|
Name |
Accession |
Description |
Interval |
E-value |
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
346-547 |
1.08e-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: 67.10 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 346 QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQ 425
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 426 EKEIQRLNKALEEAL--SIQASPSSPPAAFGSPEGVGGHLR----------------------KQELVTQNELLKQQVKI 481
Cdd:COG4942 96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRrlqylkylaparreqaeelradLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568975051 482 FEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 547
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-543 |
5.02e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 311 AAEKKVKLleQQRMELLEVNKQW--DQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDR---------- 378
Cdd:COG1196 211 KAERYREL--KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 379 KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspeg 458
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 459 vgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQK 538
Cdd:COG1196 359 ----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
....*
gi 568975051 539 RKAKA 543
Cdd:COG1196 435 EEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
345-543 |
1.23e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 345 EQKITELRQKLVDLQKQVTELEAEREQ-------KQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSP 417
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 418 LTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMN 497
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568975051 498 EEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKA 543
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-542 |
6.30e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 311 AAEKKVKLLEQQRMEL-LEVNKQWDQHFRSMKQ--QYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdRKLLLAKSKI 387
Cdd:COG1196 264 ELEAELEELRLELEELeLELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELE----EELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 388 EMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAspssppaafgspegvgghlrkQE 467
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA---------------------EL 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975051 468 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAK 542
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-541 |
3.36e-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: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 348 ITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEK 427
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 428 EIQRLNKALEEALSIQASPSSPPAAFGSpegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 507
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQ--------QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190
....*....|....*....|....*....|....
gi 568975051 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 |
1.00e-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: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 313 EKKVKLLEQQRMELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLVDLQKQVTELEAERE----QKQRDFDRKLll 382
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 383 aKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspEGVGGH 462
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK--------ENQSYK 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 463 LRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKE 532
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
213-511 |
1.69e-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: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 213 KNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGAGKKGVAG 292
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 293 QQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQY------------------------EQKI 348
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerleslerriaatERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 349 TELRQKLVDLQKQVTELEAEREQKQRDFDR------KLLLAKSKIEME----ETDKEQLTAEAKELRQKVRYLQDQLSPL 418
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEEleseleALLNERASLEEAlallRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 419 TRQRE-YQEK------EIQRLNKALEEALSI--QASPSSPPAAFGSPEGVGGHLRKqelvtqnelLKQQVKIF------- 482
Cdd:TIGR02168 921 REKLAqLELRleglevRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRRLKR---------LENKIKELgpvnlaa 991
|
330 340
....*....|....*....|....*....
gi 568975051 483 EEDFQRERSDRERMNEEKEELKKQVEKLQ 511
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
226-557 |
1.70e-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: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 226 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnssckeglcgqpsspkpegagKKGVAGQQQASVMASKVpe 305
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----------------------RKELEELSRQISALRKD-- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 306 agaFGAAEKKVKLLEQQRMELLEVNKQwdqhfrsmkqqYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKS 385
Cdd:TIGR02168 735 ---LARLEAEVEQLEERIAQLSKELTE-----------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 386 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEgvgghlrk 465
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI-------- 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 466 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASG 545
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
330
....*....|..
gi 568975051 546 ERYHMEPHPEHV 557
Cdd:TIGR02168 949 YSLTLEEAEALE 960
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
206-560 |
1.94e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 206 RLASKVHKNEQRTSILQTLcEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLmnssckeglcgqpsspkpega 285
Cdd:COG1196 226 EAELLLLKLRELEAELEEL-EAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 286 gkkGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWdqhfrsmkqqyEQKITELRQKLVDLQKQVTEL 365
Cdd:COG1196 284 ---EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-----------EEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 366 EAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAs 445
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 446 pssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 525
Cdd:COG1196 429 ------------------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330 340 350
....*....|....*....|....*....|....*
gi 568975051 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 |
2.74e-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: 54.93 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 342 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQ 421
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 422 REYQ--EKEIQRLNKAL----EEALSIQAspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDREr 495
Cdd:COG1579 89 KEYEalQKEIESLKRRIsdleDEILELME-------------------RIEELEEELAELEAELAELEAELEEKKAELD- 148
|
170
....*....|....*...
gi 568975051 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 |
1.16e-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: 1.16e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568975051 465 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 513
Cdd:cd09803 34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
340-549 |
1.43e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 340 MKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS 416
Cdd:COG4913 247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 417 PLTRQREYQ--------EKEIQRLNKALEEalsiqaspssppaafgspegvgghlRKQELVTQNELLKQ---QVKIFEED 485
Cdd:COG4913 327 ELEAQIRGNggdrleqlEREIERLERELEE-------------------------RERRRARLEALLAAlglPLPASAEE 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975051 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 |
1.84e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.69 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 345 EQKITELRQKLVDLQKQVTELEAEREQKQRDfdRKLLLAKSKIEMEEtdkeqLTAEAKELRQKVRYLQDQLSPLTRQREY 424
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYE-----LLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 425 QEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFE---EDFQRER----SDRERMN 497
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErelEDAEERLakleAEIDKLL 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568975051 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 |
2.51e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 342 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVRYLQDQLSPLTRQ 421
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEEL-----------EEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 422 REYQEKEIQRLNKALEEALSIQASPSSppaafgspEGVGGHLRKQELVTQNELLKQQVKIFEEDFQrerSDRERMNEEKE 501
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEE--------RLEEAEEELAEAEAEIEELEAQIEQLKEELK---ALREALDELRA 810
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 568975051 502 ELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERY 548
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
341-547 |
4.59e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 4.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 341 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSplTR 420
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 421 QREYQEKeiQRLNKALEEALSiqaspSSPPAAFgspegvgghLRKQELVT-----QNELLKQQ---VKIFEEDFQRERSD 492
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLG-----SESFSDF---------LDRLSALSkiadaDADLLEELkadKAELEAKKAELEAK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568975051 493 RERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 547
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
334-548 |
1.32e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 334 DQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQ-KQR----DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKV 408
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 409 RYLQDQL--SPLTRQREYQEKEIQRLNKALEEA------LSIQASPSSPPAafgspegvgghlrkQELVTQNELLKQQVK 480
Cdd:COG3206 243 AALRAQLgsGPDALPELLQSPVIQQLRAQLAELeaelaeLSARYTPNHPDV--------------IALRAQIAALRAQLQ 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568975051 481 ifeedfQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKakeALKQQKRKAKASGERY 548
Cdd:COG3206 309 ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA---ELRRLEREVEVARELY 367
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
166-441 |
2.54e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 166 EDSNLKLHLQRLETTLSVCAEEpdHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQ 245
Cdd:COG1196 233 KLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 246 RDLAAERLREENTELKKLlmnssckeglcgqpsspkpegAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRME 325
Cdd:COG1196 311 RRELEERLEELEEELAEL---------------------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 326 LLEVNKQWDQHFRSMKQQY---EQKITELRQKLVDLQKQVTELE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTA 399
Cdd:COG1196 370 AEAELAEAEEELEELAEELleaLRAAAELAAQLEELEEAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568975051 400 EAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 441
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
206-547 |
2.57e-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: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 206 RLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGA 285
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 286 GKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNkqwdqhfRSMKQQYEQKITELRQKLVDLQKQVTEL 365
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-------KSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 366 EAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAS 445
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 446 PSSPpaafgspegvgGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 525
Cdd:pfam02463 407 AQLL-----------LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|..
gi 568975051 526 EEEKAKEALKQQKRKAKASGER 547
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEE 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-511 |
3.10e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 301 SKVPE-AGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMK------QQYEQKITELRQKLVDLQKQVTELE-----AE 368
Cdd:PRK03918 214 SELPElREELEKLEKEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVKELKelkekAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 369 REQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLN---KALEEALSIQAS 445
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEE 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568975051 446 PSSPPAAFGSpegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQ 511
Cdd:PRK03918 374 LERLKKRLTG-------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
211-529 |
3.29e-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: 50.50 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 211 VHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLcgqpsspKPEGAGKKGV 290
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL-------KLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 291 AG--QQQASVMASKVPEAG-AFGAAEKKVKLLEQQ----RMELlevnkqwdQHFRSMKQQYEQKITELRQKLVDLQKQVT 363
Cdd:pfam15921 564 IEilRQQIENMTQLVGQHGrTAGAMQVEKAQLEKEindrRLEL--------QEFKILKDKKDAKIRELEARVSDLELEKV 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 364 ELEAEREQKQRdfdrklllAKSKIEMEetdKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEAL-SI 442
Cdd:pfam15921 636 KLVNAGSERLR--------AVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLkSA 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 443 QASPSSPPAAFGSPEGVGGHLRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 513
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQItakrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
330
....*....|....*.
gi 568975051 514 VTLTNAQLKTLKEEEK 529
Cdd:pfam15921 785 KNKMAGELEVLRSQER 800
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
197-507 |
6.05e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 197 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLD---KGLEQRDLAAERLREENTELKKLLMNSsckegl 273
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSHS------ 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 274 cgqpssPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQ---KITE 350
Cdd:TIGR02169 792 ------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 351 LRQKLVDLQKQVTELEAEREQKQRDFDR---KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS---PLTRQREY 424
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEE 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 425 QEKEIQRLNKALEEALSIQASPSS-PPAAFGSPEGVgghlrKQELVTQNELLKQQVKIFEEdfqreRSDRERMNEEKEEL 503
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRAlEPVNMLAIQEY-----EEVLKRLDELKEKRAKLEEE-----RKAILERIEEYEKK 1015
|
....
gi 568975051 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 |
8.75e-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: 8.75e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 568975051 473 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 515
Cdd:pfam16516 55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-547 |
9.12e-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: 48.91 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 182 SVCAEEPDHSQLFTH-LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTEL 260
Cdd:TIGR02169 667 LFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 261 kkllmnSSCKEGLcgqpSSPKPEGAGKKGVAGQQQASvmaskvpeagafgAAEKKVKLLEQQRMELLEVNKQWDQHFRSM 340
Cdd:TIGR02169 747 ------SSLEQEI----ENVKSELKELEARIEELEED-------------LHKLEEALNDLEARLSHSRIPEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 341 KQQY---EQKITELRQKLVDLQKQVTELEAEREQKQ---RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQ 414
Cdd:TIGR02169 804 EEEVsriEARLREIEQKLNRLTLEKEYLEKEIQELQeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 415 LSPLTRQREYQEKEIQRLNKALEEaLSIQASPSsppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRE 494
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEE-LEAQIEKK--------------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568975051 495 RMNEEkEELKKQVEKLQAQV-TLTNAQLKTLKEEEKAKEALKQ-QKRKAKASGER 547
Cdd:TIGR02169 949 EELSL-EDVQAELQRVEEEIrALEPVNMLAIQEYEEVLKRLDElKEKRAKLEEER 1002
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-513 |
9.26e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 312 AEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQkITELRQKLVDLQKQ------VTELEAEREQKQRDFDRkLLLAKS 385
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYswdeidVASAEREIAELEAELER-LDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 386 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAafgspegvgghlrk 465
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL-------------- 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568975051 466 qELVTQNELLKQQVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQ 513
Cdd:COG4913 752 -EERFAAALGDAVERELRENLEER---IDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-545 |
9.39e-06 |
|
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: 48.22 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 311 AAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQ---YEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLA---- 383
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyrlg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 384 ---KSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREyqekEIQRLNKALEEALSIQASpssppaafgspegvg 460
Cdd:COG4942 118 rqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEA--------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 461 ghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQaqvtltnAQLKTLKEEEKAKEALKQQKRK 540
Cdd:COG4942 179 ---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAAAAERTPAAGF 248
|
....*
gi 568975051 541 AKASG 545
Cdd:COG4942 249 AALKG 253
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-542 |
9.64e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.86 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 313 EKKVKLLEQQRMELlevnkqwdQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEET 392
Cdd:TIGR04523 186 QKNIDKIKNKLLKL--------ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 393 DKEQLTAEAKELRQKVRYLQD---QLSPLTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspEGVGGHLRKQE-- 467
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKEQDWN---------------KELKSELKNQEkk 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 468 -LVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQvtlTNAQLKTLKEEEKAKEALKQQ 537
Cdd:TIGR04523 323 lEEIQNQIsqnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEIKNLESQINDLESK 399
|
....*
gi 568975051 538 KRKAK 542
Cdd:TIGR04523 400 IQNQE 404
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
204-543 |
1.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 204 FNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENtELKKLLMNSSCKeglcGQPSSPKPE 283
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKK----ADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 284 GAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEvnkqwdqhfrsMKQQYEQKITELRQKLVDLQKQVT 363
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-----------KKAEEKKKADEAKKKAEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 364 ELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRylQDQLSPLTRQREYQEKEIQRLNKALEEALSIQ 443
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE--EAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 444 ASPSSPPAAfgspegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK---EELKKQVEKLQAQVTLTNAQ 520
Cdd:PTZ00121 1487 EAKKKAEEA----------KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADELKKAEE 1556
|
330 340
....*....|....*....|...
gi 568975051 521 LKTLKEEEKAKEALKQQKRKAKA 543
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMA 1579
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
202-514 |
2.56e-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: 47.76 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 202 LEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnssckeglcgqpsspk 281
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------------------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 282 peGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMEL-LEVNKQwdqhfRSMKQQYEQKITELRQKLVDLQK 360
Cdd:TIGR02169 285 --GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLeAEIDKL-----LAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 361 QVTELEAEREQKQRDF---DRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLN---K 434
Cdd:TIGR02169 358 EYAELKEELEDLRAELeevDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEakiN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 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 |
2.95e-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: 47.43 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 313 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQklvdlqkqvtELEAEREQKQRDFDRKLLLAKSKIEMEET 392
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 393 DKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQEL---- 468
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 469 -----------VTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKkqveKLQAQVTLTNAQLKTLKEEEKAKEALKQQ 537
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR----RIQEQMRKATEERSRLEAMEREREMMRQI 581
|
....*....
gi 568975051 538 KRKAKASGE 546
Cdd:pfam17380 582 VESEKARAE 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
199-551 |
3.78e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 199 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRQENEALK-AKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQP 277
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 278 SSPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEK-----KVKLLEQQRMEllEVNKQWDQHFRSMKQQYEQKITELR 352
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 353 QKLVDLQKQVTELEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEI 429
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 430 QRLNKALEEalsiqaspssppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEK 509
Cdd:PTZ00121 1678 EEAKKAEED-----------------------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568975051 510 LQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERYHME 551
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
341-507 |
4.05e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 341 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEmEETdkEQLTAEAKELRQKVRYLQDQLSPLTR 420
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-QAI--KEAKKEADEIIKELRQLQKGGYASVK 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 421 QREYQEKeIQRLNKALEEALSIQASPSSPPAAFgspeGVGGHLR---------------KQELVTQNELLKQQVKIfeed 485
Cdd:PRK00409 606 AHELIEA-RKRLNKANEKKEKKKKKQKEKQEEL----KVGDEVKylslgqkgevlsipdDKEAIVQAGIMKMKVPL---- 676
|
170 180
....*....|....*....|..
gi 568975051 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 |
5.64e-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: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 313 EKKVKLLEQQRMELLEVNKQwdqhfrsmKQQYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdrklllakSKIEMEET 392
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 393 DKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKaleealsiqaspssppaafgspegvgghlRKQELVTQN 472
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN-----------------------------TRESLETQL 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568975051 473 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRK 540
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
318-527 |
5.82e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 318 LLEQQRMELLEVNKQWDQhfrsmKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKE 395
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-----KEEKDlhERLNGLESELAELDEEIERYEEQREQARETRDE----ADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 396 QLTaeakELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEaLSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELL 475
Cdd:PRK02224 252 ELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568975051 476 KQ-------QVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEE 527
Cdd:PRK02224 327 RDrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
335-526 |
5.87e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 335 QHFRSMKQQY-EQKIteLRQKLVDLQKQVTELEaEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQD 413
Cdd:PRK04863 496 DVARELLRRLrEQRH--LAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 414 QLSPLTRQREYQEKEIQRLnKALEEALSIQASP--SSPPAAFGSPEGVGGHLRKQELVTQnelLKQQVKIFEEDFQRErs 491
Cdd:PRK04863 573 SVSEARERRMALRQQLEQL-QARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTE---YMQQLLERERELTVE-- 646
|
170 180 190
....*....|....*....|....*....|....*
gi 568975051 492 dRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKE 526
Cdd:PRK04863 647 -RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
311-543 |
6.11e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 311 AAEKKVKLLEQQRMELLEVNKQWDQhFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQ-------RDFDRKLLLA 383
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 384 KSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLnkALEEALSIQASPSSPPAAFGSPEGVGGhL 463
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL--IAAALLALLGLGGSLLSLILTIAGVLF-L 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 464 RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKA 543
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
340-548 |
9.08e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 340 MKQQYEQKITELRQKLVDLQKQVTELEAEREQkqrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLT 419
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 420 R-------QREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSD 492
Cdd:pfam02463 241 LlqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568975051 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 |
9.78e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 203 EFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLmnsSCKEGLcgqpsspkp 282
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK---EELESL--------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 283 egagkkgvagQQQASVMASKVPEAGAfgAAEKKVKLLEQQRMELLEVNKQwdqhfrsmKQQYEQKITELRQKLVDLQKQV 362
Cdd:TIGR02168 357 ----------EAELEELEAELEELES--RLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 363 TELEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 441
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
..
gi 568975051 442 IQ 443
Cdd:TIGR02168 497 LQ 498
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
227-264 |
9.96e-05 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 44.58 E-value: 9.96e-05
10 20 30
....*....|....*....|....*....|....*...
gi 568975051 227 QLRQENEALKAKLDKgLEQRDLAAERLREENTELKKLL 264
Cdd:PRK13922 73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
302-445 |
1.82e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 302 KVPEAGAFGAAEKKVKLLEQQRME--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQ 373
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975051 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 |
1.94e-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: 44.72 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 321 QQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQR------DFDRKLLLAKSKIEME-ETD 393
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 394 KEQltaeAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQASpssppaafgspegvgGHLRKQELVTQNE 473
Cdd:pfam15921 397 KEQ----NKRLWDRDTGNSITIDHLRRELDDRNMEVQRL-EALLKAMKSECQ---------------GQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 474 llkqqvkifEEDFQRERSDRERMNEEKEELKKQVEKLQA-QVTLTNAQ------LKTLKEEEKAKEALKQQKRKAKAS-- 544
Cdd:pfam15921 457 ---------NESLEKVSSLTAQLESTKEMLRKVVEELTAkKMTLESSErtvsdlTASLQEKERAIEATNAEITKLRSRvd 527
|
250
....*....|....*.
gi 568975051 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 |
2.20e-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: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 313 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQY---EQKITELRQKLVDLQKQVTELEAE---------------REQKQR 374
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldntrESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 375 DFDRKLLLAKSKIEMEETDKE---------QLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKAL----EEALS 441
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKElkskekelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdleDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 442 IQASPSsppaaFGSPEGVGGHLRKQ--EL-VTQNELLKQQVKIFEEDFQRErsdrermnEEKEELKKQVEKLQAQVTLTN 518
Cdd:TIGR04523 550 DDFELK-----KENLEKEIDEKNKEieELkQTQKSLKKKQEEKQELIDQKE--------KEKKDLIKEIEEKEKKISSLE 616
|
250
....*....|....*..
gi 568975051 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 |
2.22e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 168 SNLKLHLQRLETTLSVCAEEPDHSQLfthlgrmalEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRD 247
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSK---------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 248 LAAERLREENTELKKLLMNSSCKEGLCGQpSSPKPEGAGKKGVAGQQQASVMASKVpeAGAFGAAEKKVKLLEQQRMELL 327
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 328 EVNKQWDQHFRSMK-------------QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKL--LLAKSKIEMEE- 391
Cdd:TIGR02168 877 ALLNERASLEEALAllrseleelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEa 956
|
250 260
....*....|....*....|....*...
gi 568975051 392 -TDKEQLTAEAKELRQKVRYLQDQLSPL 418
Cdd:TIGR02168 957 eALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
226-500 |
3.33e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 226 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKegLCGQPSSPKPEGAGKkgvagQQQASVMASKVPE 305
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK--LYEEEKKMKAEEAKK-----AEEAKIKAEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 306 AGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKqvtelEAEREQKQRDFDRKLLLAKS 385
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK-----AEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 386 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQaspssppaafgspegvggHLRK 465
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA------------------HLKK 1764
|
250 260 270
....*....|....*....|....*....|....*
gi 568975051 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 568975051 312 AEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFdRKLLLAKSKIEMEe 391
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAKIKSK- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 392 tdKEQLTAEAKELRQ----------------KVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQaspssppaafgs 455
Cdd:PHA02562 271 --IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS------------ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 456 pegvgghLRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKealk 535
Cdd:PHA02562 337 -------KKLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI---- 391
|
250
....*....|....
gi 568975051 536 qQKRKAKASGERYH 549
Cdd:PHA02562 392 -VKTKSELVKEKYH 404
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
334-449 |
5.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 334 DQHFRSMKQQY---EQKITELRQKL-------VDLQKQVTELEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKE 403
Cdd:COG3206 262 SPVIQQLRAQLaelEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQ 338
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568975051 404 LRQKVRYL---QDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSP 449
Cdd:COG3206 339 LEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
165-547 |
6.42e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 165 PEDSNLKLHLQRLETTLSVC---AEEPDHSQ----LFTHLGRMALEFNRLASKVHKNEQRTSILQTLceQLRQENEALKA 237
Cdd:PRK04863 223 PENSGVRKAFQDMEAALRENrmtLEAIRVTQsdrdLFKHLITESTNYVAADYMRHANERRVHLEEAL--ELRRELYTSRR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 238 KLDKglEQRDLaaERLREENTELKKllmnsscKEGLCGQPSspkpegagkkgvagqQQASVMASKVPEAGAF-------- 309
Cdd:PRK04863 301 QLAA--EQYRL--VEMARELAELNE-------AESDLEQDY---------------QAASDHLNLVQTALRQqekieryq 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 310 GAAEKKVKLLEQQRMELLEVNKQWDQHfRSMKQQYEQKITELRQKLVDLQKQVTELEA---EREQKQRDFDR-KLLLAKS 385
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEEN-EARAEAAEEEVDELKSQLADYQQALDVQQTraiQYQQAVQALERaKQLCGLP 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 386 KIEMEETDK--EQLTAEAKELRQKVRYLQDQLSPLTRQREYQEK----------EIQRlNKALEEALS-IQASPSSPPAA 452
Cdd:PRK04863 434 DLTADNAEDwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagEVSR-SEAWDVARElLRRLREQRHLA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 453 fGSPEGVGGHLR--KQELVTQ---NELLKQQVKIF------EEDFQRERSDRErmnEEKEELKKQVEKLQAQVTLTNAQL 521
Cdd:PRK04863 513 -EQLQQLRMRLSelEQRLRQQqraERLLAEFCKRLgknlddEDELEQLQEELE---ARLESLSESVSEARERRMALRQQL 588
|
410 420
....*....|....*....|....*.
gi 568975051 522 KTLKEEEKAKEALKQQKRKAKASGER 547
Cdd:PRK04863 589 EQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
446-544 |
7.22e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 446 PSSPPAAFGSPEGVGGHLrkQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 525
Cdd:PRK11448 127 WDFKPGPFVPPEDPENLL--HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ 204
|
90
....*....|....*....
gi 568975051 526 EEEKAKEALKQQKRKAKAS 544
Cdd:PRK11448 205 EKAAETSQERKQKRKEITD 223
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
345-542 |
7.83e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 345 EQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREY 424
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 425 QEKEIQRLNKALEEALSIQ--------------------------ASPSSPPAAFGSPEG--------VGGHLRKQELVT 470
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKgkcpvcgrelteehrkelleeytaelKRIEKELKEIEEKERklrkelreLEKVLKKESELI 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975051 471 QNELLKQQVKIFEEDFQR-ERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAK 542
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
315-397 |
7.87e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 315 KVKLLEQQRMELLEVNKQWDQHFRSMKQ----------QYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllAK 384
Cdd:PRK11448 150 EVLTLKQQLELQAREKAQSQALAEAQQQelvaleglaaELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQ---AA 226
|
90
....*....|...
gi 568975051 385 SKIEMEETDKEQL 397
Cdd:PRK11448 227 KRLELSEEETRIL 239
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
321-538 |
1.03e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 321 QQRMELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLVDLQKQVTELEAEREQKQRDfdrkllLAKSKIEMEETDK 394
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 395 EQL-TAEAKELRQKVRYLQDQL-----------SPLTRQREYQE----------KEIQRLNKALeEALSIQASPSSPPaa 452
Cdd:PRK11281 116 ETLsTLSLRQLESRLAQTLDQLqnaqndlaeynSQLVSLQTQPEraqaalyansQRLQQIRNLL-KGGKVGGKALRPS-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 453 fgspegvgghlRKQELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQaqvTLTNAq 520
Cdd:PRK11281 193 -----------QRVLLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQ---EAINS- 252
|
250
....*....|....*....
gi 568975051 521 lKTLKE-EEKAKEALKQQK 538
Cdd:PRK11281 253 -KRLTLsEKTVQEAQSQDE 270
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
338-439 |
1.12e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 338 RSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllaKSKIEMEEtdkEQLTAEAKELRQKVRylqdqlsp 417
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIERLE---RELSEARSEERREIR-------- 462
|
90 100
....*....|....*....|....
gi 568975051 418 ltRQREYQ--EKEIQRLNKALEEA 439
Cdd:COG2433 463 --KDREISrlDREIERLERELEEE 484
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-540 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 313 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLqKQVTELEAEREQKQRDFDRKLLLAKSKIEMEET 392
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 393 DKEQLTAEAKELRQKVRYLQDQLSpltrqREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvggHLRKQELVTQN 472
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEEL----------------------KQTQKSLKKKQ 584
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568975051 473 ELLKQQVKIFEEDFQRERSDRE-------RMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKA-KEALKQQKRK 540
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQiKETIKEIRNK 660
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
311-412 |
1.17e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 311 AAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRkLLLAKSKiEME 390
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
|
90 100
....*....|....*....|..
gi 568975051 391 ETDKEQLTAEAKELRQKVRYLQ 412
Cdd:cd16269 270 ALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
311-412 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 311 AAEKKVKLLEQQRMELlevnkqwDQHFRSMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRklLLAKSKIEME 390
Cdd:pfam02841 215 AAEAEQELLREKQKEE-------EQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER--MLEHKLQEQE 275
|
90 100
....*....|....*....|..
gi 568975051 391 ETDKEQLTAEAKELRQKVRYLQ 412
Cdd:pfam02841 276 ELLKEGFKTEAESLQKEIQDLK 297
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
327-543 |
1.48e-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: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 327 LEVNKQwdqhfrSMKQQYEQKIT------ELRQKLvdLQKQVTELEAER--EQKQRDfdrKLLLAKSKIEMEETDKE-QL 397
Cdd:pfam01576 718 LEVNMQ------ALKAQFERDLQardeqgEEKRRQ--LVKQVRELEAELedERKQRA---QAVAAKKKLELDLKELEaQI 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 398 TAEAK---ELRQKVRYLQDQLSPLTRQRE----------YQEKEIQRLNKALE-EALSIQASPSSPPAAFG--------- 454
Cdd:pfam01576 787 DAANKgreEAVKQLKKLQAQMKDLQRELEearasrdeilAQSKESEKKLKNLEaELLQLQEDLAASERARRqaqqerdel 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 455 SPEGVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTltnAQLKTLKEEEKAKEAL 534
Cdd:pfam01576 867 ADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA---AERSTSQKSESARQQL 943
|
....*....
gi 568975051 535 KQQKRKAKA 543
Cdd:pfam01576 944 ERQNKELKA 952
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
299-526 |
1.67e-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: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 299 MASKVPEAGAFGAAEkkvklleqqrmELLEvnkqwdqHFRSMKQQYEQkITELRQKLVDLQKQVTELEAEREQkQRDFDR 378
Cdd:COG3096 484 IAGEVERSQAWQTAR-----------ELLR-------RYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERL-LEEFCQ 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 379 KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNK------ALEEALSIQASPSSppAA 452
Cdd:COG3096 544 RIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSG--EA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568975051 453 FGSPEGVGGHLrkqelvtqnellkQQVKIFEEDFQRERsdrERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKE 526
Cdd:COG3096 622 LADSQEVTAAM-------------QQLLEREREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
197-555 |
1.79e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 197 LGRMALEFNRLASKVHKNE---QRTSILQTLCEQLRQENEALK-AKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEG 272
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAaakKKADEAKKKAEEKKKADEAKKkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 273 LCGQPSSPKPEGAGKKGVAGQQQASVMASKvpeAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELR 352
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKA---AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 353 qKLVDLQKqvTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLspltRQREYQEKEIQRL 432
Cdd:PTZ00121 1553 -KAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 433 NKALEEALSIQASPSSPPAAFGSPEgvggHLRKQElvTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQA 512
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAE----ELKKAE--EENKIKAAEEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568975051 513 QVTLTNAQLKTLKEEEKAK-EALKQQKRKAKASGERYHMEPHPE 555
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKaEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
321-526 |
2.22e-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: 41.35 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 321 QQRMELLEvNKQWD--QHFRSMKQQYEQKitelRQKLVDLQKQVTELEAEREQKQRDFDRKlllAKSKIEMEEtDKEQLT 398
Cdd:pfam10174 309 QTKLETLT-NQNSDckQHIEVLKESLTAK----EQRAAILQTEVDALRLRLEEKESFLNKK---TKQLQDLTE-EKSTLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 399 AEAKELRQ-------KVRYLQDQLSPLTRQREYQEKEIQRLNKALEealSIQASPSSPPAAfgspegvgghlrkqeLVTQ 471
Cdd:pfam10174 380 GEIRDLKDmldvkerKINVLQKKIENLQEQLRDKDKQLAGLKERVK---SLQTDSSNTDTA---------------LTTL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975051 472 NELLKQQVKIFEE-DFQRERSDRERMNE------EKEELKKQVEKLQAQVTLTNAQLKTLKE 526
Cdd:pfam10174 442 EEALSEKERIIERlKEQREREDRERLEEleslkkENKDLKEKVSALQPELTEKESSLIDLKE 503
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
206-513 |
2.99e-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: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 206 RLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGA 285
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 286 GKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTEL 365
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 366 EAEREQKQRDFDRKLLLAKSKI---EMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 442
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLkdeLESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975051 443 QASPSSPPAAFGSPE----GVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 513
Cdd:pfam02463 943 EEADEKEKEENNKEEeeerNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
315-437 |
2.99e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 40.29 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 315 KVKLLEQQRMELLEVNKQWDQHF----RSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEME 390
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568975051 391 ETDKEQLTAEAKELRQkvrylqdQLSPLTRQREYQEKEIQRLNKALE 437
Cdd:pfam00038 95 LNLRTSAENDLVGLRK-------DLDEATLARVDLEAKIESLKEELA 134
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
342-521 |
3.07e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 342 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVRYLQDqlSP- 417
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSARYTPN--HPd 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 418 ---LTRQREYQEKEIQRLNKALEEALSIQASpssppaafgspegvGGHLRKQELVTQNELLKQQVKIFEEDfQRERSDRE 494
Cdd:COG3206 293 viaLRAQIAALRAQLQQEAQRILASLEAELE--------------ALQAREASLQAQLAQLEARLAELPEL-EAELRRLE 357
|
170 180 190
....*....|....*....|....*....|...
gi 568975051 495 RMNEEKEE-----LKKQVE-KLQAQVTLTNAQL 521
Cdd:COG3206 358 REVEVARElyeslLQRLEEaRLAEALTVGNVRV 390
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
328-438 |
3.55e-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: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 328 EVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTEL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 406
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
|
90 100 110
....*....|....*....|....*....|..
gi 568975051 407 KVRYLQDQLSplTRQREYQEKEIQRLNKALEE 438
Cdd:smart00935 77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
345-514 |
3.60e-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: 40.20 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 345 EQKITELRQK------LVD----LQKQVTELEAEREQ---KQRDFDRKL-----LLAKSKIEMEET--DKEQLTAEAKEL 404
Cdd:pfam15066 345 EKKVKELQMKitkqqvFVDiinkLKENVEELIEDKYNvilEKNDINKTLqnlqeILANTQKHLQESrkEKETLQLELKKI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 405 rqKVRYLQDQLSPLTrqreyqekEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKqelVTQN--ELLKQQVKIF 482
Cdd:pfam15066 425 --KVNYVHLQERYIT--------EMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEK---ATTSalDLLKREKETR 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 568975051 483 EEDF---QRERSDRERMN-EEKEELKKQVEKLQAQV 514
Cdd:pfam15066 492 EQEFlslQEEFQKHEKENlEERQKLKSRLEKLVAQV 527
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
221-534 |
4.21e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 221 LQTLCEQLRQENEALKAKLdkgleqRDLAAERLREENT--ELKKLLMNSSCKEglCGQP--SSPKPEGAGKKGV------ 290
Cdd:PRK02224 410 AEDFLEELREERDELRERE------AELEATLRTARERveEAEALLEAGKCPE--CGQPveGSPHVETIEEDRErveele 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 291 -----AGQQQASVmASKVPEAGAFGAAEKKVKLLEQQRMELLEvnkqwdqhfrsMKQQYEQKITELRQKLVDLQKQVTEL 365
Cdd:PRK02224 482 aeledLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEE-----------LIAERRETIEEKRERAEELRERAAEL 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 366 EAEREQKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVRYLQDQLSpltrQREYQEKEIQRLNKALEEALSIQas 445
Cdd:PRK02224 550 EAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLERIRTLLA----AIADAEDEIERLREKREALAELN-- 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 446 pssppaafgspegvggHLRKQELVTQNELLKQQVKIFEED-FQRERSDRER-------MNEEKEELKKQVEKLQAQVTLT 517
Cdd:PRK02224 623 ----------------DERRERLAEKRERKRELEAEFDEArIEEAREDKERaeeyleqVEEKLDELREERDDLQAEIGAV 686
|
330
....*....|....*..
gi 568975051 518 NAQLKTLKEEEKAKEAL 534
Cdd:PRK02224 687 ENELEELEELRERREAL 703
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
335-458 |
4.25e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 335 QHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKqrdfdrklllakskiemeETDKEQLTAEAKELRQKVRYLQDQ 414
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQ 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568975051 415 LSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEG 458
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
169-439 |
4.71e-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: 40.34 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 169 NLKLHLQRLETTLSVCAEEpdHSQLFTHLGRMALEFnrLASKVHKNEQRTSILQTLCEQLRQ----ENEALKAKLDKGLE 244
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQE--LALKLTALHALQLTL--TQERVREHALSIRVLPKELLASRQlalqKMQSEKEQLTYWKE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 245 QRDLAAERLREENTELKKllmNSSCKEGLCGQPSSPKPEGAGKKGVAGQQQASVMASkvpeagaFGAAEKKVKLLEQQRM 324
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEE---YDREFNEIENASSSLGSDLAAREDALNQSLKELMHQ-------ARTVLKARTEAHFNNN 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 325 ELLEVNKQWDQHFRSMKQQYEQKITELRQklvdLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKEL 404
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREE----DTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAT 843
|
250 260 270
....*....|....*....|....*....|....*
gi 568975051 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 |
5.63e-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: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 230 QENEALKAKLDKGLEQRDLA---AERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGAGKKGVAGQQQASVMASKVPEA 306
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSArekQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 307 GAFgaAEKKVKLLEQQRMELLEVNKQWDQHF-------RSMKQQYEQKITELRQKLVDLQKQVTELE---AEREQKQRDF 376
Cdd:pfam12128 677 KDS--ANERLNSLEAQLKQLDKKHQAWLEEQkeqkreaRTEKQAYWQVVEGALDAQLALLKAAIAARrsgAKAELKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 377 DRKLLLAK--------SKIEMEETDKEQLTAEAKELRQKV----RYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQA 444
Cdd:pfam12128 755 WYKRDLASlgvdpdviAKLKREIRTLERKIERIAVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLARLI 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 445 SPSSppaafgspegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEElkKQVEKLQAQVTLTNAQLKTL 524
Cdd:pfam12128 835 ADTK--------------LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED--ANSEQAQGSIGERLAQLEDL 898
|
330
....*....|....*....
gi 568975051 525 KEE-EKAKEALKQQKRKAK 542
Cdd:pfam12128 899 KLKrDYLSESVKKYVEHFK 917
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
470-542 |
6.28e-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: 6.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568975051 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 |
6.78e-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: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 397 LTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQASPSSPPAAFGSPEGvgghlRKQELVTQNELL 475
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQLATERS-----ARREAEAELERL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568975051 476 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQvtLTNAQLKTLKEEE 528
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQ--LTSKSQSSSSQSE 167
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
305-440 |
7.63e-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: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 305 EAGAfgaaekKVKL--------LEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAeREQKQRDF 376
Cdd:COG0542 397 EAAA------RVRMeidskpeeLDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKEL 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 377 DRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEE 438
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEE 545
|
..
gi 568975051 439 AL 440
Cdd:COG0542 546 EL 547
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
318-541 |
7.91e-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: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 318 LLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKL----VDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEME--- 390
Cdd:pfam12128 273 LIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpsw 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 391 --------------ETDKEQLTAEAKELRQKVRY-LQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGS 455
Cdd:pfam12128 353 qselenleerlkalTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 456 PEGVGGHLRKQELVTQNELLKQQVKIFEEDF-QRERSDR--ERMNEEKEELKKQVEKLQAQVTltnaQLKTLKeeEKAKE 532
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATATPELLlQLENFDEriERAREEQEAANAEVERLQSELR----QARKRR--DQASE 506
|
....*....
gi 568975051 533 ALKQQKRKA 541
Cdd:pfam12128 507 ALRQASRRL 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
346-521 |
8.70e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 346 QKITELRQKLVDLQKQVTELEAEREqkqrDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQ 425
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERERE----ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 426 EKEIQrlnkalEEALSIQASPSSPPAAFGSPEgvgghlrkqELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKK 505
Cdd:PRK02224 327 RDRLE------ECRVAAQAHNEEAESLREDAD---------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
170
....*....|....*.
gi 568975051 506 QVEKLQAQVTLTNAQL 521
Cdd:PRK02224 392 EIEELRERFGDAPVDL 407
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
312-544 |
9.41e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 312 AEKKVKLLEQQRMELLEVNKQwdqhFRSMKQQYEQKITELRQKLVDLQ---KQVTELEAEREQKQRDFDRKLLL-AKSKI 387
Cdd:pfam01576 129 TEAKIKKLEEDILLLEDQNSK----LSKERKLLEERISEFTSNLAEEEekaKSLSKLKNKHEAMISDLEERLKKeEKGRQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 388 EMEETdKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspegvgghlRKQE 467
Cdd:pfam01576 205 ELEKA-KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA----------------------QKNN 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 468 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQV--TL--TNAQ--LKTLKEEEKA--KEALKQQKR 539
Cdd:pfam01576 262 ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELedTLdtTAAQqeLRSKREQEVTelKKALEEETR 341
|
....*
gi 568975051 540 KAKAS 544
Cdd:pfam01576 342 SHEAQ 346
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
341-514 |
9.44e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 341 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllakskiemeetDKEQLTA--EAKELRQkvryLQDQLSPL 418
Cdd:COG1579 40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK--------------YEEQLGNvrNNKEYEA----LQKEIESL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 419 TRQREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvgghlrKQELVTQNELLKQQVKIFEEDFQRERSDRERMNE 498
Cdd:COG1579 102 KRRISDLEDEILELMERIEEL-------------------------EEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 568975051 499 EKEELKKQVEKLQAQV 514
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
328-438 |
9.59e-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: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 328 EVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQK 407
Cdd:pfam03938 19 AAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKK---------------------EQELQQL 77
|
90 100 110
....*....|....*....|....*....|.
gi 568975051 408 VRYLQDQLSplTRQREYQEKEIQRLNKALEE 438
Cdd:pfam03938 78 QQKAQQELQ--KKQQELLQPIQDKINKAIKE 106
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
321-539 |
9.75e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.11 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 321 QQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAE---REQKQRDFDRKLLLAKSKIEMEETDKEQL 397
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEElrqSREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975051 398 TAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvggHLRKQELVTQNELLKQ 477
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKA----------------------GAQRKEEEAERKQLQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975051 478 QVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKR 539
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR 240
|
|
| |
