:COG1196 311 RRELEERLEELEEELAEL---------------------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 326 LLEVNKQWDQHFRSMKQQY---EQKITELRQKLVDLQKQVTELE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTA 399
Cdd:COG1196 370 AEAELAEAEEELEELAEELleaLRAAAELAAQLEELEEAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 755539259 400 EAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 441
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
211-529 |
3.79e-06 |
|
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: 50.12 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 211 VHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLcgqpsspKPEGAGKKGV 290
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL-------KLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 291 AG--QQQASVMASKVPEAG-AFGAAEKKVKLLEQQ----RMELlevnkqwdQHFRSMKQQYEQKITELRQKLVDLQKQVT 363
Cdd:pfam15921 564 IEilRQQIENMTQLVGQHGrTAGAMQVEKAQLEKEindrRLEL--------QEFKILKDKKDAKIRELEARVSDLELEKV 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 364 ELEAEREQKQRdfdrklllAKSKIEMEetdKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEAL-SI 442
Cdd:pfam15921 636 KLVNAGSERLR--------AVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLkSA 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 443 QASPSSPPAAFGSPEGVGGHLRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 513
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQItakrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
330
....*....|....*.
gi 755539259 514 VTLTNAQLKTLKEEEK 529
Cdd:pfam15921 785 KNKMAGELEVLRSQER 800
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-511 |
4.91e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 301 SKVPE-AGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMK------QQYEQKITELRQKLVDLQKQVTELE-----AE 368
Cdd:PRK03918 214 SELPElREELEKLEKEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVKELKelkekAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 369 REQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLN---KALEEALSIQAS 445
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEE 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755539259 446 PSSPPAAFGSpegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQ 511
Cdd:PRK03918 374 LERLKKRLTG-------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-507 |
7.29e-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: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 197 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLD---KGLEQRDLAAERLREENTELKKLLMNSsckegl 273
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSHS------ 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 274 cgqpssPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQ---KITE 350
Cdd:TIGR02169 792 ------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 351 LRQKLVDLQKQVTELEAEREQKQRDFDR---KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS---PLTRQREY 424
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEE 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 425 QEKEIQRLNKALEEALSIQASPSS-PPAAFGSPEGVgghlrKQELVTQNELLKQQVKIFEEdfqreRSDRERMNEEKEEL 503
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRAlEPVNMLAIQEY-----EEVLKRLDELKEKRAKLEEE-----RKAILERIEEYEKK 1015
|
....
gi 755539259 504 KKQV 507
Cdd:TIGR02169 1016 KREV 1019
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
473-515 |
8.91e-06 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 44.59 E-value: 8.91e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 755539259 473 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 515
Cdd:pfam16516 55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-542 |
1.01e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 313 EKKVKLLEQQRMELlevnkqwdQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEET 392
Cdd:TIGR04523 186 QKNIDKIKNKLLKL--------ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 393 DKEQLTAEAKELRQKVRYLQD---QLSPLTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspEGVGGHLRKQE-- 467
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKEQDWN---------------KELKSELKNQEkk 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 468 -LVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQvtlTNAQLKTLKEEEKAKEALKQQ 537
Cdd:TIGR04523 323 lEEIQNQIsqnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEIKNLESQINDLESK 399
|
....*
gi 755539259 538 KRKAK 542
Cdd:TIGR04523 400 IQNQE 404
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-513 |
1.08e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 312 AEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYE---------QKITELRQKLVD---LQKQVTELEAEREQkqrdfdrk 379
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDalqerrealQRLAEYSWDEIDvasAEREIAELEAELER-------- 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 380 LLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAafgspegv 459
Cdd:COG4913 680 LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL-------- 751
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 755539259 460 gghlrkqELVTQNELLKQQVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQ 513
Cdd:COG4913 752 -------EERFAAALGDAVERELRENLEER---IDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-547 |
1.13e-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: 48.91 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 182 SVCAEEPDHSQLFTH-LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTEL 260
Cdd:TIGR02169 667 LFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 261 kkllmnSSCKEGLcgqpSSPKPEGAGKKGVAGQQQASvmaskvpeagafgAAEKKVKLLEQQRMELLEVNKQWDQHFRSM 340
Cdd:TIGR02169 747 ------SSLEQEI----ENVKSELKELEARIEELEED-------------LHKLEEALNDLEARLSHSRIPEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 341 KQQY---EQKITELRQKLVDLQKQVTELEAEREQKQ---RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQ 414
Cdd:TIGR02169 804 EEEVsriEARLREIEQKLNRLTLEKEYLEKEIQELQeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 415 LSPLTRQREYQEKEIQRLNKALEEaLSIQASPSsppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRE 494
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEE-LEAQIEKK--------------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 755539259 495 RMNEEkEELKKQVEKLQAQV-TLTNAQLKTLKEEEKAKEALKQ-QKRKAKASGER 547
Cdd:TIGR02169 949 EELSL-EDVQAELQRVEEEIrALEPVNMLAIQEYEEVLKRLDElKEKRAKLEEER 1002
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
204-543 |
1.27e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 204 FNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENtELKKLLMNSSCKeglcGQPSSPKPE 283
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKK----ADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 284 GAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEvnkqwdqhfrsMKQQYEQKITELRQKLVDLQKQVT 363
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-----------KKAEEKKKADEAKKKAEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 364 ELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRylQDQLSPLTRQREYQEKEIQRLNKALEEALSIQ 443
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE--EAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 444 ASPSSPPAAfgspegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK---EELKKQVEKLQAQVTLTNAQ 520
Cdd:PTZ00121 1487 EAKKKAEEA----------KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADELKKAEE 1556
|
330 340
....*....|....*....|...
gi 755539259 521 LKTLKEEEKAKEALKQQKRKAKA 543
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMA 1579
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-545 |
1.30e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 311 AAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQ---YEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLA---- 383
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyrlg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 384 ---KSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREyqekEIQRLNKALEEALSIQASpssppaafgspegvg 460
Cdd:COG4942 118 rqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEA--------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 461 ghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQaqvtltnAQLKTLKEEEKAKEALKQQKRK 540
Cdd:COG4942 179 ---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAAAAERTPAAGF 248
|
....*
gi 755539259 541 AKASG 545
Cdd:COG4942 249 AALKG 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-514 |
2.81e-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: 47.37 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 202 LEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnssckeglcgqpsspk 281
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------------------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 282 peGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMEL-LEVNKQwdqhfRSMKQQYEQKITELRQKLVDLQK 360
Cdd:TIGR02169 285 --GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLeAEIDKL-----LAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 361 QVTELEAEREQKQRDF---DRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLN---K 434
Cdd:TIGR02169 358 EYAELKEELEDLRAELeevDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEakiN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 435 ALEEALsiqaspssppaafgspEGVGGHLRKQElvTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQV 514
Cdd:TIGR02169 438 ELEEEK----------------EDKALEIKKQE--WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
313-546 |
3.61e-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: 47.04 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 313 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQklvdlqkqvtELEAEREQKQRDFDRKLLLAKSKIEMEET 392
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 393 DKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQEL---- 468
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 469 -----------VTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKkqveKLQAQVTLTNAQLKTLKEEEKAKEALKQQ 537
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR----RIQEQMRKATEERSRLEAMEREREMMRQI 581
|
....*....
gi 755539259 538 KRKAKASGE 546
Cdd:pfam17380 582 VESEKARAE 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
199-551 |
3.64e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 199 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRQENEALK-AKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQP 277
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 278 SSPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEK-----KVKLLEQQRMEllEVNKQWDQHFRSMKQQYEQKITELR 352
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 353 QKLVDLQKQVTELEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEI 429
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 430 QRLNKALEEalsiqaspssppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEK 509
Cdd:PTZ00121 1678 EEAKKAEED-----------------------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 755539259 510 LQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERYHME 551
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
341-507 |
4.59e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 341 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEmEETdkEQLTAEAKELRQKVRYLQDQLSPLTR 420
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-QAI--KEAKKEADEIIKELRQLQKGGYASVK 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 421 QREYQEKeIQRLNKALEEALSIQASPSSPPAAFgspeGVGGHLR---------------KQELVTQNELLKQQVKIfeed 485
Cdd:PRK00409 606 AHELIEA-RKRLNKANEKKEKKKKKQKEKQEEL----KVGDEVKylslgqkgevlsipdDKEAIVQAGIMKMKVPL---- 676
|
170 180
....*....|....*....|..
gi 755539259 486 fqrerSDRERMNEEKEELKKQV 507
Cdd:PRK00409 677 -----SDLEKIQKPKKKKKKKP 693
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-540 |
5.77e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 313 EKKVKLLEQQRMELLEVNKQwdqhfrsmKQQYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdrklllakSKIEMEET 392
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 393 DKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKaleealsiqaspssppaafgspegvgghlRKQELVTQN 472
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN-----------------------------TRESLETQL 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755539259 473 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRK 540
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
318-527 |
5.81e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 318 LLEQQRMELLEVNKQWDQhfrsmKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKE 395
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-----KEEKDlhERLNGLESELAELDEEIERYEEQREQARETRDE----ADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 396 QLTaeakELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEaLSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELL 475
Cdd:PRK02224 252 ELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 755539259 476 KQ-------QVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEE 527
Cdd:PRK02224 327 RDrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
335-526 |
6.28e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 335 QHFRSMKQQY-EQKIteLRQKLVDLQKQVTELEaEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQD 413
Cdd:PRK04863 496 DVARELLRRLrEQRH--LAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 414 QLSPLTRQREYQEKEIQRLnKALEEALSIQASP--SSPPAAFGSPEGVGGHLRKQELVTQnelLKQQVKIFEEDFQRErs 491
Cdd:PRK04863 573 SVSEARERRMALRQQLEQL-QARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTE---YMQQLLERERELTVE-- 646
|
170 180 190
....*....|....*....|....*....|....*
gi 755539259 492 dRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKE 526
Cdd:PRK04863 647 -RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-543 |
7.24e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 311 AAEKKVKLLEQQRMELLEVNKQWDQhFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQ-------RDFDRKLLLA 383
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 384 KSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLnkALEEALSIQASPSSPPAAFGSPEGVGGhL 463
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL--IAAALLALLGLGGSLLSLILTIAGVLF-L 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 464 RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKA 543
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
227-264 |
9.94e-05 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 44.58 E-value: 9.94e-05
10 20 30
....*....|....*....|....*....|....*...
gi 755539259 227 QLRQENEALKAKLDKgLEQRDLAAERLREENTELKKLL 264
Cdd:PRK13922 73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
340-548 |
1.13e-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: 45.35 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 340 MKQQYEQKITELRQKLVDLQKQVTELEAEREQkqrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLT 419
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 420 R-------QREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSD 492
Cdd:pfam02463 241 LlqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755539259 493 RERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERY 548
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
203-443 |
1.19e-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: 45.43 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 203 EFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLmnsSCKEGLcgqpsspkp 282
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK---EELESL--------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 283 egagkkgvagQQQASVMASKVPEAGAfgAAEKKVKLLEQQRMELLEVNKQwdqhfrsmKQQYEQKITELRQKLVDLQKQV 362
Cdd:TIGR02168 357 ----------EAELEELEAELEELES--RLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 363 TELEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 441
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
..
gi 755539259 442 IQ 443
Cdd:TIGR02168 497 LQ 498
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
302-445 |
1.98e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 302 KVPEAGAFGAAEKKVKLLEQQRME--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQ 373
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755539259 374 RDFDRK---LLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTrqreyQEKEIQRLNKALEEALSIQAS 445
Cdd:PRK12704 103 ELLEKReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLT-----AEEAKEILLEKVEEEARHEAA 172
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
321-557 |
2.26e-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: 44.34 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 321 QQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQR------DFDRKLLLAKSKIEME-ETD 393
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 394 KEQltaeAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQASpssppaafgspegvgGHLRKQELVTQNE 473
Cdd:pfam15921 397 KEQ----NKRLWDRDTGNSITIDHLRRELDDRNMEVQRL-EALLKAMKSECQ---------------GQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 474 llkqqvkifEEDFQRERSDRERMNEEKEELKKQVEKLQA-QVTLTNAQ------LKTLKEEEKAKEALKQQKRKAKAS-- 544
Cdd:pfam15921 457 ---------NESLEKVSSLTAQLESTKEMLRKVVEELTAkKMTLESSErtvsdlTASLQEKERAIEATNAEITKLRSRvd 527
|
250
....*....|....*.
gi 755539259 545 ---GERYHMEPHPEHV 557
Cdd:pfam15921 528 lklQELQHLKNEGDHL 543
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-535 |
2.29e-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: 44.24 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 313 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQY---EQKITELRQKLVDLQKQVTELEAE---------------REQKQR 374
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldntrESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 375 DFDRKLLLAKSKIEMEETDKE---------QLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKAL----EEALS 441
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKElkskekelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdleDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 442 IQASPSsppaaFGSPEGVGGHLRKQ--EL-VTQNELLKQQVKIFEEDFQRErsdrermnEEKEELKKQVEKLQAQVTLTN 518
Cdd:TIGR04523 550 DDFELK-----KENLEKEIDEKNKEieELkQTQKSLKKKQEEKQELIDQKE--------KEKKDLIKEIEEKEKKISSLE 616
|
250
....*....|....*..
gi 755539259 519 AQLKTLKEEEKAKEALK 535
Cdd:TIGR04523 617 KELEKAKKENEKLSSII 633
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
168-418 |
2.51e-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: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 168 SNLKLHLQRLETTLSVCAEEPDHSQLfthlgrmalEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRD 247
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSK---------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 248 LAAERLREENTELKKLLMNSSCKEGLCGQpSSPKPEGAGKKGVAGQQQASVMASKVpeAGAFGAAEKKVKLLEQQRMELL 327
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 328 EVNKQWDQHFRSMK-------------QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKL--LLAKSKIEMEE- 391
Cdd:TIGR02168 877 ALLNERASLEEALAllrseleelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEa 956
|
250 260
....*....|....*....|....*...
gi 755539259 392 -TDKEQLTAEAKELRQKVRYLQDQLSPL 418
Cdd:TIGR02168 957 eALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
226-500 |
3.21e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 226 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKegLCGQPSSPKPEGAGKkgvagQQQASVMASKVPE 305
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK--LYEEEKKMKAEEAKK-----AEEAKIKAEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 306 AGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKqvtelEAEREQKQRDFDRKLLLAKS 385
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK-----AEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 386 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQaspssppaafgspegvggHLRK 465
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA------------------HLKK 1764
|
250 260 270
....*....|....*....|....*....|....*
gi 755539259 466 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 500
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
312-549 |
4.02e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 312 AEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFdRKLLLAKSKIEMEe 391
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAKIKSK- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 392 tdKEQLTAEAKELRQ----------------KVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQaspssppaafgs 455
Cdd:PHA02562 271 --IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS------------ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 456 pegvgghLRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKealk 535
Cdd:PHA02562 337 -------KKLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI---- 391
|
250
....*....|....
gi 755539259 536 qQKRKAKASGERYH 549
Cdd:PHA02562 392 -VKTKSELVKEKYH 404
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
446-544 |
7.03e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 446 PSSPPAAFGSPEGVGGHLrkQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 525
Cdd:PRK11448 127 WDFKPGPFVPPEDPENLL--HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ 204
|
90
....*....|....*....
gi 755539259 526 EEEKAKEALKQQKRKAKAS 544
Cdd:PRK11448 205 EKAAETSQERKQKRKEITD 223
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
165-547 |
7.04e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 165 PEDSNLKLHLQRLETTLSVC---AEEPDHSQ----LFTHLGRMALEFNRLASKVHKNEQRTSILQTLceQLRQENEALKA 237
Cdd:PRK04863 223 PENSGVRKAFQDMEAALRENrmtLEAIRVTQsdrdLFKHLITESTNYVAADYMRHANERRVHLEEAL--ELRRELYTSRR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 238 KLDKglEQRDLaaERLREENTELKKllmnsscKEGLCGQPSspkpegagkkgvagqQQASVMASKVPEAGAF-------- 309
Cdd:PRK04863 301 QLAA--EQYRL--VEMARELAELNE-------AESDLEQDY---------------QAASDHLNLVQTALRQqekieryq 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 310 GAAEKKVKLLEQQRMELLEVNKQWDQHfRSMKQQYEQKITELRQKLVDLQKQVTELEA---EREQKQRDFDR-KLLLAKS 385
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEEN-EARAEAAEEEVDELKSQLADYQQALDVQQTraiQYQQAVQALERaKQLCGLP 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 386 KIEMEETDK--EQLTAEAKELRQKVRYLQDQLSPLTRQREYQEK----------EIQRlNKALEEALS-IQASPSSPPAA 452
Cdd:PRK04863 434 DLTADNAEDwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagEVSR-SEAWDVARElLRRLREQRHLA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 453 fGSPEGVGGHLR--KQELVTQ---NELLKQQVKIF------EEDFQRERSDRErmnEEKEELKKQVEKLQAQVTLTNAQL 521
Cdd:PRK04863 513 -EQLQQLRMRLSelEQRLRQQqraERLLAEFCKRLgknlddEDELEQLQEELE---ARLESLSESVSEARERRMALRQQL 588
|
410 420
....*....|....*....|....*.
gi 755539259 522 KTLKEEEKAKEALKQQKRKAKASGER 547
Cdd:PRK04863 589 EQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
315-397 |
8.12e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 315 KVKLLEQQRMELLEVNKQWDQHFRSMKQ----------QYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllAK 384
Cdd:PRK11448 150 EVLTLKQQLELQAREKAQSQALAEAQQQelvaleglaaELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQ---AA 226
|
90
....*....|...
gi 755539259 385 SKIEMEETDKEQL 397
Cdd:PRK11448 227 KRLELSEEETRIL 239
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
334-449 |
8.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 334 DQHFRSMKQQY---EQKITELRQKL-------VDLQKQVTELEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKE 403
Cdd:COG3206 262 SPVIQQLRAQLaelEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQ 338
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 755539259 404 LRQKVRYL---QDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSP 449
Cdd:COG3206 339 LEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-540 |
1.19e-03 |
|
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: 41.93 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 313 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLqKQVTELEAEREQKQRDFDRKLLLAKSKIEMEET 392
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 393 DKEQLTAEAKELRQKVRYLQDQLSpltrqREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvggHLRKQELVTQN 472
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEEL----------------------KQTQKSLKKKQ 584
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755539259 473 ELLKQQVKIFEEDFQRERSDRE-------RMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKA-KEALKQQKRK 540
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQiKETIKEIRNK 660
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
345-542 |
1.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 345 EQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREY 424
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 425 QEKEIQRLNKALEEALSIQ--------------------------ASPSSPPAAFGSPEG--------VGGHLRKQELVT 470
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKgkcpvcgrelteehrkelleeytaelKRIEKELKEIEEKERklrkelreLEKVLKKESELI 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755539259 471 QNELLKQQVKIFEEDFQR-ERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAK 542
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
321-538 |
1.30e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 321 QQRMELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLVDLQKQVTELEAEREQKQRDfdrkllLAKSKIEMEETDK 394
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 395 EQL-TAEAKELRQKVRYLQDQL-----------SPLTRQREYQE----------KEIQRLNKALeEALSIQASPSSPPaa 452
Cdd:PRK11281 116 ETLsTLSLRQLESRLAQTLDQLqnaqndlaeynSQLVSLQTQPEraqaalyansQRLQQIRNLL-KGGKVGGKALRPS-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 453 fgspegvgghlRKQELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQaqvTLTNAq 520
Cdd:PRK11281 193 -----------QRVLLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQ---EAINS- 252
|
250
....*....|....*....
gi 755539259 521 lKTLKE-EEKAKEALKQQK 538
Cdd:PRK11281 253 -KRLTLsEKTVQEAQSQDE 270
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
311-412 |
1.33e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 311 AAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRkLLLAKSKiEME 390
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
|
90 100
....*....|....*....|..
gi 755539259 391 ETDKEQLTAEAKELRQKVRYLQ 412
Cdd:cd16269 270 ALLEEGFKEQAELLQEEIRSLK 291
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
338-439 |
1.41e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 338 RSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllaKSKIEMEEtdkEQLTAEAKELRQKVRylqdqlsp 417
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIERLE---RELSEARSEERREIR-------- 462
|
90 100
....*....|....*....|....
gi 755539259 418 ltRQREYQ--EKEIQRLNKALEEA 439
Cdd:COG2433 463 --KDREISrlDREIERLERELEEE 484
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
327-543 |
1.51e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 327 LEVNKQwdqhfrSMKQQYEQKIT------ELRQKLvdLQKQVTELEAER--EQKQRDfdrKLLLAKSKIEMEETDKE-QL 397
Cdd:pfam01576 718 LEVNMQ------ALKAQFERDLQardeqgEEKRRQ--LVKQVRELEAELedERKQRA---QAVAAKKKLELDLKELEaQI 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 398 TAEAK---ELRQKVRYLQDQLSPLTRQRE----------YQEKEIQRLNKALE-EALSIQASPSSPPAAFG--------- 454
Cdd:pfam01576 787 DAANKgreEAVKQLKKLQAQMKDLQRELEearasrdeilAQSKESEKKLKNLEaELLQLQEDLAASERARRqaqqerdel 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 455 SPEGVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTltnAQLKTLKEEEKAKEAL 534
Cdd:pfam01576 867 ADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA---AERSTSQKSESARQQL 943
|
....*....
gi 755539259 535 KQQKRKAKA 543
Cdd:pfam01576 944 ERQNKELKA 952
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
311-412 |
1.55e-03 |
|
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: 41.12 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 311 AAEKKVKLLEQQRMELlevnkqwDQHFRSMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRklLLAKSKIEME 390
Cdd:pfam02841 215 AAEAEQELLREKQKEE-------EQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER--MLEHKLQEQE 275
|
90 100
....*....|....*....|..
gi 755539259 391 ETDKEQLTAEAKELRQKVRYLQ 412
Cdd:pfam02841 276 ELLKEGFKTEAESLQKEIQDLK 297
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-555 |
1.63e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 197 LGRMALEFNRLASKVHKNE---QRTSILQTLCEQLRQENEALK-AKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEG 272
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAaakKKADEAKKKAEEKKKADEAKKkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 273 LCGQPSSPKPEGAGKKGVAGQQQASVMASKvpeAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELR 352
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKA---AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 353 qKLVDLQKqvTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLspltRQREYQEKEIQRL 432
Cdd:PTZ00121 1553 -KAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 433 NKALEEALSIQASPSSPPAAFGSPEgvggHLRKQElvTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQA 512
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAE----ELKKAE--EENKIKAAEEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 755539259 513 QVTLTNAQLKTLKEEEKAK-EALKQQKRKAKASGERYHMEPHPE 555
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKaEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
299-526 |
1.75e-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: 41.86 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 299 MASKVPEAGAFGAAEkkvklleqqrmELLEvnkqwdqHFRSMKQQYEQkITELRQKLVDLQKQVTELEAEREQkQRDFDR 378
Cdd:COG3096 484 IAGEVERSQAWQTAR-----------ELLR-------RYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERL-LEEFCQ 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 379 KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNK------ALEEALSIQASPSSppAA 452
Cdd:COG3096 544 RIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSG--EA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755539259 453 FGSPEGVGGHLrkqelvtqnellkQQVKIFEEDFQRERsdrERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKE 526
Cdd:COG3096 622 LADSQEVTAAM-------------QQLLEREREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
321-526 |
2.33e-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: 40.96 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 321 QQRMELLEvNKQWD--QHFRSMKQQYEQKitelRQKLVDLQKQVTELEAEREQKQRDFDRKlllAKSKIEMEEtDKEQLT 398
Cdd:pfam10174 309 QTKLETLT-NQNSDckQHIEVLKESLTAK----EQRAAILQTEVDALRLRLEEKESFLNKK---TKQLQDLTE-EKSTLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 399 AEAKELRQ-------KVRYLQDQLSPLTRQREYQEKEIQRLNKALEealSIQASPSSPPAAfgspegvgghlrkqeLVTQ 471
Cdd:pfam10174 380 GEIRDLKDmldvkerKINVLQKKIENLQEQLRDKDKQLAGLKERVK---SLQTDSSNTDTA---------------LTTL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755539259 472 NELLKQQVKIFEE-DFQRERSDRERMNE------EKEELKKQVEKLQAQVTLTNAQLKTLKE 526
Cdd:pfam10174 442 EEALSEKERIIERlKEQREREDRERLEEleslkkENKDLKEKVSALQPELTEKESSLIDLKE 503
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
315-437 |
3.26e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 315 KVKLLEQQRMELLEVNKQWDQHF----RSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEME 390
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 755539259 391 ETDKEQLTAEAKELRQkvrylqdQLSPLTRQREYQEKEIQRLNKALE 437
Cdd:pfam00038 95 LNLRTSAENDLVGLRK-------DLDEATLARVDLEAKIESLKEELA 134
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
345-514 |
3.30e-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: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 345 EQKITELRQK------LVD----LQKQVTELEAEREQ---KQRDFDRKL-----LLAKSKIEMEET--DKEQLTAEAKEL 404
Cdd:pfam15066 345 EKKVKELQMKitkqqvFVDiinkLKENVEELIEDKYNvilEKNDINKTLqnlqeILANTQKHLQESrkEKETLQLELKKI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 405 rqKVRYLQDQLSPLTrqreyqekEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKqelVTQN--ELLKQQVKIF 482
Cdd:pfam15066 425 --KVNYVHLQERYIT--------EMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEK---ATTSalDLLKREKETR 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 755539259 483 EEDF---QRERSDRERMN-EEKEELKKQVEKLQAQV 514
Cdd:pfam15066 492 EQEFlslQEEFQKHEKENlEERQKLKSRLEKLVAQV 527
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
206-513 |
3.30e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 206 RLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGA 285
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 286 GKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTEL 365
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 366 EAEREQKQRDFDRKLLLAKSKI---EMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 442
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLkdeLESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755539259 443 QASPSSPPAAFGSPE----GVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 513
Cdd:pfam02463 943 EEADEKEKEENNKEEeeerNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
328-438 |
3.61e-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: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 328 EVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTEL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 406
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
|
90 100 110
....*....|....*....|....*....|..
gi 755539259 407 KVRYLQDQLSplTRQREYQEKEIQRLNKALEE 438
Cdd:smart00935 77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
335-458 |
3.79e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 335 QHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKqrdfdrklllakskiemeETDKEQLTAEAKELRQKVRYLQDQ 414
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQ 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 755539259 415 LSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEG 458
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
221-534 |
4.24e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 221 LQTLCEQLRQENEALKAKLdkgleqRDLAAERLREENT--ELKKLLMNSSCKEglCGQP--SSPKPEGAGKKGV------ 290
Cdd:PRK02224 410 AEDFLEELREERDELRERE------AELEATLRTARERveEAEALLEAGKCPE--CGQPveGSPHVETIEEDRErveele 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 291 -----AGQQQASVmASKVPEAGAFGAAEKKVKLLEQQRMELLEvnkqwdqhfrsMKQQYEQKITELRQKLVDLQKQVTEL 365
Cdd:PRK02224 482 aeledLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEE-----------LIAERRETIEEKRERAEELRERAAEL 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 366 EAEREQKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVRYLQDQLSpltrQREYQEKEIQRLNKALEEALSIQas 445
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLERIRTLLA----AIADAEDEIERLREKREALAELN-- 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 446 pssppaafgspegvggHLRKQELVTQNELLKQQVKIFEED-FQRERSDRER-------MNEEKEELKKQVEKLQAQVTLT 517
Cdd:PRK02224 623 ----------------DERRERLAEKRERKRELEAEFDEArIEEAREDKERaeeyleqVEEKLDELREERDDLQAEIGAV 686
|
330
....*....|....*..
gi 755539259 518 NAQLKTLKEEEKAKEAL 534
Cdd:PRK02224 687 ENELEELEELRERREAL 703
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
342-521 |
4.99e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 342 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVRYLQDqlSP- 417
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSARYTPN--HPd 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 418 ---LTRQREYQEKEIQRLNKALEEALSIQASpssppaafgspegvGGHLRKQELVTQNELLKQQVKIFEEDfQRERSDRE 494
Cdd:COG3206 293 viaLRAQIAALRAQLQQEAQRILASLEAELE--------------ALQAREASLQAQLAQLEARLAELPEL-EAELRRLE 357
|
170 180 190
....*....|....*....|....*....|...
gi 755539259 495 RMNEEKEE-----LKKQVE-KLQAQVTLTNAQL 521
Cdd:COG3206 358 REVEVARElyeslLQRLEEaRLAEALTVGNVRV 390
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
169-439 |
5.67e-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: 39.95 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 169 NLKLHLQRLETTLSVCAEEpdHSQLFTHLGRMALEFnrLASKVHKNEQRTSILQTLCEQLRQ----ENEALKAKLDKGLE 244
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQE--LALKLTALHALQLTL--TQERVREHALSIRVLPKELLASRQlalqKMQSEKEQLTYWKE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 245 QRDLAAERLREENTELKKllmNSSCKEGLCGQPSSPKPEGAGKKGVAGQQQASVMASkvpeagaFGAAEKKVKLLEQQRM 324
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEE---YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ-------ARTVLKARTEAHFNNN 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 325 ELLEVNKQWDQHFRSMKQQYEQKITELRQklvdLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKEL 404
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREE----DTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAT 843
|
250 260 270
....*....|....*....|....*....|....*
gi 755539259 405 RQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEA 439
Cdd:TIGR00618 844 LGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
230-542 |
5.81e-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: 39.82 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 230 QENEALKAKLDKGLEQRDLA---AERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGAGKKGVAGQQQASVMASKVPEA 306
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSArekQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 307 GAFgaAEKKVKLLEQQRMELLEVNKQWDQHF-------RSMKQQYEQKITELRQKLVDLQKQVTELE---AEREQKQRDF 376
Cdd:pfam12128 677 KDS--ANERLNSLEAQLKQLDKKHQAWLEEQkeqkreaRTEKQAYWQVVEGALDAQLALLKAAIAARrsgAKAELKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 377 DRKLLLAK--------SKIEMEETDKEQLTAEAKELRQKV----RYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQA 444
Cdd:pfam12128 755 WYKRDLASlgvdpdviAKLKREIRTLERKIERIAVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLARLI 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 445 SPSSppaafgspegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEElkKQVEKLQAQVTLTNAQLKTL 524
Cdd:pfam12128 835 ADTK--------------LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED--ANSEQAQGSIGERLAQLEDL 898
|
330
....*....|....*....
gi 755539259 525 KEE-EKAKEALKQQKRKAK 542
Cdd:pfam12128 899 KLKrDYLSESVKKYVEHFK 917
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
470-542 |
5.95e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755539259 470 TQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEE-EKAKEALKQQKRKAK 542
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiAEAEAEIEERREELG 89
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
397-528 |
7.45e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 38.97 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 397 LTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQASPSSPPAAFGSPEGvgghlRKQELVTQNELL 475
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQLATERS-----ARREAEAELERL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 755539259 476 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQvtLTNAQLKTLKEEE 528
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQ--LTSKSQSSSSQSE 167
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
318-541 |
8.03e-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: 39.44 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 318 LLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKL----VDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEME--- 390
Cdd:pfam12128 273 LIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpsw 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 391 --------------ETDKEQLTAEAKELRQKVRY-LQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGS 455
Cdd:pfam12128 353 qselenleerlkalTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 456 PEGVGGHLRKQELVTQNELLKQQVKIFEEDF-QRERSDR--ERMNEEKEELKKQVEKLQAQVTltnaQLKTLKeeEKAKE 532
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATATPELLlQLENFDEriERAREEQEAANAEVERLQSELR----QARKRR--DQASE 506
|
....*....
gi 755539259 533 ALKQQKRKA 541
Cdd:pfam12128 507 ALRQASRRL 515
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
305-440 |
8.59e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.29 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 305 EAGAfgaaekKVKL--------LEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAeREQKQRDF 376
Cdd:COG0542 397 EAAA------RVRMeidskpeeLDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKEL 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 377 DRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEE 438
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEE 545
|
..
gi 755539259 439 AL 440
Cdd:COG0542 546 EL 547
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
346-521 |
8.76e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 346 QKITELRQKLVDLQKQVTELEAEREqkqrDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQ 425
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERERE----ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 426 EKEIQrlnkalEEALSIQASPSSPPAAFGSPEgvgghlrkqELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKK 505
Cdd:PRK02224 327 RDRLE------ECRVAAQAHNEEAESLREDAD---------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
170
....*....|....*.
gi 755539259 506 QVEKLQAQVTLTNAQL 521
Cdd:PRK02224 392 EIEELRERFGDAPVDL 407
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
328-438 |
9.95e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 36.79 E-value: 9.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755539259 328 EVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQK 407
Cdd:pfam03938 19 AAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKK---------------------EQELQQL 77
|
90 100 110
....*....|....*....|....*....|.
gi 755539259 408 VRYLQDQLSplTRQREYQEKEIQRLNKALEE 438
Cdd:pfam03938 78 QQKAQQELQ--KKQQELLQPIQDKINKAIKE 106
|
|
| |
