|
Name |
Accession |
Description |
Interval |
E-value |
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
260-461 |
1.65e-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: 65.94 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 260 QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQ 339
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 340 EKEIQRLNKALEEAL--SIQASPSSPPAAFGSPEGVGGHLR----------------------KQELVTQNELLKQQVKI 395
Cdd:COG4942 96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRrlqylkylaparreqaeelradLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366994 396 FEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 461
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-457 |
4.09e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 225 AAEKKVKLleQQRMELLEVNKQW--DQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDR---------- 292
Cdd:COG1196 211 KAERYREL--KEELKELEAELLLlkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEleleleeaqa 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 293 KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspeg 372
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA---------- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 373 vgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQK 452
Cdd:COG1196 359 ----ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
....*
gi 1720366994 453 RKAKA 457
Cdd:COG1196 435 EEEEE 439
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
259-457 |
1.07e-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: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 259 EQKITELRQKLVDLQKQVTELEAEREQ-------KQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSP 331
Cdd:COG1196 185 EENLERLEDILGELERQLEPLERQAEKaeryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 332 LTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMN 411
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1720366994 412 EEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKA 457
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-456 |
5.52e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 225 AAEKKVKLLEQQRMEL-LEVNKQWDQHFRSMKQ--QYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdRKLLLAKSKI 301
Cdd:COG1196 264 ELEAELEELRLELEELeLELEEAQAEEYELLAElaRLEQDIARLEERRRELEERLEELEEELAELE----EELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 302 EMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAspssppaafgspegvgghlrkQE 381
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA---------------------EL 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366994 382 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAK 456
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-455 |
3.26e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 262 ITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEK 341
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 342 EIQRLNKALEEALSIQASPSSPPAAFGSpegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 421
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQ--------QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190
....*....|....*....|....*....|....
gi 1720366994 422 EKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKA 455
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
120-474 |
1.74e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 120 RLASKVHKNEQRTSILQTLcEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLmnssckeglcgqpsspkpega 199
Cdd:COG1196 226 EAELLLLKLRELEAELEEL-EAELEELEAELEELEAELAELEAELEELRLELEELELEL--------------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 200 gkkGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWdqhfrsmkqqyEQKITELRQKLVDLQKQVTEL 279
Cdd:COG1196 284 ---EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-----------EEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 280 EAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAs 359
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 360 pssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 439
Cdd:COG1196 429 ------------------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330 340 350
....*....|....*....|....*....|....*
gi 1720366994 440 EEEKAKEALKQQKRKAKASGERYHMEPHPEHVCGA 474
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
140-471 |
1.85e-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: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 140 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnssckeglcgqpsspkpegagKKGVAGQQQASVMASKVpe 219
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQL-----------------------RKELEELSRQISALRKD-- 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 220 agaFGAAEKKVKLLEQQRMELLEVNKQwdqhfrsmkqqYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKS 299
Cdd:TIGR02168 735 ---LARLEAEVEQLEERIAQLSKELTE-----------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKE 796
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 300 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEgvgghlrk 379
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI-------- 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 380 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASG 459
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
330
....*....|..
gi 1720366994 460 ERYHMEPHPEHV 471
Cdd:TIGR02168 949 YSLTLEEAEALE 960
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
127-425 |
2.12e-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: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 127 KNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGAGKKGVAG 206
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 207 QQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQY------------------------EQKI 262
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaanlrerleslerriaatERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 263 TELRQKLVDLQKQVTELEAEREQKQRDFDR------KLLLAKSKIEME----ETDKEQLTAEAKELRQKVRYLQDQLSPL 332
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEEleseleALLNERASLEEAlallRSELEELSEELRELESKRSELRRELEEL 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 333 TRQRE-YQEK------EIQRLNKALEEALSI--QASPSSPPAAFGSPEGVGGHLRKqelvtqnelLKQQVKIF------- 396
Cdd:TIGR02168 921 REKLAqLELRleglevRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRRLKR---------LENKIKELgpvnlaa 991
|
330 340
....*....|....*....|....*....
gi 1720366994 397 EEDFQRERSDRERMNEEKEELKKQVEKLQ 425
Cdd:TIGR02168 992 IEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
227-446 |
3.72e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.18 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 227 EKKVKLLEQQRMELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLVDLQKQVTELEAERE----QKQRDFDRKLll 296
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 297 aKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSppaafgspEGVGGH 376
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKK--------ENQSYK 383
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 377 LRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKE 446
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
256-427 |
4.50e-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: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 256 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQ 335
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 336 REYQ--EKEIQRLNKAL----EEALSIQAspssppaafgspegvgghlRKQELVTQNELLKQQVKIFEEDFQRERSDREr 409
Cdd:COG1579 89 KEYEalQKEIESLKRRIsdleDEILELME-------------------RIEELEEELAELEAELAELEAELEEKKAELD- 148
|
170
....*....|....*...
gi 1720366994 410 mnEEKEELKKQVEKLQAQ 427
Cdd:COG1579 149 --EELAELEAELEELEAE 164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-463 |
1.62e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 254 MKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS 330
Cdd:COG4913 247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 331 PLTRQREYQ--------EKEIQRLNKALEEalsiqaspssppaafgspegvgghlRKQELVTQNELLKQ---QVKIFEED 399
Cdd:COG4913 327 ELEAQIRGNggdrleqlEREIERLERELEE-------------------------RERRRARLEALLAAlglPLPASAEE 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366994 400 FQRErsdRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEA-LKQQKRKAKASGERYH 463
Cdd:COG4913 382 FAAL---RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAeIASLERRKSNIPARLL 443
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
259-465 |
1.64e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 259 EQKITELRQKLVDLQKQVTELEAEREQKQRDfdRKLLLAKSKIEMEEtdkeqLTAEAKELRQKVRYLQDQLSPLTRQREY 338
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYE-----LLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 339 QEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFE---EDFQRER----SDRERMN 411
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErelEDAEERLakleAEIDKLL 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1720366994 412 EEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERYHME 465
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
379-427 |
1.86e-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: 1.86e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720366994 379 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 427
Cdd:cd09803 34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-462 |
2.55e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 256 QQYEQKITELRQKLVDLQKQVTELEAER---EQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPL 332
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 333 TRQREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQrerSDRERMNE 412
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEA----------------------EEELAEAEAEIEELEAQIEQLKEELK---ALREALDE 807
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1720366994 413 EKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERY 462
Cdd:TIGR02168 808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
255-461 |
3.93e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 255 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSplTR 334
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 335 QREYQEKeiQRLNKALEEALSiqaspSSPPAAFgspegvgghLRKQELVT-----QNELLKQQ---VKIFEEDFQRERSD 406
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLG-----SESFSDF---------LDRLSALSkiadaDADLLEELkadKAELEAKKAELEAK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1720366994 407 RERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGER 461
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
248-462 |
1.36e-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: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 248 DQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQ-KQR----DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKV 322
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 323 RYLQDQL--SPLTRQREYQEKEIQRLNKALEEA------LSIQASPSSPPAafgspegvgghlrkQELVTQNELLKQQVK 394
Cdd:COG3206 243 AALRAQLgsGPDALPELLQSPVIQQLRAQLAELeaelaeLSARYTPNHPDV--------------IALRAQIAALRAQLQ 308
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366994 395 ifeedfQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKakeALKQQKRKAKASGERY 462
Cdd:COG3206 309 ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEA---ELRRLEREVEVARELY 367
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
80-355 |
2.29e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 80 EDSNLKLHLQRLETTLSVCAEEpdHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQ 159
Cdd:COG1196 233 KLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 160 RDLAAERLREENTELKKLlmnssckeglcgqpsspkpegAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRME 239
Cdd:COG1196 311 RRELEERLEELEEELAEL---------------------EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 240 LLEVNKQWDQHFRSMKQQY---EQKITELRQKLVDLQKQVTELE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTA 313
Cdd:COG1196 370 AEAELAEAEEELEELAEELleaLRAAAELAAQLEELEEAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1720366994 314 EAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 355
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
215-425 |
3.43e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 215 SKVPE-AGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMK------QQYEQKITELRQKLVDLQKQVTELE-----AE 282
Cdd:PRK03918 214 SELPElREELEKLEKEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVKELKelkekAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 283 REQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLN---KALEEALSIQAS 359
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEE 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366994 360 PSSPPAAFGSpegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQ 425
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 ... |
120-461 |
3.52e-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: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 120 RLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGA 199
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 200 GKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNkqwdqhfRSMKQQYEQKITELRQKLVDLQKQVTEL 279
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL-------KSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 280 EAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQAS 359
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 360 PSSPpaafgspegvgGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 439
Cdd:pfam02463 407 AQLL-----------LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|..
gi 1720366994 440 EEEKAKEALKQQKRKAKASGER 461
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEE 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
111-421 |
5.33e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 111 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLD---KGLEQRDLAAERLREENTELKKLLMNSsckegl 187
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKeleARIEELEEDLHKLEEALNDLEARLSHS------ 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 188 cgqpssPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQ---KITE 264
Cdd:TIGR02169 792 ------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 265 LRQKLVDLQKQVTELEAEREQKQRDFDR---KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS---PLTRQREY 338
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeieDPKGEDEE 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 339 QEKEIQRLNKALEEALSIQASPSS-PPAAFGSPEGVgghlrKQELVTQNELLKQQVKIFEEdfqreRSDRERMNEEKEEL 417
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRAlEPVNMLAIQEY-----EEVLKRLDELKEKRAKLEEE-----RKAILERIEEYEKK 1015
|
....
gi 1720366994 418 KKQV 421
Cdd:TIGR02169 1016 KREV 1019
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
125-443 |
6.64e-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: 49.35 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 125 VHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLcgqpsspKPEGAGKKGV 204
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEAL-------KLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 205 AG--QQQASVMASKVPEAG-AFGAAEKKVKLLEQQ----RMELlevnkqwdQHFRSMKQQYEQKITELRQKLVDLQKQVT 277
Cdd:pfam15921 564 IEilRQQIENMTQLVGQHGrTAGAMQVEKAQLEKEindrRLEL--------QEFKILKDKKDAKIRELEARVSDLELEKV 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 278 ELEAEREQKQRdfdrklllAKSKIEMEetdKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEAL-SI 356
Cdd:pfam15921 636 KLVNAGSERLR--------AVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLkSA 704
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 357 QASPSSPPAAFGSPEGVGGHLRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 427
Cdd:pfam15921 705 QSELEQTRNTLKSMEGSDGHAMKVAMGMQKQItakrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE 784
|
330
....*....|....*.
gi 1720366994 428 VTLTNAQLKTLKEEEK 443
Cdd:pfam15921 785 KNKMAGELEVLRSQER 800
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
96-461 |
8.17e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 8.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 96 SVCAEEPDHSQLFTH-LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTEL 174
Cdd:TIGR02169 667 LFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 175 kkllmnSSCKEGLcgqpSSPKPEGAGKKGVAGQQQASvmaskvpeagafgAAEKKVKLLEQQRMELLEVNKQWDQHFRSM 254
Cdd:TIGR02169 747 ------SSLEQEI----ENVKSELKELEARIEELEED-------------LHKLEEALNDLEARLSHSRIPEIQAELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 255 KQQY---EQKITELRQKLVDLQKQVTELEAEREQKQ---RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQ 328
Cdd:TIGR02169 804 EEEVsriEARLREIEQKLNRLTLEKEYLEKEIQELQeqrIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 329 LSPLTRQREYQEKEIQRLNKALEEaLSIQASPSsppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRE 408
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEE-LEAQIEKK--------------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1720366994 409 RMNEEkEELKKQVEKLQAQV-TLTNAQLKTLKEEEKAKEALKQ-QKRKAKASGER 461
Cdd:TIGR02169 949 EELSL-EDVQAELQRVEEEIrALEPVNMLAIQEYEEVLKRLDElKEKRAKLEEER 1002
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
226-427 |
9.77e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 226 AEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQkITELRQKLVDLQKQ------VTELEAEREQKQRDFDRkLLLAKS 299
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDA-LQERREALQRLAEYswdeidVASAEREIAELEAELER-LDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 300 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAafgspegvgghlrk 379
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL-------------- 751
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720366994 380 qELVTQNELLKQQVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQ 427
Cdd:COG4913 752 -EERFAAALGDAVERELRENLEER---IDALRARLNRAEEELERAMRA 795
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
387-429 |
1.45e-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: 1.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1720366994 387 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 429
Cdd:pfam16516 55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
225-459 |
1.50e-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: 47.45 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 225 AAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQ---YEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLA---- 297
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALyrlg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 298 ---KSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREyqekEIQRLNKALEEALSIQASpssppaafgspegvg 374
Cdd:COG4942 118 rqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEA--------------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 375 ghlRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQaqvtltnAQLKTLKEEEKAKEALKQQKRK 454
Cdd:COG4942 179 ---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAAAAERTPAAGF 248
|
....*
gi 1720366994 455 AKASG 459
Cdd:COG4942 249 AALKG 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
116-428 |
2.19e-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: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 116 LEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnssckeglcgqpsspk 195
Cdd:TIGR02169 223 YEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------------------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 196 peGAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMEL-LEVNKQwdqhfRSMKQQYEQKITELRQKLVDLQK 274
Cdd:TIGR02169 285 --GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLeAEIDKL-----LAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 275 QVTELEAEREQKQRDF---DRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLN---K 348
Cdd:TIGR02169 358 EYAELKEELEDLRAELeevDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEakiN 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 349 ALEEALsiqaspssppaafgspEGVGGHLRKQElvTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQV 428
Cdd:TIGR02169 438 ELEEEK----------------EDKALEIKKQE--WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
118-457 |
2.42e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 118 FNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENtELKKLLMNSSCKeglcGQPSSPKPE 197
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKK----ADAAKKKAE 1339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 198 GAGKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEvnkqwdqhfrsMKQQYEQKITELRQKLVDLQKQVT 277
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAK-----------KKAEEKKKADEAKKKAEEDKKKAD 1408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 278 ELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRylQDQLSPLTRQREYQEKEIQRLNKALEEALSIQ 357
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE--EAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 358 ASPSSPPAAfgspegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK---EELKKQVEKLQAQVTLTNAQ 434
Cdd:PTZ00121 1487 EAKKKAEEA----------KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADELKKAEE 1556
|
330 340
....*....|....*....|...
gi 1720366994 435 LKTLKEEEKAKEALKQQKRKAKA 457
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMA 1579
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
232-441 |
3.96e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 232 LLEQQRMELLEVNKQWDQhfrsmKQQYE--QKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEMEETDKE 309
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-----KEEKDlhERLNGLESELAELDEEIERYEEQREQARETRDE----ADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 310 QLTaeakELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEaLSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELL 389
Cdd:PRK02224 252 ELE----TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE-LEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720366994 390 KQ-------QVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEE 441
Cdd:PRK02224 327 RDrleecrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREE 385
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
255-421 |
4.01e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 255 KQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEmEETdkEQLTAEAKELRQKVRYLQDQLSPLTR 334
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQ-QAI--KEAKKEADEIIKELRQLQKGGYASVK 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 335 QREYQEKeIQRLNKALEEALSIQASPSSPPAAFgspeGVGGHLR---------------KQELVTQNELLKQQVKIfeed 399
Cdd:PRK00409 606 AHELIEA-RKRLNKANEKKEKKKKKQKEKQEEL----KVGDEVKylslgqkgevlsipdDKEAIVQAGIMKMKVPL---- 676
|
170 180
....*....|....*....|..
gi 1720366994 400 fqrerSDRERMNEEKEELKKQV 421
Cdd:PRK00409 677 -----SDLEKIQKPKKKKKKKP 693
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
248-456 |
4.40e-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: 46.55 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 248 DQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQD 327
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 328 ---QLSPLTRQREYQEKEIQRLNKALEEALSiqaspssppaafgspEGVGGHLRKQE---LVTQNEL---------LKQQ 392
Cdd:TIGR04523 279 nnkKIKELEKQLNQLKSEISDLNNQKEQDWN---------------KELKSELKNQEkklEEIQNQIsqnnkiisqLNEQ 343
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366994 393 VKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQvtlTNAQLKTLKEEEKAKEALKQQKRKAK 456
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQEIKNLESQINDLESKIQNQE 404
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
249-440 |
6.17e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 249 QHFRSMKQQY-EQKIteLRQKLVDLQKQVTELEaEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQD 327
Cdd:PRK04863 496 DVARELLRRLrEQRH--LAEQLQQLRMRLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 328 QLSPLTRQREYQEKEIQRLnKALEEALSIQASP--SSPPAAFGSPEGVGGHLRKQELVTQnelLKQQVKIFEEDFQRErs 405
Cdd:PRK04863 573 SVSEARERRMALRQQLEQL-QARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTE---YMQQLLERERELTVE-- 646
|
170 180 190
....*....|....*....|....*....|....*
gi 1720366994 406 dRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKE 440
Cdd:PRK04863 647 -RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
227-460 |
6.24e-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: 45.88 E-value: 6.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 227 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQklvdlqkqvtELEAEREQKQRDFDRKLLLAKSKIEMEET 306
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 307 DKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQEL---- 382
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 383 -----------VTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKkqveKLQAQVTLTNAQLKTLKEEEKAKEALKQQ 451
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR----RIQEQMRKATEERSRLEAMEREREMMRQI 581
|
....*....
gi 1720366994 452 KRKAKASGE 460
Cdd:pfam17380 582 VESEKARAE 590
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
113-465 |
7.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 113 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRQENEALK-AKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQP 191
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 192 SSPKPEGAGKKGVAGQQQASVMASKVPEAGAFGAAEK-----KVKLLEQQRMEllEVNKQWDQHFRSMKQQYEQKITELR 266
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 267 QKLVDLQKQVTELEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEI 343
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 344 QRLNKALEEalsiqaspssppaafgspegvggHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEK 423
Cdd:PTZ00121 1678 EEAKKAEED-----------------------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1720366994 424 LQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERYHME 465
Cdd:PTZ00121 1735 AKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
141-178 |
8.25e-05 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 44.58 E-value: 8.25e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1720366994 141 QLRQENEALKAKLDKgLEQRDLAAERLREENTELKKLL 178
Cdd:PRK13922 73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-457 |
9.35e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 225 AAEKKVKLLEQQRMELLEVNKQWDQhFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQ-------RDFDRKLLLA 297
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 298 KSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLnkALEEALSIQASPSSPPAAFGSPEGVGGhL 377
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL--IAAALLALLGLGGSLLSLILTIAGVLF-L 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 378 RKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKA 457
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-357 |
1.05e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 117 EFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLmnsSCKEGLcgqpsspkp 196
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK---EELESL--------- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 197 egagkkgvagQQQASVMASKVPEAGAfgAAEKKVKLLEQQRMELLEVNKQwdqhfrsmKQQYEQKITELRQKLVDLQKQV 276
Cdd:TIGR02168 357 ----------EAELEELEAELEELES--RLEELEEQLETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 277 TELEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 355
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
..
gi 1720366994 356 IQ 357
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 ... |
254-462 |
1.34e-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: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 254 MKQQYEQKITELRQKLVDLQKQVTELEAEREQkqrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLT 333
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 334 R-------QREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSD 406
Cdd:pfam02463 241 LlqellrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720366994 407 RERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAKASGERY 462
Cdd:pfam02463 321 KEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
216-359 |
1.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 216 KVPEAGAFGAAEKKVKLLEQQRME--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQ 287
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366994 288 RDFDRK---LLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTrqreyQEKEIQRLNKALEEALSIQAS 359
Cdd:PRK12704 103 ELLEKReeeLEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLT-----AEEAKEILLEKVEEEARHEAA 172
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
140-461 |
1.67e-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: 44.83 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 140 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLlmnSSCKEGLCGQPSSPKPEGAGKKGVAGQQQASVMAskVPE 219
Cdd:pfam12128 322 SELEALEDQHGAFLDADIETAAADQEQLPSWQSELENL---EERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIA--GIK 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 220 AGAFGAAEKKVKLLEQQRMELLEVNKQWdqhfrsmKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKS 299
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESEL-------REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENF 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 300 KIEMEETDKEQLTAEAKELRqkvryLQDQLSPLTRQREYQEKEIQRLNKALEE------ALSIQASPSS----------- 362
Cdd:pfam12128 470 DERIERAREEQEAANAEVER-----LQSELRQARKRRDQASEALRQASRRLEErqsaldELELQLFPQAgtllhflrkea 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 363 ----------------------PPAAFGSPE------GVGGHLRK---QELVTQNELLKQQVKIFEEDFQRERSDRERMN 411
Cdd:pfam12128 545 pdweqsigkvispellhrtdldPEVWDGSVGgelnlyGVKLDLKRidvPEWAASEEELRERLDKAEEALQSAREKQAAAE 624
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1720366994 412 EEKEELKKQVEKLQAQVTLTNAQLK----TLKEEEKAKEALKQQKRKAKASGER 461
Cdd:pfam12128 625 EQLVQANGELEKASREETFARTALKnarlDLRRLFDEKQSEKDKKNKALAERKD 678
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
227-454 |
1.79e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 227 EKKVKLLEQQRMELLEVNKQwdqhfrsmKQQYEQKITELRQKLVDLQKQVTELEAEREQKQrdfdrklllakSKIEMEET 306
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 307 DKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKaleealsiqaspssppaafgspegvgghlRKQELVTQN 386
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN-----------------------------TRESLETQL 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720366994 387 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRK 454
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
82-332 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 82 SNLKLHLQRLETTLSVCAEEPDHSQLfthlgrmalEFNRLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRD 161
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSK---------ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 162 LAAERLREENTELKKLLMNSSCKEGLCGQpSSPKPEGAGKKGVAGQQQASVMASKVpeAGAFGAAEKKVKLLEQQRMELL 241
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLES-LERRIAATERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELE 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 242 EVNKQWDQHFRSMK-------------QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKL--LLAKSKIEMEE- 305
Cdd:TIGR02168 877 ALLNERASLEEALAllrseleelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEa 956
|
250 260
....*....|....*....|....*...
gi 1720366994 306 -TDKEQLTAEAKELRQKVRYLQDQLSPL 332
Cdd:TIGR02168 957 eALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
235-471 |
3.97e-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: 43.57 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 235 QQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQR------DFDRKLLLAKSKIEME-ETD 307
Cdd:pfam15921 317 RQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 308 KEQltaeAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQASpssppaafgspegvgGHLRKQELVTQNE 387
Cdd:pfam15921 397 KEQ----NKRLWDRDTGNSITIDHLRRELDDRNMEVQRL-EALLKAMKSECQ---------------GQMERQMAAIQGK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 388 llkqqvkifEEDFQRERSDRERMNEEKEELKKQVEKLQA-QVTLTNAQ------LKTLKEEEKAKEALKQQKRKAKAS-- 458
Cdd:pfam15921 457 ---------NESLEKVSSLTAQLESTKEMLRKVVEELTAkKMTLESSErtvsdlTASLQEKERAIEATNAEITKLRSRvd 527
|
250
....*....|....*.
gi 1720366994 459 ---GERYHMEPHPEHV 471
Cdd:pfam15921 528 lklQELQHLKNEGDHL 543
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
226-463 |
4.14e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 226 AEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFdRKLLLAKSKIEMEe 305
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAKIKSK- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 306 tdKEQLTAEAKELRQ----------------KVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQaspssppaafgs 369
Cdd:PHA02562 271 --IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS------------ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 370 pegvgghLRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKealk 449
Cdd:PHA02562 337 -------KKLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI---- 391
|
250
....*....|....
gi 1720366994 450 qQKRKAKASGERYH 463
Cdd:PHA02562 392 -VKTKSELVKEKYH 404
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
140-414 |
4.90e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 140 EQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKegLCGQPSSPKPEGAGKkgvagQQQASVMASKVPE 219
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK--LYEEEKKMKAEEAKK-----AEEAKIKAEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 220 AGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKqvtelEAEREQKQRDFDRKLLLAKS 299
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK-----AEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 300 KIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQaspssppaafgspegvggHLRK 379
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA------------------HLKK 1764
|
250 260 270
....*....|....*....|....*....|....*
gi 1720366994 380 QELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 414
Cdd:PTZ00121 1765 EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
248-363 |
5.63e-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: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 248 DQHFRSMKQQY---EQKITELRQKL-------VDLQKQVTELEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKE 317
Cdd:COG3206 262 SPVIQQLRAQLaelEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQ 338
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720366994 318 LRQKVRYL---QDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSP 363
Cdd:COG3206 339 LEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
360-458 |
6.51e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 360 PSSPPAAFGSPEGVGGHLrkQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLK 439
Cdd:PRK11448 127 WDFKPGPFVPPEDPENLL--HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ 204
|
90
....*....|....*....
gi 1720366994 440 EEEKAKEALKQQKRKAKAS 458
Cdd:PRK11448 205 EKAAETSQERKQKRKEITD 223
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
229-311 |
7.93e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 229 KVKLLEQQRMELLEVNKQWDQHFRSMKQ----------QYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllAK 298
Cdd:PRK11448 150 EVLTLKQQLELQAREKAQSQALAEAQQQelvaleglaaELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQ---AA 226
|
90
....*....|...
gi 1720366994 299 SKIEMEETDKEQL 311
Cdd:PRK11448 227 KRLELSEEETRIL 239
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
252-353 |
8.47e-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: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 252 RSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKlllaKSKIEMEEtdkEQLTAEAKELRQKVRylqdqlsp 331
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEK----DERIERLE---RELSEARSEERREIR-------- 462
|
90 100
....*....|....*....|....
gi 1720366994 332 ltRQREYQ--EKEIQRLNKALEEA 353
Cdd:COG2433 463 --KDREISrlDREIERLERELEEE 484
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
259-456 |
8.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 259 EQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREY 338
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 339 QEKEIQRLNKALEEALSIQ--------------------------ASPSSPPAAFGSPEG--------VGGHLRKQELVT 384
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKgkcpvcgrelteehrkelleeytaelKRIEKELKEIEEKERklrkelreLEKVLKKESELI 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366994 385 QNELLKQQVKIFEEDFQR-ERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALKQQKRKAK 456
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELE 569
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
227-449 |
9.21e-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: 42.31 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 227 EKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLqKQVTELEAEREQKQRDFDRKLLLAKSKIEMEET 306
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLES 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 307 DKEQLTAEAKELRQKVRYLQDQLSpltrqREYQEKEIQRLNKALEEAlsiqaspssppaafgspegvgghlrKQelvTQN 386
Cdd:TIGR04523 532 EKKEKESKISDLEDELNKDDFELK-----KENLEKEIDEKNKEIEEL-------------------------KQ---TQK 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720366994 387 ELLKQQVKIFEEDFQRErsdrermnEEKEELKKQVEKLQAQVTLTNAQLKTLKEEEKAKEALK 449
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKE--------KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
79-461 |
1.02e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 79 PEDSNLKLHLQRLETTLSVC---AEEPDHSQ----LFTHLGRMALEFNRLASKVHKNEQRTSILQTLceQLRQENEALKA 151
Cdd:PRK04863 223 PENSGVRKAFQDMEAALRENrmtLEAIRVTQsdrdLFKHLITESTNYVAADYMRHANERRVHLEEAL--ELRRELYTSRR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 152 KLDKglEQRDLaaERLREENTELKKllmnsscKEGLCGQPSspkpegagkkgvagqQQASVMASKVPEAGAF-------- 223
Cdd:PRK04863 301 QLAA--EQYRL--VEMARELAELNE-------AESDLEQDY---------------QAASDHLNLVQTALRQqekieryq 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 224 GAAEKKVKLLEQQRMELLEVNKQWDQHfRSMKQQYEQKITELRQKLVDLQKQVTELEA---EREQKQRDFDR-KLLLAKS 299
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEEN-EARAEAAEEEVDELKSQLADYQQALDVQQTraiQYQQAVQALERaKQLCGLP 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 300 KIEMEETDK--EQLTAEAKELRQKVRYLQDQLSPLTRQREYQEK----------EIQRlNKALEEALS-IQASPSSPPAA 366
Cdd:PRK04863 434 DLTADNAEDwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagEVSR-SEAWDVARElLRRLREQRHLA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 367 fGSPEGVGGHLR--KQELVTQ---NELLKQQVKIF------EEDFQRERSDRErmnEEKEELKKQVEKLQAQVTLTNAQL 435
Cdd:PRK04863 513 -EQLQQLRMRLSelEQRLRQQqraERLLAEFCKRLgknlddEDELEQLQEELE---ARLESLSESVSEARERRMALRQQL 588
|
410 420
....*....|....*....|....*.
gi 1720366994 436 KTLKEEEKAKEALKQQKRKAKASGER 461
Cdd:PRK04863 589 EQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
235-452 |
1.48e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 235 QQRMELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLVDLQKQVTELEAEREQKQRDFDR--KLLLAKSKIEMEET 306
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAlkDDNDEETRETLSTL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 307 DKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEA------LSIQASPSSPPAAFGSPEgvgghlRKQ 380
Cdd:PRK11281 122 SLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANsqrlqqIRNLLKGGKVGGKALRPS------QRV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 381 ELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQaqvTLTNAqlKTLKE-EEKAKEA 447
Cdd:PRK11281 196 LLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQ---EAINS--KRLTLsEKTVQEA 265
|
....*
gi 1720366994 448 LKQQK 452
Cdd:PRK11281 266 QSQDE 270
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
225-326 |
1.76e-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: 40.64 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 225 AAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRkLLLAKSKiEME 304
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
|
90 100
....*....|....*....|..
gi 1720366994 305 ETDKEQLTAEAKELRQKVRYLQ 326
Cdd:cd16269 270 ALLEEGFKEQAELLQEEIRSLK 291
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
213-440 |
1.93e-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: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 213 MASKVPEAGAFGAAEkkvklleqqrmELLEvnkqwdqHFRSMKQQYEQkITELRQKLVDLQKQVTELEAEREQkQRDFDR 292
Cdd:COG3096 484 IAGEVERSQAWQTAR-----------ELLR-------RYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERL-LEEFCQ 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 293 KLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNK------ALEEALSIQASPSSppAA 366
Cdd:COG3096 544 RIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDALERLREQSG--EA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366994 367 FGSPEGVGGHLrkqelvtqnellkQQVKIFEEDFQRERsdrERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKE 440
Cdd:COG3096 622 LADSQEVTAAM-------------QQLLEREREATVER---DELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
225-326 |
2.14e-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: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 225 AAEKKVKLLEQQRMELlevnkqwDQHFRSMKQQYEQKITELRQKlvdlqkqvteLEAEREQKQRDFDRklLLAKSKIEME 304
Cdd:pfam02841 215 AAEAEQELLREKQKEE-------EQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER--MLEHKLQEQE 275
|
90 100
....*....|....*....|..
gi 1720366994 305 ETDKEQLTAEAKELRQKVRYLQ 326
Cdd:pfam02841 276 ELLKEGFKTEAESLQKEIQDLK 297
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
147-448 |
2.17e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 147 EALKAKLDKGLEQRDLAAERLREENTELK----------KLLMNSSCKEglCGQP--SSPKPEGAGKKGV---------- 204
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRtarerveeaeALLEAGKCPE--CGQPveGSPHVETIEEDRErveeleaele 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 205 -AGQQQASVmASKVPEAGAFGAAEKKVKLLEQQRmELLEvnkqwdqhfrSMKQQYEQKITELRQKLVDLQKQVTELEAER 283
Cdd:PRK02224 486 dLEEEVEEV-EERLERAEDLVEAEDRIERLEERR-EDLE----------ELIAERRETIEEKRERAEELRERAAELEAEA 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 284 EQKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVRYLQDQLSpltrQREYQEKEIQRLNKALEEALSIQaspssp 363
Cdd:PRK02224 554 EEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLERIRTLLA----AIADAEDEIERLREKREALAELN------ 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 364 paafgspegvggHLRKQELVTQNELLKQQVKIFEED-FQRERSDRER-------MNEEKEELKKQVEKLQAQVTLTNAQL 435
Cdd:PRK02224 623 ------------DERRERLAEKRERKRELEAEFDEArIEEAREDKERaeeyleqVEEKLDELREERDDLQAEIGAVENEL 690
|
330
....*....|...
gi 1720366994 436 KTLKEEEKAKEAL 448
Cdd:PRK02224 691 EELEELRERREAL 703
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
111-469 |
3.04e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 111 LGRMALEFNRLASKVHKNE---QRTSILQTLCEQLRQENEALK-AKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEG 186
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAaakKKADEAKKKAEEKKKADEAKKkAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 187 LCGQPSSPKPEGAGKKGVAGQQQASVMASKvpeAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELR 266
Cdd:PTZ00121 1476 KKKAEEAKKADEAKKKAEEAKKKADEAKKA---AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 267 qKLVDLQKqvTELEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLspltRQREYQEKEIQRL 346
Cdd:PTZ00121 1553 -KAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA----KKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 347 NKALEEALSIQASPSSPPAAFGSPEgvggHLRKQElvTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQA 426
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAE----ELKKAE--EENKIKAAEEAKKAEE-DKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1720366994 427 QVTLTNAQLKTLKEEEKAK-EALKQQKRKAKASGERYHMEPHPE 469
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKaEELKKAEEENKIKAEEAKKEAEED 1742
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
256-435 |
3.22e-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: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 256 QQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVRYLQDqlSP- 331
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSARYTPN--HPd 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 332 ---LTRQREYQEKEIQRLNKALEEALSIQASpssppaafgspegvGGHLRKQELVTQNELLKQQVKIFEEDfQRERSDRE 408
Cdd:COG3206 293 viaLRAQIAALRAQLQQEAQRILASLEAELE--------------ALQAREASLQAQLAQLEARLAELPEL-EAELRRLE 357
|
170 180 190
....*....|....*....|....*....|...
gi 1720366994 409 RMNEEKEE-----LKKQVE-KLQAQVTLTNAQL 435
Cdd:COG3206 358 REVEVARElyeslLQRLEEaRLAEALTVGNVRV 390
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
241-457 |
3.40e-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: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 241 LEVNKQW--DQHFRSMKQQYEQKITELRQklvdLQKQVTELEAER--EQKQRDfdrKLLLAKSKIEMEETDKE-QLTAEA 315
Cdd:pfam01576 718 LEVNMQAlkAQFERDLQARDEQGEEKRRQ----LVKQVRELEAELedERKQRA---QAVAAKKKLELDLKELEaQIDAAN 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 316 K---ELRQKVRYLQDQLSPLTRQRE----------YQEKEIQRLNKALE-EALSIQASPSSPPAAFG---------SPEG 372
Cdd:pfam01576 791 KgreEAVKQLKKLQAQMKDLQRELEearasrdeilAQSKESEKKLKNLEaELLQLQEDLAASERARRqaqqerdelADEI 870
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 373 VGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTltnAQLKTLKEEEKAKEALKQQK 452
Cdd:pfam01576 871 ASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA---AERSTSQKSESARQQLERQN 947
|
....*
gi 1720366994 453 RKAKA 457
Cdd:pfam01576 948 KELKA 952
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
229-351 |
3.47e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.90 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 229 KVKLLEQQRMELLEVNKQWDQHF----RSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKQRDFDRklllAKSKIEME 304
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1720366994 305 ETDKEQLTAEAKELRQkvrylqdQLSPLTRQREYQEKEIQRLNKALE 351
Cdd:pfam00038 95 LNLRTSAENDLVGLRK-------DLDEATLARVDLEAKIESLKEELA 134
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
249-372 |
3.71e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 249 QHFRSMKQQYEQKITELRQKLVDLQKQVTELEAEREQKqrdfdrklllakskiemeETDKEQLTAEAKELRQKVRYLQDQ 328
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL------------------EAQQAEQEALLAQLSAEEAAAEAQ 197
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720366994 329 LSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGSPEG 372
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
120-427 |
3.88e-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: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 120 RLASKVHKNEQRTSILQTLCEQLRQENEALKAKLDKGLEQRDLAAERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGA 199
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREK 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 200 GKKGVAGQQQASVMASKVPEAGAFGAAEKKVKLLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTEL 279
Cdd:pfam02463 783 TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 280 EAEREQKQRDFDRKLLLAKSKI---EMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 356
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLkdeLESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720366994 357 QASPSSPPAAFGSPE----GVGGHLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 427
Cdd:pfam02463 943 EEADEKEKEENNKEEeeerNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
235-440 |
4.98e-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: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 235 QQRMELLEvNKQWD--QHFRSMKQQYEQKitelRQKLVDLQKQVTELEAEREQKQRDFDRKlllAKSKIEMEEtDKEQLT 312
Cdd:pfam10174 309 QTKLETLT-NQNSDckQHIEVLKESLTAK----EQRAAILQTEVDALRLRLEEKESFLNKK---TKQLQDLTE-EKSTLA 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 313 AEAKELRQ-------KVRYLQDQLSPLTRQREYQEKEIQRLNKALEealSIQASPSSPPAAfgspegvgghlrkqeLVTQ 385
Cdd:pfam10174 380 GEIRDLKDmldvkerKINVLQKKIENLQEQLRDKDKQLAGLKERVK---SLQTDSSNTDTA---------------LTTL 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720366994 386 NELLKQQVKIFEE-DFQRERSDRERMNE------EKEELKKQVEKLQAQVTLTNAQLKTLKE 440
Cdd:pfam10174 442 EEALSEKERIIERlKEQREREDRERLEEleslkkENKDLKEKVSALQPELTEKESSLIDLKE 503
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
384-456 |
5.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 5.36e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720366994 384 TQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLTNAQLKTLKEE-EKAKEALKQQKRKAK 456
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiAEAEAEIEERREELG 89
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
219-354 |
5.55e-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: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 219 EAGAfgaaekKVKL--------LEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTELEAeREQKQRDF 290
Cdd:COG0542 397 EAAA------RVRMeidskpeeLDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKEL 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 291 DRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEE 352
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEE 545
|
..
gi 1720366994 353 AL 354
Cdd:COG0542 546 EL 547
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
259-428 |
5.99e-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: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 259 EQKITELRQK------LVD----LQKQVTELEAEREQ---KQRDFDRKL-----LLAKSKIEMEET--DKEQLTAEAKEL 318
Cdd:pfam15066 345 EKKVKELQMKitkqqvFVDiinkLKENVEELIEDKYNvilEKNDINKTLqnlqeILANTQKHLQESrkEKETLQLELKKI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 319 rqKVRYLQDQLSPLTrqreyqekEIQRLNKALEEALSIQASPSSPPAAFGSPEGVGGHLRKqelVTQN--ELLKQQVKIF 396
Cdd:pfam15066 425 --KVNYVHLQERYIT--------EMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEK---ATTSalDLLKREKETR 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 1720366994 397 EEDF---QRERSDRERMN-EEKEELKKQVEKLQAQV 428
Cdd:pfam15066 492 EQEFlslQEEFQKHEKENlEERQKLKSRLEKLVAQV 527
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
242-352 |
6.03e-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: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 242 EVNKQWDQHFRSMKQQYEQKITELRQKLVDLQKQVTEL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 320
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
|
90 100 110
....*....|....*....|....*....|..
gi 1720366994 321 KVRYLQDQLSplTRQREYQEKEIQRLNKALEE 352
Cdd:smart00935 77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-435 |
6.33e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 260 QKITELRQKLVDLQKQVTELEAEREqkqrDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVRYLQDQLSPLTRQREYQ 339
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERERE----ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 340 EKEIQrlnkalEEALSIQASPSSPPAAFGSPEgvgghlrkqELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKK 419
Cdd:PRK02224 327 RDRLE------ECRVAAQAHNEEAESLREDAD---------DLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
170
....*....|....*.
gi 1720366994 420 QVEKLQAQVTLTNAQL 435
Cdd:PRK02224 392 EIEELRERFGDAPVDL 407
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
311-442 |
7.68e-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: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 311 LTAEAKELRQKVRYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQASPSSPPAAFGSPEGvgghlRKQELVTQNELL 389
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQLATERS-----ARREAEAELERL 119
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720366994 390 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQvtLTNAQLKTLKEEE 442
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQ--LTSKSQSSSSQSE 167
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
144-456 |
8.59e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.05 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 144 QENEALKAKLDKGLEQRDLA---AERLREENTELKKLLMNSSCKEGLCGQPSSPKPEGAGKKGVAGQQQASVMASKVPEA 220
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSArekQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAER 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 221 GAFgaAEKKVKLLEQQRMELLEVNKQWDQHF-------RSMKQQYEQKITELRQKLVDLQKQVTELE---AEREQKQRDF 290
Cdd:pfam12128 677 KDS--ANERLNSLEAQLKQLDKKHQAWLEEQkeqkreaRTEKQAYWQVVEGALDAQLALLKAAIAARrsgAKAELKALET 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 291 DRKLLLAK--------SKIEMEETDKEQLTAEAKELRQKV----RYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQA 358
Cdd:pfam12128 755 WYKRDLASlgvdpdviAKLKREIRTLERKIERIAVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLARLI 834
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 359 SPSSppaafgspegvgghLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEElkKQVEKLQAQVTLTNAQLKTL 438
Cdd:pfam12128 835 ADTK--------------LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED--ANSEQAQGSIGERLAQLEDL 898
|
330
....*....|....*....
gi 1720366994 439 KEE-EKAKEALKQQKRKAK 456
Cdd:pfam12128 899 KLKrDYLSESVKKYVEHFK 917
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
232-455 |
9.94e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.05 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 232 LLEQQRMELLEVNKQWDQHFRSMKQQYEQKITELRQKL----VDLQKQVTELEAEREQKQRDFDRKLLLAKSKIEME--- 304
Cdd:pfam12128 273 LIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLpsw 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 305 --------------ETDKEQLTAEAKELRQKVRY-LQDQLSPLTRQREYQEKEIQRLNKALEEALSIQASPSSPPAAFGS 369
Cdd:pfam12128 353 qselenleerlkalTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720366994 370 PEGVGGHLRKQELVTQNELLKQQVKIFEEDF-QRERSDR--ERMNEEKEELKKQVEKLQAQVTltnaQLKTLKEEekAKE 446
Cdd:pfam12128 433 LEFNEEEYRLKSRLGELKLRLNQATATPELLlQLENFDEriERAREEQEAANAEVERLQSELR----QARKRRDQ--ASE 506
|
....*....
gi 1720366994 447 ALKQQKRKA 455
Cdd:pfam12128 507 ALRQASRRL 515
|
|
| |
