|
Name |
Accession |
Description |
Interval |
E-value |
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
293-494 |
1.48e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 293 QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQ 372
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 373 EKEIQRLNKALEEAL--SIQASPSSPPAAFGSPEGVGGHLR----------------------KQELVTQNELLKQQVKI 428
Cdd:COG4942 96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRrlqylkylaparreqaeelradLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568975053 429 FEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 494
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
258-490 |
5.82e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 258 AAEKKVKLleQQRMELLEVNKQW--DQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDR---------- 325
Cdd:COG1196 211 KAERYREL--KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 326 KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspeg 405
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 406 vgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQK 485
Cdd:COG1196 359 ----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
....*
gi 568975053 486 RKAKA 490
Cdd:COG1196 435 EEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
292-490 |
1.36e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 292 EQKITELRQKLVDLQKQVTELEAEREQ-------KQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSP 364
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 365 LTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMN 444
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568975053 445 EEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKA 490
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
258-494 |
7.88e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 258 AAEKKVKLLEQQRMEL-LEVNKQWDQHFRSMKQ--QYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdRKLLLAKSKI 334
Cdd:COG1196 264 ELEAELEELRLELEELeLELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELE----EELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 335 EMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspegvgghlRKQE 414
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----------------------AAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 415 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 494
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
295-488 |
4.07e-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: 59.69 E-value: 4.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 295 ITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEK 374
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 375 EIQRLNKALEEALSIQASPSSPPAAFGSpegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 454
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQ--------QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190
....*....|....*....|....*....|....
gi 568975053 455 EKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKA 488
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-504 |
2.36e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 173 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnssckeglcgqpsspkpegagKKGVAGQQQASVMASKVpe 252
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----------------------RKELEELSRQISALRKD-- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 253 agaFGAAEKKVKLLEQQRMELLEVNKQwdqhfrsmkqqYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKS 332
Cdd:TIGR02168 735 ---LARLEAEVEQLEERIAQLSKELTE-----------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 333 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEgvgghlrk 412
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI-------- 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 413 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASG 492
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
330
....*....|..
gi 568975053 493 ERYHMEPHPEHV 504
Cdd:TIGR02168 949 YSLTLEEAEALE 960
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
153-507 |
2.53e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 153 RLASKVHKNEQRTSILQTLcEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLmnssckeglcgqpsspkpega 232
Cdd:COG1196 226 EAELLLLKLRELEAELEEL-EAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 233 gkkGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWdqhfrsmkqqyEQKITELRQKLVDLQKQVTEL 312
Cdd:COG1196 284 ---EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-----------EEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 313 EAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAs 392
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 393 pssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 472
Cdd:COG1196 429 ------------------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330 340 350
....*....|....*....|....*....|....*
gi 568975053 473 EEEKAKEALKQQKRKAKASGERYHMEPHPEHVCGA 507
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
160-458 |
2.73e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 160 KNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGAGKKGVAG 239
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 240 QQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQY------------------------EQKI 295
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerleslerriaatERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 296 TELRQKLVDLQKQVTELEAEREQKQRDFDR------KLLLAKSKIEME----ETDKEQLTAEAKELRQKVRYLQDQLSPL 365
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEEleseleALLNERASLEEAlallRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 366 TRQRE-YQEK------EIQRLNKALEEALSI--QASPSSPPAAFGSPEGVGGHLRKqelvtqnelLKQQVKIF------- 429
Cdd:TIGR02168 921 REKLAqLELRleglevRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRRLKR---------LENKIKELgpvnlaa 991
|
330 340
....*....|....*....|....*....
gi 568975053 430 EEDFQRERSDRERMNEEKEELKKQVEKLQ 458
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
260-479 |
3.21e-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: 56.57 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 260 EKKVKLLEQQRMELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLVDLQKQVTELEAERE----QKQRDFDRKLll 329
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 330 aKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspEGVGGH 409
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK--------ENQSYK 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 410 LRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKE 479
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
289-460 |
5.34e-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: 54.16 E-value: 5.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 289 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQ 368
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 369 REYQ--EKEIQRLNKAL----EEALSIQAspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDREr 442
Cdd:COG1579 89 KEYEalQKEIESLKRRIsdleDEILELME-------------------RIEELEEELAELEAELAELEAELEEKKAELD- 148
|
170
....*....|....*...
gi 568975053 443 mnEEKEELKKQVEKLQAQ 460
Cdd:COG1579 149 --EELAELEAELEELEAE 164
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
412-460 |
1.99e-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: 48.88 E-value: 1.99e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 568975053 412 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 460
Cdd:cd09803 34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
292-498 |
2.09e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 292 EQKITELRQKLVDLQKQVTELEAEREQKQRDfdRKLLLAKSKIEMEEtdkeqLTAEAKELRQKVRYLQDQLSPLTRQREY 371
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYE-----LLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 372 QEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFE---EDFQRER----SDRERMN 444
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErelEDAEERLakleAEIDKLL 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 568975053 445 EEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERYHME 498
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-496 |
2.19e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 287 MKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS 363
Cdd:COG4913 247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 364 PLTRQREYQ--------EKEIQRLNKALEEalsiqaspssppaafgspegvgghlRKQELVTQNELLKQ---QVKIFEED 432
Cdd:COG4913 327 ELEAQIRGNggdrleqlEREIERLERELEE-------------------------RERRRARLEALLAAlglPLPASAEE 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975053 433 FQRErsdRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEA-LKQQKRKAKASGERYH 496
Cdd:COG4913 382 FAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeIASLERRKSNIPARLL 443
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
289-495 |
3.24e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 289 QQYEQKITELRQKLVDLQKQVTELEAER---EQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPL 365
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 366 TRQREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQrerSDRERMNE 445
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEA----------------------EEELAEAEAEIEELEAQIEQLKEELK---ALREALDE 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 568975053 446 EKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERY 495
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
288-494 |
9.29e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 288 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSplTR 367
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 368 QREYQEKeiQRLNKALEEALSiqaspSSPPAAFgspegvgghLRKQELVT-----QNELLKQQ---VKIFEEDFQRERSD 439
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLG-----SESFSDF---------LDRLSALSkiadaDADLLEELkadKAELEAKKAELEAK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 568975053 440 RERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 494
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
281-495 |
1.75e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.17 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 281 DQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQ-KQR----DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKV 355
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 356 RYLQDQL--SPLTRQREYQEKEIQRLNKALEEA------LSIQASPSSPPAafgspegvgghlrkQELVTQNELLKQQVK 427
Cdd:COG3206 243 AALRAQLgsGPDALPELLQSPVIQQLRAQLAELeaelaeLSARYTPNHPDV--------------IALRAQIAALRAQLQ 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568975053 428 ifeedfQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKakeALKQQKRKAKASGERY 495
Cdd:COG3206 309 ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA---ELRRLEREVEVARELY 367
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-388 |
2.92e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 113 EDSNLKLHLQRLETTLSVCAEEpdHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQ 192
Cdd:COG1196 233 KLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 193 RDLAAERLREENTELKKLlmnssckeglcgqpsspkpegAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRME 272
Cdd:COG1196 311 RRELEERLEELEEELAEL---------------------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 273 LLEVNKQWDQHFRSMKQQY---EQKITELRQKLVDLQKQVTELE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTA 346
Cdd:COG1196 370 AEAELAEAEEELEELAEELleaLRAAAELAAQLEELEEAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 568975053 347 EAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 388
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
248-458 |
3.14e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 248 SKVPE-AGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMK------QQYEQKITELRQKLVDLQKQVTELE-----AE 315
Cdd:PRK03918 214 SELPElREELEKLEKEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVKELKelkekAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 316 REQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLN---KALEEALSIQAS 392
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEE 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568975053 393 PSSPPAAFGSpegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQ 458
Cdd:PRK03918 374 LERLKKRLTG-------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
153-494 |
3.72e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.97 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 153 RLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGA 232
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 233 GKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNkqwdqhfRSMKQQYEQKITELRQKLVDLQKQVTEL 312
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-------KSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 313 EAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAS 392
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 393 PSSPpaafgspegvgGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 472
Cdd:pfam02463 407 AQLL-----------LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|..
gi 568975053 473 EEEKAKEALKQQKRKAKASGER 494
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEE 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-454 |
6.91e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 6.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 144 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLD---KGLEQRDLAAERLREENTELKKLLMNSsckegl 220
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSHS------ 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 221 cgqpssPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQ---KITE 297
Cdd:TIGR02169 792 ------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 298 LRQKLVDLQKQVTELEAEREQKQRDFDR---KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS---PLTRQREY 371
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEE 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 372 QEKEIQRLNKALEEALSIQASPSS-PPAAFGSPEGVgghlrKQELVTQNELLKQQVKIFEEdfqreRSDRERMNEEKEEL 450
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRAlEPVNMLAIQEY-----EEVLKRLDELKEKRAKLEEE-----RKAILERIEEYEKK 1015
|
....
gi 568975053 451 KKQV 454
Cdd:TIGR02169 1016 KREV 1019
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
158-476 |
8.45e-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: 48.96 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 158 VHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLcgqpsspKPEGAGKKGV 237
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL-------KLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 238 AG--QQQASVMASKVPEAG-AFGAAEKKVKLLEQQ----RMELlevnkqwdQHFRSMKQQYEQKITELRQKLVDLQKQVT 310
Cdd:pfam15921 564 IEilRQQIENMTQLVGQHGrTAGAMQVEKAQLEKEindrRLEL--------QEFKILKDKKDAKIRELEARVSDLELEKV 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 311 ELEAEREQKQRdfdrklllAKSKIEMEetdKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEAL-SI 389
Cdd:pfam15921 636 KLVNAGSERLR--------AVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLkSA 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 390 QASPSSPPAAFGSPEGVGGHLRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 460
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQItakrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
330
....*....|....*.
gi 568975053 461 VTLTNAQLKTLKEEEK 476
Cdd:pfam15921 785 KNKMAGELEVLRSQER 800
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
129-494 |
1.05e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 129 SVCAEEPDHSQLFTH-LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTEL 207
Cdd:TIGR02169 667 LFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 208 kkllmnSSCKEGLcgqpSSPKPEGAGKKGVAGQQQASvmaskvpeagafgAAEKKVKLLEQQRMELLEVNKQWDQHFRSM 287
Cdd:TIGR02169 747 ------SSLEQEI----ENVKSELKELEARIEELEED-------------LHKLEEALNDLEARLSHSRIPEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 288 KQQY---EQKITELRQKLVDLQKQVTELEAEREQKQ---RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQ 361
Cdd:TIGR02169 804 EEEVsriEARLREIEQKLNRLTLEKEYLEKEIQELQeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 362 LSPLTRQREYQEKEIQRLNKALEEaLSIQASPSsppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRE 441
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEE-LEAQIEKK--------------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 568975053 442 RMNEEkEELKKQVEKLQAQV-TLTNAQLKTLKEEEKAKEALKQ-QKRKAKASGER 494
Cdd:TIGR02169 949 EELSL-EDVQAELQRVEEEIrALEPVNMLAIQEYEEVLKRLDElKEKRAKLEEER 1002
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
259-460 |
1.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 259 AEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQkITELRQKLVDLQKQ------VTELEAEREQKQRDFDRkLLLAKS 332
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYswdeidVASAEREIAELEAELER-LDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 333 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAafgspegvgghlrk 412
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL-------------- 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568975053 413 qELVTQNELLKQQVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQ 460
Cdd:COG4913 752 -EERFAAALGDAVERELRENLEER---IDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
258-492 |
1.33e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 258 AAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQ---YEQKITELRQKLVDLQKQVTELEAEREQKQRDFDR--------- 325
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 326 -----KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALeealsiqaspssppaaf 400
Cdd:COG4942 118 rqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL----------------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 401 gspegvgghlrkQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQaqvtltnAQLKTLKEEEKAKEA 480
Cdd:COG4942 181 ------------AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAAAAE 241
|
250
....*....|..
gi 568975053 481 LKQQKRKAKASG 492
Cdd:COG4942 242 RTPAAGFAALKG 253
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
420-462 |
1.49e-05 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 43.82 E-value: 1.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 568975053 420 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 462
Cdd:pfam16516 55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-490 |
2.87e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 151 FNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENtELKKLLMNSSCKeglcGQPSSPKPE 230
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKK----ADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 231 GAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEvnkqwdqhfrsMKQQYEQKITELRQKLVDLQKQVT 310
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-----------KKAEEKKKADEAKKKAEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 311 ELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRylQDQLSPLTRQREYQEKEIQRLNKALEEALSIQ 390
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE--EAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 391 ASPSSPPAAfgspegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK---EELKKQVEKLQAQVTLTNAQ 467
Cdd:PTZ00121 1487 EAKKKAEEA----------KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADELKKAEE 1556
|
330 340
....*....|....*....|...
gi 568975053 468 LKTLKEEEKAKEALKQQKRKAKA 490
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMA 1579
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
149-461 |
2.88e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 149 LEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnssckeglcgqpsspk 228
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------------------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 229 peGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMEL-LEVNKQwdqhfRSMKQQYEQKITELRQKLVDLQK 307
Cdd:TIGR02169 285 --GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLeAEIDKL-----LAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 308 QVTELEAEREQKQRDF---DRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLN---K 381
Cdd:TIGR02169 358 EYAELKEELEDLRAELeevDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEakiN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 382 ALEEALsiqaspssppaafgspEGVGGHLRKQElvTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQV 461
Cdd:TIGR02169 438 ELEEEK----------------EDKALEIKKQE--WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
260-489 |
3.31e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 260 EKKVKLLEQQRMELlevnkqwdQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEET 339
Cdd:TIGR04523 186 QKNIDKIKNKLLKL--------ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 340 DKEQLTAEAKELRQKVRYLQD---QLSPLTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspEGVGGHLRKQE-- 414
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKEQDWN---------------KELKSELKNQEkk 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 415 -LVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQvtlTNAQLKTLKEEEKAKEALKQQ 484
Cdd:TIGR04523 323 lEEIQNQIsqnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEIKNLESQINDLESK 399
|
....*
gi 568975053 485 KRKAK 489
Cdd:TIGR04523 400 IQNQE 404
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
288-454 |
3.94e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 288 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEmEETdkEQLTAEAKELRQKVRYLQDQLSPLTR 367
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-QAI--KEAKKEADEIIKELRQLQKGGYASVK 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 368 QREYQEKeIQRLNKALEEALSIQASPSSPPAAFgspeGVGGHLR---------------KQELVTQNELLKQQVKIfeed 432
Cdd:PRK00409 606 AHELIEA-RKRLNKANEKKEKKKKKQKEKQEEL----KVGDEVKylslgqkgevlsipdDKEAIVQAGIMKMKVPL---- 676
|
170 180
....*....|....*....|..
gi 568975053 433 fqrerSDRERMNEEKEELKKQV 454
Cdd:PRK00409 677 -----SDLEKIQKPKKKKKKKP 693
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
260-493 |
5.20e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 260 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQklvdlqkqvtELEAEREQKQRDFDRKLLLAKSKIEMEET 339
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 340 DKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQEL---- 415
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 416 -----------VTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKkqveKLQAQVTLTNAQLKTLKEEEKAKEALKQQ 484
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR----RIQEQMRKATEERSRLEAMEREREMMRQI 581
|
....*....
gi 568975053 485 KRKAKASGE 493
Cdd:pfam17380 582 VESEKARAE 590
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
265-474 |
7.03e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 7.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 265 LLEQQRMELLEVNKQWDQhfrsmKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKE 342
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-----KEEKDlhERLNGLESELAELDEEIERYEEQREQARETRDE----ADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 343 QLTaeakELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEaLSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELL 422
Cdd:PRK02224 252 ELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 568975053 423 KQ-------QVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEE 474
Cdd:PRK02224 327 RDrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
282-473 |
7.51e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 7.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 282 QHFRSMKQQY-EQKIteLRQKLVDLQKQVTELEaEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQD 360
Cdd:PRK04863 496 DVARELLRRLrEQRH--LAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 361 QLSPLTRQREYQEKEIQRLnKALEEALSIQASP--SSPPAAFGSPEGVGGHLRKQELVTQnelLKQQVKIFEEDFQRErs 438
Cdd:PRK04863 573 SVSEARERRMALRQQLEQL-QARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTE---YMQQLLERERELTVE-- 646
|
170 180 190
....*....|....*....|....*....|....*
gi 568975053 439 dRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKE 473
Cdd:PRK04863 647 -RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
258-490 |
8.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 258 AAEKKVKLLEQQRMELLEVNKQWDQhFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQ-------RDFDRKLLLA 330
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 331 KSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLnkALEEALSIQASPSSPPAAFGSPEGVGGhL 410
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL--IAAALLALLGLGGSLLSLILTIAGVLF-L 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 411 RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKA 490
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
146-498 |
8.76e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 146 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRQENEALK-AKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQP 224
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 225 SSPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEK-----KVKLLEQQRMEllEVNKQWDQHFRSMKQQYEQKITELR 299
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 300 QKLVDLQKQVTELEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEI 376
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 377 QRLNKALEEalsiqaspssppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEK 456
Cdd:PTZ00121 1678 EEAKKAEED-----------------------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 568975053 457 LQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERYHME 498
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
174-211 |
8.92e-05 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 44.58 E-value: 8.92e-05
10 20 30
....*....|....*....|....*....|....*...
gi 568975053 174 QLRQENEALKAKLDKgLEQRDLAAERLREENTELKKLL 211
Cdd:PRK13922 73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
150-390 |
1.29e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 150 EFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLmnsSCKEGLcgqpsspkp 229
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK---EELESL--------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 230 egagkkgvagQQQASVMASKVPEAGAfgAAEKKVKLLEQQRMELLEVNKQwdqhfrsmKQQYEQKITELRQKLVDLQKQV 309
Cdd:TIGR02168 357 ----------EAELEELEAELEELES--RLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 310 TELEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 388
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
..
gi 568975053 389 IQ 390
Cdd:TIGR02168 497 LQ 498
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
287-495 |
1.37e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 44.96 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 287 MKQQYEQKITELRQKLVDLQKQVTELEAEREQkqrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLT 366
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 367 R-------QREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSD 439
Cdd:pfam02463 241 LlqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568975053 440 RERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERY 495
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
260-487 |
1.40e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 260 EKKVKLLEQQRMELLEVNKQwdqhfrsmKQQYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdrklllakSKIEMEET 339
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 340 DKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKaleealsiqaspssppaafgspegvgghlRKQELVTQN 419
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN-----------------------------TRESLETQL 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568975053 420 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRK 487
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
249-392 |
1.66e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 249 KVPEAGAFGAAEKKVKLLEQQRME--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQ 320
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975053 321 RDFDRK---LLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTrqreyQEKEIQRLNKALEEALSIQAS 392
Cdd:PRK12704 103 ELLEKReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLT-----AEEAKEILLEKVEEEARHEAA 172
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
173-494 |
2.25e-04 |
|
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: 44.44 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 173 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnSSCKEGLCGQPSSPKPEGAGKKGVAGQQQASVMAskVPE 252
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL---EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIA--GIK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 253 AGAFGAAEKKVKLLEQQRMELLEVNKQWdqhfrsmKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKS 332
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESEL-------REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENF 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 333 KIEMEETDKEQLTAEAKELRqkvryLQDQLSPLTRQREYQEKEIQRLNKALEE------ALSIQASPSS----------- 395
Cdd:pfam12128 470 DERIERAREEQEAANAEVER-----LQSELRQARKRRDQASEALRQASRRLEErqsaldELELQLFPQAgtllhflrkea 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 396 ----------------------PPAAFGSPE------GVGGHLRK---QELVTQNELLKQQVKIFEEDFQRERSDRERMN 444
Cdd:pfam12128 545 pdweqsigkvispellhrtdldPEVWDGSVGgelnlyGVKLDLKRidvPEWAASEEELRERLDKAEEALQSAREKQAAAE 624
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 568975053 445 EEKEELKKQVEKLQAQVTLTNAQLK----TLKEEEKAKEALKQQKRKAKASGER 494
Cdd:pfam12128 625 EQLVQANGELEKASREETFARTALKnarlDLRRLFDEKQSEKDKKNKALAERKD 678
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
115-365 |
2.68e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 115 SNLKLHLQRLETTLSVCAEEPDHSQLfthlgrmalEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRD 194
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSK---------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 195 LAAERLREENTELKKLLMNSSCKEGLCGQpSSPKPEGAGKKGVAGQQQASVMASKVpeAGAFGAAEKKVKLLEQQRMELL 274
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 275 EVNKQWDQHFRSMK-------------QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKL--LLAKSKIEMEE- 338
Cdd:TIGR02168 877 ALLNERASLEEALAllrseleelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEa 956
|
250 260
....*....|....*....|....*...
gi 568975053 339 -TDKEQLTAEAKELRQKVRYLQDQLSPL 365
Cdd:TIGR02168 957 eALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
268-504 |
4.61e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 268 QQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQR------DFDRKLLLAKSKIEME-ETD 340
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 341 KEQltaeAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQASpssppaafgspegvgGHLRKQELVTQNE 420
Cdd:pfam15921 397 KEQ----NKRLWDRDTGNSITIDHLRRELDDRNMEVQRL-EALLKAMKSECQ---------------GQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 421 llkqqvkifEEDFQRERSDRERMNEEKEELKKQVEKLQA-QVTLTNAQ------LKTLKEEEKAKEALKQQKRKAKAS-- 491
Cdd:pfam15921 457 ---------NESLEKVSSLTAQLESTKEMLRKVVEELTAkKMTLESSErtvsdlTASLQEKERAIEATNAEITKLRSRvd 527
|
250
....*....|....*.
gi 568975053 492 ---GERYHMEPHPEHV 504
Cdd:pfam15921 528 lklQELQHLKNEGDHL 543
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
259-496 |
4.93e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 259 AEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFdRKLLLAKSKIEMEe 338
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAKIKSK- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 339 tdKEQLTAEAKELRQ----------------KVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQaspssppaafgs 402
Cdd:PHA02562 271 --IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS------------ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 403 pegvgghLRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKealk 482
Cdd:PHA02562 337 -------KKLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI---- 391
|
250
....*....|....
gi 568975053 483 qQKRKAKASGERYH 496
Cdd:PHA02562 392 -VKTKSELVKEKYH 404
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
173-447 |
5.65e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 173 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKegLCGQPSSPKPEGAGKkgvagQQQASVMASKVPE 252
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK--LYEEEKKMKAEEAKK-----AEEAKIKAEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 253 AGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKqvtelEAEREQKQRDFDRKLLLAKS 332
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK-----AEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 333 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQaspssppaafgspegvggHLRK 412
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA------------------HLKK 1764
|
250 260 270
....*....|....*....|....*....|....*
gi 568975053 413 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 447
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
393-491 |
7.01e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 393 PSSPPAAFGSPEGVGGHLrkQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 472
Cdd:PRK11448 127 WDFKPGPFVPPEDPENLL--HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ 204
|
90
....*....|....*....
gi 568975053 473 EEEKAKEALKQQKRKAKAS 491
Cdd:PRK11448 205 EKAAETSQERKQKRKEITD 223
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
281-396 |
7.24e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 281 DQHFRSMKQQY---EQKITELRQKL-------VDLQKQVTELEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKE 350
Cdd:COG3206 262 SPVIQQLRAQLaelEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQ 338
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 568975053 351 LRQKVRYL---QDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSP 396
Cdd:COG3206 339 LEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
260-482 |
7.27e-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: 42.70 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 260 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQY---EQKITELRQKLVDLQKQVTELEAE---------------REQKQR 321
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldntrESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 322 DFDRKLLLAKSKIEMEETDKE---------QLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKAL----EEALS 388
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKElkskekelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIsdleDELNK 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 389 IQASPSsppaaFGSPEGVGGHLRKQ--EL-VTQNELLKQQVKIFEEDFQRErsdrermnEEKEELKKQVEKLQAQVTLTN 465
Cdd:TIGR04523 550 DDFELK-----KENLEKEIDEKNKEieELkQTQKSLKKKQEEKQELIDQKE--------KEKKDLIKEIEEKEKKISSLE 616
|
250
....*....|....*..
gi 568975053 466 AQLKTLKEEEKAKEALK 482
Cdd:TIGR04523 617 KELEKAKKENEKLSSII 633
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
292-489 |
7.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 292 EQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREY 371
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 372 QEKEIQRLNKALEEALSIQ--------------------------ASPSSPPAAFGSPEG--------VGGHLRKQELVT 417
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKgkcpvcgrelteehrkelleeytaelKRIEKELKEIEEKERklrkelreLEKVLKKESELI 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568975053 418 QNELLKQQVKIFEEDFQR-ERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAK 489
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
262-344 |
8.60e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 262 KVKLLEQQRMELLEVNKQWDQHFRSMKQ----------QYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllAK 331
Cdd:PRK11448 150 EVLTLKQQLELQAREKAQSQALAEAQQQelvaleglaaELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQ---AA 226
|
90
....*....|...
gi 568975053 332 SKIEMEETDKEQL 344
Cdd:PRK11448 227 KRLELSEEETRIL 239
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
285-386 |
9.92e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 285 RSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllaKSKIEMEEtdkEQLTAEAKELRQKVRylqdqlsp 364
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIERLE---RELSEARSEERREIR-------- 462
|
90 100
....*....|....*....|....
gi 568975053 365 ltRQREYQ--EKEIQRLNKALEEA 386
Cdd:COG2433 463 --KDREISrlDREIERLERELEEE 484
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
268-485 |
1.29e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 268 QQRMELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLVDLQKQVTELEAEREQKQRDfdrkllLAKSKIEMEETDK 341
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 342 EQL-TAEAKELRQKVRYLQDQLspltrqreyqekeiQRLNKALEEA----LSIQASPSSPPAAF---------------- 400
Cdd:PRK11281 116 ETLsTLSLRQLESRLAQTLDQL--------------QNAQNDLAEYnsqlVSLQTQPERAQAALyansqrlqqirnllkg 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 401 GSPEGVG-GHLRKQELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQaqvTLTNAq 467
Cdd:PRK11281 182 GKVGGKAlRPSQRVLLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQ---EAINS- 252
|
250
....*....|....*....
gi 568975053 468 lKTLKE-EEKAKEALKQQK 485
Cdd:PRK11281 253 -KRLTLsEKTVQEAQSQDE 270
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
112-494 |
1.38e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 112 PEDSNLKLHLQRLETTLSVC---AEEPDHSQ----LFTHLGRMALEFNRLASKVHKNEQRTSILQTLceQLRQENEALKA 184
Cdd:PRK04863 223 PENSGVRKAFQDMEAALRENrmtLEAIRVTQsdrdLFKHLITESTNYVAADYMRHANERRVHLEEAL--ELRRELYTSRR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 185 KLDKglEQRDLaaERLREENTELKKllmnsscKEGLCGQPSspkpegagkkgvagqQQASVMASKVPEAGAF-------- 256
Cdd:PRK04863 301 QLAA--EQYRL--VEMARELAELNE-------AESDLEQDY---------------QAASDHLNLVQTALRQqekieryq 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 257 GAAEKKVKLLEQQRMELLEVNKQWDQHfRSMKQQYEQKITELRQKLVDLQKQVTELEA---EREQKQRDFDR-KLLLAKS 332
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEEN-EARAEAAEEEVDELKSQLADYQQALDVQQTraiQYQQAVQALERaKQLCGLP 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 333 KIEMEETDK--EQLTAEAKELRQKVRYLQDQLSPLTRQREYQEK----------EIQRlNKALEEALS-IQASPSSPPAA 399
Cdd:PRK04863 434 DLTADNAEDwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagEVSR-SEAWDVARElLRRLREQRHLA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 400 fGSPEGVGGHLR--KQELVTQ---NELLKQQVKIF------EEDFQRERSDRErmnEEKEELKKQVEKLQAQVTLTNAQL 468
Cdd:PRK04863 513 -EQLQQLRMRLSelEQRLRQQqraERLLAEFCKRLgknlddEDELEQLQEELE---ARLESLSESVSEARERRMALRQQL 588
|
410 420
....*....|....*....|....*.
gi 568975053 469 KTLKEEEKAKEALKQQKRKAKASGER 494
Cdd:PRK04863 589 EQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
258-359 |
1.54e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 258 AAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRkLLLAKSKiEME 337
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
|
90 100
....*....|....*....|..
gi 568975053 338 ETDKEQLTAEAKELRQKVRYLQ 359
Cdd:cd16269 270 ALLEEGFKEQAELLQEEIRSLK 291
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
258-359 |
2.17e-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: 40.35 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 258 AAEKKVKLLEQQRMELlevnkqwDQHFRSMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRklLLAKSKIEME 337
Cdd:pfam02841 215 AAEAEQELLREKQKEE-------EQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER--MLEHKLQEQE 275
|
90 100
....*....|....*....|..
gi 568975053 338 ETDKEQLTAEAKELRQKVRYLQ 359
Cdd:pfam02841 276 ELLKEGFKTEAESLQKEIQDLK 297
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
246-473 |
2.48e-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: 41.09 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 246 MASKVPEAGAFGAAEkkvklleqqrmELLEvnkqwdqHFRSMKQQYEQkITELRQKLVDLQKQVTELEAEREQkQRDFDR 325
Cdd:COG3096 484 IAGEVERSQAWQTAR-----------ELLR-------RYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERL-LEEFCQ 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 326 KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNK------ALEEALSIQASPSSppAA 399
Cdd:COG3096 544 RIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSG--EA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568975053 400 FGSPEGVGGHLrkqelvtqnellkQQVKIFEEDFQRERsdrERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKE 473
Cdd:COG3096 622 LADSQEVTAAM-------------QQLLEREREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
260-487 |
2.99e-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: 40.77 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 260 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLqKQVTELEAEREQKQRDFDRKLLLAKSKIEMEET 339
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 340 DKEQLTAEAKELRQKVRYLQDQLSpltrqREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvggHLRKQELVTQN 419
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEEL----------------------KQTQKSLKKKQ 584
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568975053 420 ELLKQQVKIFEEDFQRERSDRE-------RMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKA-KEALKQQKRK 487
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQiKETIKEIRNK 660
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-502 |
3.83e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 144 LGRMALEFNRLASKVHKNE---QRTSILQTLCEQLRQENEALK-AKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEG 219
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAaakKKADEAKKKAEEKKKADEAKKkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 220 LCGQPSSPKPEGAGKKGVAGQQQASVMASKvpeAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELR 299
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKA---AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 300 qKLVDLQKqvTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLspltRQREYQEKEIQRL 379
Cdd:PTZ00121 1553 -KAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 380 NKALEEALSIQASPSSPPAAFGSPEgvggHLRKQElvTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQA 459
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAE----ELKKAE--EENKIKAAEEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568975053 460 QVTLTNAQLKTLKEEEKAK-EALKQQKRKAKASGERYHMEPHPE 502
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKaEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
274-490 |
3.84e-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: 40.54 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 274 LEVNKQW--DQHFRSMKQQYEQKITELRQklvdLQKQVTELEAER--EQKQRDfdrKLLLAKSKIEMEETDKE-QLTAEA 348
Cdd:pfam01576 718 LEVNMQAlkAQFERDLQARDEQGEEKRRQ----LVKQVRELEAELedERKQRA---QAVAAKKKLELDLKELEaQIDAAN 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 349 K---ELRQKVRYLQDQLSPLTRQRE----------YQEKEIQRLNKALE-EALSIQASPSSPPAAFG---------SPEG 405
Cdd:pfam01576 791 KgreEAVKQLKKLQAQMKDLQRELEearasrdeilAQSKESEKKLKNLEaELLQLQEDLAASERARRqaqqerdelADEI 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 406 VGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTltnAQLKTLKEEEKAKEALKQQK 485
Cdd:pfam01576 871 ASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA---AERSTSQKSESARQQLERQN 947
|
....*
gi 568975053 486 RKAKA 490
Cdd:pfam01576 948 KELKA 952
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
289-468 |
3.86e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.39 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 289 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVRYLQDqlSP- 364
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSARYTPN--HPd 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 365 ---LTRQREYQEKEIQRLNKALEEALSIQASpssppaafgspegvGGHLRKQELVTQNELLKQQVKIFEEDfQRERSDRE 441
Cdd:COG3206 293 viaLRAQIAALRAQLQQEAQRILASLEAELE--------------ALQAREASLQAQLAQLEARLAELPEL-EAELRRLE 357
|
170 180 190
....*....|....*....|....*....|...
gi 568975053 442 RMNEEKEE-----LKKQVE-KLQAQVTLTNAQL 468
Cdd:COG3206 358 REVEVARElyeslLQRLEEaRLAEALTVGNVRV 390
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
262-384 |
3.92e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.52 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 262 KVKLLEQQRMELLEVNKQWDQHF----RSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEME 337
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568975053 338 ETDKEQLTAEAKELRQkvrylqdQLSPLTRQREYQEKEIQRLNKALE 384
Cdd:pfam00038 95 LNLRTSAENDLVGLRK-------DLDEATLARVDLEAKIESLKEELA 134
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
153-460 |
4.13e-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: 40.34 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 153 RLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGA 232
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 233 GKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTEL 312
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 313 EAEREQKQRDFDRKLLLAKSKI---EMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 389
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLkdeLESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568975053 390 QASPSSPPAAFGSPE----GVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 460
Cdd:pfam02463 943 EEADEKEKEENNKEEeeerNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
168-481 |
5.08e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 168 LQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREEntelKKLLMNSSCKEglCGQP--SSPKPEGAGKKGV-------- 237
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEA----EALLEAGKCPE--CGQPveGSPHVETIEEDRErveeleae 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 238 ---AGQQQASVmASKVPEAGAFGAAEKKVKLLEQQRMELLEvnkqwdqhfrsMKQQYEQKITELRQKLVDLQKQVTELEA 314
Cdd:PRK02224 484 ledLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEE-----------LIAERRETIEEKRERAEELRERAAELEA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 315 EREQKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVRYLQDQLSpltrQREYQEKEIQRLNKALEEALSIQasps 394
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLERIRTLLA----AIADAEDEIERLREKREALAELN---- 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 395 sppaafgspegvggHLRKQELVTQNELLKQQVKIFEED-FQRERSDRER-------MNEEKEELKKQVEKLQAQVTLTNA 466
Cdd:PRK02224 623 --------------DERRERLAEKRERKRELEAEFDEArIEEAREDKERaeeyleqVEEKLDELREERDDLQAEIGAVEN 688
|
330
....*....|....*
gi 568975053 467 QLKTLKEEEKAKEAL 481
Cdd:PRK02224 689 ELEELEELRERREAL 703
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
268-473 |
5.21e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 268 QQRMELLEvNKQWD--QHFRSMKQQYEQKitelRQKLVDLQKQVTELEAEREQKQRDFDRKlllAKSKIEMEEtDKEQLT 345
Cdd:pfam10174 309 QTKLETLT-NQNSDckQHIEVLKESLTAK----EQRAAILQTEVDALRLRLEEKESFLNKK---TKQLQDLTE-EKSTLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 346 AEAKELRQ-------KVRYLQDQLSPLTRQREYQEKEIQRLNKALEealSIQASPSSPPAAfgspegvgghlrkqeLVTQ 418
Cdd:pfam10174 380 GEIRDLKDmldvkerKINVLQKKIENLQEQLRDKDKQLAGLKERVK---SLQTDSSNTDTA---------------LTTL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568975053 419 NELLKQQVKIFEE-DFQRERSDRERMNE------EKEELKKQVEKLQAQVTLTNAQLKTLKE 473
Cdd:pfam10174 442 EEALSEKERIIERlKEQREREDRERLEEleslkkENKDLKEKVSALQPELTEKESSLIDLKE 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
282-405 |
6.04e-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: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 282 QHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKqrdfdrklllakskiemeETDKEQLTAEAKELRQKVRYLQDQ 361
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQ 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568975053 362 LSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEG 405
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
252-387 |
6.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 252 EAGAfgaaekKVKL--------LEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAeREQKQRDF 323
Cdd:COG0542 397 EAAA------RVRMeidskpeeLDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKEL 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 324 DRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEE 385
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEE 545
|
..
gi 568975053 386 AL 387
Cdd:COG0542 546 EL 547
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
275-385 |
6.39e-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: 37.18 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 275 EVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTEL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 353
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
|
90 100 110
....*....|....*....|....*....|..
gi 568975053 354 KVRYLQDQLSplTRQREYQEKEIQRLNKALEE 385
Cdd:smart00935 77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
292-461 |
6.94e-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: 39.43 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 292 EQKITELRQK------LVD----LQKQVTELEAEREQ---KQRDFDRKL-----LLAKSKIEMEET--DKEQLTAEAKEL 351
Cdd:pfam15066 345 EKKVKELQMKitkqqvFVDiinkLKENVEELIEDKYNvilEKNDINKTLqnlqeILANTQKHLQESrkEKETLQLELKKI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 352 rqKVRYLQDQLSPLTrqreyqekEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKqelVTQN--ELLKQQVKIF 429
Cdd:pfam15066 425 --KVNYVHLQERYIT--------EMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEK---ATTSalDLLKREKETR 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 568975053 430 EEDF---QRERSDRERMN-EEKEELKKQVEKLQAQV 461
Cdd:pfam15066 492 EQEFlslQEEFQKHEKENlEERQKLKSRLEKLVAQV 527
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
344-475 |
7.93e-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: 38.59 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 344 LTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQASPSSPPAAFGSPEGvgghlRKQELVTQNELL 422
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQLATERS-----ARREAEAELERL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 568975053 423 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQvtLTNAQLKTLKEEE 475
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQ--LTSKSQSSSSQSE 167
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
417-489 |
8.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 8.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568975053 417 TQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEE-EKAKEALKQQKRKAK 489
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiAEAEAEIEERREELG 89
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
293-468 |
9.89e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.87 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 293 QKITELRQKLVDLQKQVTELEAEREqkqrDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQ 372
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERERE----ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568975053 373 EKEIQrlnkalEEALSIQASPSSPPAAFGSPEgvgghlrkqELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKK 452
Cdd:PRK02224 327 RDRLE------ECRVAAQAHNEEAESLREDAD---------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
170
....*....|....*.
gi 568975053 453 QVEKLQAQVTLTNAQL 468
Cdd:PRK02224 392 EIEELRERFGDAPVDL 407
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