|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-477 |
1.74e-11 |
|
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: 67.39 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 246 AAEKKVKMLEQQRSELLEVNKQwdqhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKI 322
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQ----LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeltELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 323 EMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQE 402
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL---------------ESLERRIAA 835
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947865 403 LVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAK 477
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
281-479 |
1.62e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 281 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 360
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 361 EKEIQRLNKALEEAL--SIQTPPSSPPTAFGSPEGAGALLRKQELVTQ-NELLKQQVKIFEEDFQRERSDRERMNEEKEE 437
Cdd:COG4942 96 RAELEAQKEELAELLraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622947865 438 LKKQVEKLQAQvtlsNAQLKAFKDEEKAREANRQQKRKAKAS 479
Cdd:COG4942 176 LEALLAELEEE----RAALEALKAERQKLLARLEKELAELAA 213
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
283-478 |
1.95e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 283 ITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEK 362
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 363 EIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQV 442
Cdd:COG1196 275 ELEELELELEEAQA----------------------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622947865 443 EKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
277-448 |
5.20e-10 |
|
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: 59.94 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 277 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 356
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEA----AKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 357 REYQ--EKEI---QRLNKALEEALsiqtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRErm 431
Cdd:COG1579 89 KEYEalQKEIeslKRRISDLEDEI------------------LELMERIEELEEELAELEAELAELEAELEEKKAELD-- 148
|
170
....*....|....*..
gi 1622947865 432 nEEKEELKKQVEKLQAQ 448
Cdd:COG1579 149 -EELAELEAELEELEAE 164
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-446 |
1.49e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsNGNKEGASGQPGSPKM 217
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL---EAEIEELEERLEEAEE 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 218 EGAGKKAVAGQQQASVTAGK---VPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYE---QKITELRQKLA 291
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKeelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEdleEQIEELSEDIE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 292 DLQKQVTDLEAEREQKQRDFDRKL-LLAKSKIEMEE--TDKEQLTAEAKELRQKVKYLQDQLSPLTRQRE-YQEK----- 362
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLnERASLEEALALlrSELEELSEELRELESKRSELRRELEELREKLAqLELRlegle 935
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 363 -EIQRLNKALEEALSI--QTPPSSPPTAFGSPEGAgallrKQELvtqnELLKQQVKIF-------EEDFQRERSDRERMN 432
Cdd:TIGR02168 936 vRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEA-----RRRL----KRLENKIKELgpvnlaaIEEYEELKERYDFLT 1006
|
330
....*....|....
gi 1622947865 433 EEKEELKKQVEKLQ 446
Cdd:TIGR02168 1007 AQKEDLTEAKETLE 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
248-467 |
2.02e-09 |
|
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: 60.42 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 248 EKKVKMLEQQRSELLEVNKQWDQHFRS---MKQQYEQKITELRQ---KLADLQKQVTDLEAERE----QKQRDFDRKLll 317
Cdd:TIGR04523 235 EKKQQEINEKTTEISNTQTQLNQLKDEqnkIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlnnQKEQDWNKEL-- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 318 aKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS-IQTPPSspptafgspEGAGA 396
Cdd:TIGR04523 313 -KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNeIEKLKK---------ENQSY 382
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622947865 397 LLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKARE 467
Cdd:TIGR04523 383 KQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
283-476 |
2.07e-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: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 283 ITELRQKLADLQKQVT------DLEAEREQKQ--------RDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQD 348
Cdd:TIGR02168 195 LNELERQLKSLERQAEkaerykELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 349 QLSPLtrqreyqEKEIQRLNKALEEALSIQtppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDR 428
Cdd:TIGR02168 275 EVSEL-------EEEIEELQKELYALANEI---------------SRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622947865 429 ERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKA 476
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
138-376 |
2.20e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkegasgqpgspkm 217
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL------------------- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 218 egAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---EQKITELRQKLADLQ 294
Cdd:COG1196 329 --EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELleaLRAAAELAAQLEELE 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 295 KQVTDLE---AEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL 371
Cdd:COG1196 407 EAEEALLerlERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
....*
gi 1622947865 372 EEALS 376
Cdd:COG1196 487 AEAAA 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
272-478 |
2.48e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 272 FRSMKQQYEQKITELR-QKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQL 350
Cdd:COG1196 215 YRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEE----LEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 351 SPLTRQREYQEKEIQRLNKALEEALSiqtppsspptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRER 430
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEE----------------------RLEELEEELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622947865 431 MNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
275-462 |
2.73e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 275 MKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFD-RKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLS 351
Cdd:COG4913 247 AREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAqRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 352 PLTRQREYQ--------EKEIQRLNKALEE-------------ALSIQTPPSspptafgspegAGALLRKQELVTQN-EL 409
Cdd:COG4913 327 ELEAQIRGNggdrleqlEREIERLERELEErerrrarleallaALGLPLPAS-----------AEEFAALRAEAAALlEA 395
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622947865 410 LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 462
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-482 |
3.06e-08 |
|
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: 57.00 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 117 SVCAEEPDHSQLFTH-LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLEL 195
Cdd:TIGR02169 667 LFSRSEPAELQRLRErLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 196 KKLLMSNGNKegasgqpgspKMEGAGKKAVAGQQQASVTAGKVpEVAALGA--AEKKVKMLEQQRSELLEVNKQWDQHFR 273
Cdd:TIGR02169 747 SSLEQEIENV----------KSELKELEARIEELEEDLHKLEE-ALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 274 SMkqqyEQKITELRQKLADLQKQVTDLEAEREQKQrdfDRKLLLAKsKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPL 353
Cdd:TIGR02169 816 EI----EQKLNRLTLEKEYLEKEIQELQEQRIDLK---EQIKSIEK-EIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 354 TRQREYQEKEIQRLNKALEEA-LSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMN 432
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELeAQIEK----------------KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622947865 433 EEkEELKKQVEKLQAQV-TLSNAQLKAFKD-EEKAREANRQQKRKAKASGER 482
Cdd:TIGR02169 952 SL-EDVQAELQRVEEEIrALEPVNMLAIQEyEEVLKRLDELKEKRAKLEEER 1002
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
242-448 |
3.47e-08 |
|
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: 55.93 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 242 AALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQ---YEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR----- 313
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAEllral 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 314 ---------KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSiqtppssp 384
Cdd:COG4942 114 yrlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE-------- 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947865 385 ptafgspegagallRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 448
Cdd:COG4942 186 --------------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| UBAN |
cd09803 |
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ... |
400-448 |
5.37e-08 |
|
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: 50.43 E-value: 5.37e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1622947865 400 KQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQ 448
Cdd:cd09803 34 QEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
276-478 |
6.02e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.22 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 276 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSplTR 355
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELG--ER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 356 QREYQEKeiQRLNKALEEALSIQtppsSPPTAFGSPEGAGALLRKQ-ELVTQNELLKQQVKIFEEDFQRERSDRERMNEE 434
Cdd:COG3883 92 ARALYRS--GGSVSYLDVLLGSE----SFSDFLDRLSALSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622947865 435 KEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
277-481 |
9.92e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 277 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRQ 356
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEEL-----------EEELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 357 REYQEKEIQRLNKALEEALSIQTPPSSpptafgspEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKE 436
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEE--------RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622947865 437 ELKkqVEKLQAQVTLSNAQlkaFKDEEKAREANRQQKRKAKASGE 481
Cdd:TIGR02168 814 LLN--EEAANLRERLESLE---RRIAATERRLEDLEEQIEELSED 853
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
177-446 |
1.67e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 177 GLEQRDQAAERL-------REENLELKKLLMSNGNKEGasgqpgspKMEGAGKKAVAGQQQASVTAGKVPEVAA-LGAAE 248
Cdd:PRK03918 156 GLDDYENAYKNLgevikeiKRRIERLEKFIKRTENIEE--------LIKEKEKELEEVLREINEISSELPELREeLEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 249 KKVKMLEQQRSELLEVNKQWDQHFRSMK------QQYEQKITELRQKLADLQKQVTDLE-----AEREQKQRDFDRKLLL 317
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVKELKelkekAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 318 AKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLN---KALEEALSIQTPPSSPPTAFGSpega 394
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERLKKRLTG---- 383
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622947865 395 galLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQ 446
Cdd:PRK03918 384 ---LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-478 |
2.73e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.99 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREEnlELKKLLMSNGNKEGASGQPGSPKM 217
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 218 EGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQV 297
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE----KKKEEAKKKADAAKKKAEEKKKA 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 298 TDLE--AEREQKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVKylQDQLSPLTRQREYQEKEIQRLNKALEEAL 375
Cdd:PTZ00121 1394 DEAKkkAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKADEAKKKAE--EAKKADEAKKKAEEAKKAEEAKKKAEEAK 1470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 376 SIQTPPSSPPTAFGSPEG---AGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK---EELKKQVEKLQAQV 449
Cdd:PTZ00121 1471 KADEAKKKAEEAKKADEAkkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkaDEAKKAEEKKKADE 1550
|
330 340
....*....|....*....|....*....
gi 1622947865 450 TLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
280-478 |
3.43e-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: 53.53 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 280 EQKITELRQKLADLQKQVTDLEAEREQKQRDfdRKLLLAKSKIEMEEtdkeqLTAEAKELRQKVKYLQDQLSPLTRQREY 359
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYE-----LLKEKEALERQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 360 QEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFE---EDFQRER----SDRERMN 432
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKErelEDAEERLakleAEIDKLL 335
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622947865 433 EEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKA 478
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
155-477 |
6.48e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 155 ILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGasgqpgspKMEGAGKKAVAGQQQASVT 234
Cdd:COG4717 43 IRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE--------ELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 235 AGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrsmkqqYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRK 314
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEE--------LEERLEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 315 LLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREY--QEKEIQRLNKALEEALSIQ---------TPPSS 383
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLliaaallalLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 384 PPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQL-KAFKDE 462
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlELLDRI 346
|
330
....*....|....*
gi 1622947865 463 EKAREANRQQKRKAK 477
Cdd:COG4717 347 EELQELLREAEELEE 361
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
276-442 |
9.83e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 276 KQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIemeetdkEQLTAEAK-ELRQKVKYL-QDQLSPL 353
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA-------QQAIKEAKkEADEIIKELrQLQKGGY 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 354 TRQREYQEKEIQR-LNKALEEALSIQTPPSSPPTAF--------GSPEGAGALLRK---QELVTQNELLKQQVKIfeedf 421
Cdd:PRK00409 602 ASVKAHELIEARKrLNKANEKKEKKKKKQKEKQEELkvgdevkyLSLGQKGEVLSIpddKEAIVQAGIMKMKVPL----- 676
|
170 180
....*....|....*....|.
gi 1622947865 422 qrerSDRERMNEEKEELKKQV 442
Cdd:PRK00409 677 ----SDLEKIQKPKKKKKKKP 693
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
132-442 |
1.29e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 132 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngnkEGASGQ 211
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL-------EARLSH 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 212 PGSPKMEGAGKKAvagQQQASVTAGKVPEV-AALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELR 287
Cdd:TIGR02169 791 SRIPEIQAELSKL---EEEVSRIEARLREIeQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEELE 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 288 QKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLtrqrEYQEKEIQRL 367
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDE----LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL----EEELSEIEDP 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 368 NKALEEalsiqTPPSSPP---------------TAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEdfqreRSDRERMN 432
Cdd:TIGR02169 940 KGEDEE-----IPEEELSledvqaelqrveeeiRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEE-----RKAILERI 1009
|
330
....*....|
gi 1622947865 433 EEKEELKKQV 442
Cdd:TIGR02169 1010 EEYEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
244-445 |
2.69e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 244 LGAAEKKVKMLEQQRSELLEVNKQWDQhfrsMKQQYEQ---KITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKS 320
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAA----LEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 321 KIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS--IQTPPSSPPTAFGSPEGAGALL 398
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRafNREWPAETADLDADLESLPEYL 818
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622947865 399 RKQELVTQNELLKQQVKIFEedFQRERSDRE------RMNEEKEELKKQVEKL 445
Cdd:COG4913 819 ALLDRLEEDGLPEYEERFKE--LLNENSIEFvadllsKLRRAIREIKERIDPL 869
|
|
| CC2-LZ |
pfam16516 |
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ... |
408-450 |
4.50e-06 |
|
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.
Pssm-ID: 465155 [Multi-domain] Cd Length: 100 Bit Score: 45.36 E-value: 4.50e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622947865 408 ELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVT 450
Cdd:pfam16516 55 SVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQRQNQ 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-378 |
4.51e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENlelKKLLMSNGNKEGasgqpgspkM 217
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE---EKLEELKEELES---------L 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 218 EGAGKKAVAGQQQASvtagkvpevAALGAAEKKvkmLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQV 297
Cdd:TIGR02168 357 EAELEELEAELEELE---------SRLEELEEQ---LETLRSKVAQLELQ--------IASLNNEIERLEARLERLEDRR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 298 TDLEAEREQKQRDFDR-KLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 376
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
..
gi 1622947865 377 IQ 378
Cdd:TIGR02168 497 LQ 498
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-492 |
6.69e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 134 RMALEFNRLASKVHKNEQrtsiLQTLCEQLRKENEALK-AKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQP 212
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEE----AKKKAEEAKKADEAKKkAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 213 GSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEK-----KVKMLEQQRSEllEVNKQWDQHFRSMKQQYEQKITELR 287
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaeEKKKAEEAKKA--EEDKNMALRKAEEAKKAEEARIEEV 1597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 288 QKLADLQKQVTDLEAEREQKQR---DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEI 364
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 365 QRLNKALEEalsiqtppsspptafgSPEGAGALLRKQELVTQNELLKQQVkifeedfQRERSDRERMNEEKEELKKQVEK 444
Cdd:PTZ00121 1678 EEAKKAEED----------------EKKAAEALKKEAEEAKKAEELKKKE-------AEEKKKAEELKKAEEENKIKAEE 1734
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1622947865 445 LQAqvtlsnaqlKAFKDEEKAREANRQQKRKAKASGERYHVEPHPEHL 492
Cdd:PTZ00121 1735 AKK---------EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-477 |
7.41e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 143 ASKVHKNEQRTSILQTLCEQLRKENEALKAKLD--KGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMEGA 220
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEekKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE 1435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 221 GKKAVAGQQQASVTAGKVPEvaALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ---KITELRQ--------- 288
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEE--AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEakkKADEAKKaaeakkkad 1513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 289 --KLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQR 366
Cdd:PTZ00121 1514 eaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 367 LNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNEllkQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQ 446
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV---EQLKKKEAE-EKKKAEELKKAEEENKIKAAEEAKK 1669
|
330 340 350
....*....|....*....|....*....|.
gi 1622947865 447 AQVTLSNAQlKAFKDEEKAREANRQQKRKAK 477
Cdd:PTZ00121 1670 AEEDKKKAE-EAKKAEEDEKKAAEALKKEAE 1699
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
132-448 |
7.76e-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: 49.20 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 132 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQ 211
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 212 PGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLA 291
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 292 DLQKQVTDLEAEREQK--------QRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ--E 361
Cdd:pfam02463 835 LEELALELKEEQKLEKlaeeelerLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLleE 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 362 KEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAG----------------ALLRKQELVTQNELLKQQVKIFEEDFQRER 425
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKekeennkeeeeernkrLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
330 340
....*....|....*....|...
gi 1622947865 426 SDRERMNEEKEELKKQVEKLQAQ 448
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQ 1017
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-397 |
9.29e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 138 EFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmsngnkegasgqpgspKM 217
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----------------AE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 218 EGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQrsellevnkqwdQHFRSMKQQYEQKITELRQKLADLQKQV 297
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL------------QYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 298 TDLEAEREQKQRDfdrklllakskIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSI 377
Cdd:COG4942 167 AELEAERAELEAL-----------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250 260
....*....|....*....|
gi 1622947865 378 QTPPSSPPTAFGSPEGAGAL 397
Cdd:COG4942 236 AAAAAERTPAAGFAALKGKL 255
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
110-369 |
9.63e-06 |
|
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: 48.68 E-value: 9.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 110 QRLETTLSVCAEEPDHSQLFTHLGRMALEFNRL----------ASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLDK 176
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTALKNARLdlrrlfdekqSEKDKKNKALAERKDSANERLNSleaQLKQLDKKHQA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 177 GLEQRDQAAERLREENLELKKLLMSNgnkegASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQ 256
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQVVEGA-----LDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKR 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 257 QRSEL------LEVNKQ-------WDQH-FRSMKQQYEQKITELRQKLADLQKQVTDLEAERE------QKQRDFDRKLL 316
Cdd:pfam12128 776 EIRTLerkierIAVRRQevlryfdWYQEtWLQRRPRLATQLSNIERAISELQQQLARLIADTKlrraklEMERKASEKQQ 855
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947865 317 ------LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 369
Cdd:pfam12128 856 vrlsenLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
150-477 |
9.81e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 150 EQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQaaeRLREENLELKKLLmsnGNKEGASGQpgspKMEGAGKKAVAGQQ 229
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAERYQAL---LKEKREYEGYELL---KEKEALERQ----KEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 230 QASVTAgkvpevaalgAAEKKVKMLEQQRSELLEVNKQwdqhfrsMKQQYEQKITELRQKLADLQKQVTDLE---AEREQ 306
Cdd:TIGR02169 253 LEKLTE----------EISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLErsiAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 307 KQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppssppt 386
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE------------- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 387 afgspegagallrkqelvTQNELLKQQVKIfeEDFQRERSD----RERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 462
Cdd:TIGR02169 383 ------------------TRDELKDYREKL--EKLKREINElkreLDRLQEELQRLSEELADLNAAIAGIEAKINELEEE 442
|
330
....*....|....*.
gi 1622947865 463 -EKAREANRQQKRKAK 477
Cdd:TIGR02169 443 kEDKALEIKKQEWKLE 458
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
248-472 |
1.14e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 248 EKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTDLEAEREQKQrdfdrklllakSKIEMEET 327
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKE--------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD-----------EQIKKLQQ 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 328 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspegagallrkqelvtqn 407
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---------------------------------- 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947865 408 elLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQ 472
Cdd:TIGR04523 466 --LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
141-477 |
1.39e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 141 RLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMEga 220
Cdd:pfam02463 174 ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 221 gkkavagqqqasvtagkvpEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhfrSMKQQYEQKITELRQKLADLQKQVTDL 300
Cdd:pfam02463 252 -------------------EIESSKQEIEKEEEKLAQVLKENKEEEKEKK---LQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 301 EAEREQKQRDfDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQreyQEKEIQRLNKALEEALSIQTP 380
Cdd:pfam02463 310 VDDEEKLKES-EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL---QEKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 381 PSSPPTAFGSpEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFK 460
Cdd:pfam02463 386 LSSAAKLKEE-ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330
....*....|....*..
gi 1622947865 461 DEEKAREANRQQKRKAK 477
Cdd:pfam02463 465 LELKKSEDLLKETQLVK 481
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
269-472 |
1.59e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 269 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQ-KQR----DFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKV 343
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 344 KYLQDQL-------SPLTRQREYQE--KEIQRLNKALEEALSIQTPpsspptafGSPEGAGAllrKQELVTQNELLKQQV 414
Cdd:COG3206 243 AALRAQLgsgpdalPELLQSPVIQQlrAQLAELEAELAELSARYTP--------NHPDVIAL---RAQIAALRAQLQQEA 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947865 415 KifeEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQ 472
Cdd:COG3206 312 Q---RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVAREL 366
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
263-492 |
1.77e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 263 EVNKQWDqhfrSMKQQYE--QKITELRQKLADLQKQVTDLEAEREQKQRDFdrklllAKSKIEMEETDKEQLTAEAKELR 340
Cdd:TIGR02168 197 ELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEELREELEE------LQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 341 QKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEA-LSIQTPPSSPPTAFGSPEGAGALLR--KQELVTQNELLKQQVKIF 417
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLANLERQLEELEAQLEelESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622947865 418 EEDfqrersdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFkdEEKAREANRQQKRKAKASGERYHVEPHPEHL 492
Cdd:TIGR02168 347 EEL-------KEELESLEAELEELEAELEELESRLEELEEQL--ETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-377 |
2.19e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 141 RLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLReenlELKKLLMSNGnkegasgqpgspkmega 220
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD----ELEAQIRGNG----------------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 221 gkkavaGQQqasvtagkvpevaaLGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL 300
Cdd:COG4913 337 ------GDR--------------LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947865 301 EAEREQKQRDFDRKlllakskiemeETDKEQLTAEAKELRQKVKYLQDQLSPLTRqreyqekEIQRLNKALEEALSI 377
Cdd:COG4913 397 EEELEALEEALAEA-----------EAALRDLRRELRELEAEIASLERRKSNIPA-------RLLALRDALAEALGL 455
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
149-374 |
2.97e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 149 NEQRTSILQTLcEQLRKENEALKAKLdkglEQRDQAAERLREENlelkKLLMSNGNKEGASGQpgspkmegagkKAVAGQ 228
Cdd:COG3206 167 ELRREEARKAL-EFLEEQLPELRKEL----EEAEAALEEFRQKN----GLVDLSEEAKLLLQQ-----------LSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 229 QQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEvnkqwDQHFRSMKQQY---EQKITELRQKLAD-------LQKQVT 298
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLaelEAELAELSARYTPnhpdviaLRAQIA 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947865 299 DLEAEREQKQRdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYL---QDQLSPLTRQREYQEKEIQRLNKALEEA 374
Cdd:COG3206 302 ALRAQLQQEAQ---RILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
248-481 |
3.60e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 248 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQkladlqkqvtDLEAEREQKQRDFDRKLLLAKSKIEMEET 327
Cdd:pfam17380 356 EERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ----------ELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 328 DKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQEL---- 403
Cdd:pfam17380 426 RAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELeerk 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 404 -----------VTQNELLKQQVKIFEEDfQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFkdeEKAREANRQQ 472
Cdd:pfam17380 506 qamieeerkrkLLEKEMEERQKAIYEEE-RRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAM---EREREMMRQI 581
|
....*....
gi 1622947865 473 KRKAKASGE 481
Cdd:pfam17380 582 VESEKARAE 590
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
248-455 |
3.68e-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: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 248 EKKVKMLEQQRSELLEVNKQWDQHFRSMKQQY---EQKITELRQKLADLQKQVTDLEAE---------------REQKQR 309
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKellEKEIERLKETIIKNNSEIKDLTNQdsvkeliiknldntrESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 310 DFDRKLLLAKSKIEMEETDKE---------QLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEealSIQTP 380
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKElkskekelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS---DLEDE 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 381 PSSPPTAFGSPEGAGALLRKQELV-----TQNELLKQQVKiFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQ 455
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNKEIeelkqTQKSLKKKQEE-KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
138-457 |
3.81e-05 |
|
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: 46.65 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 138 EFNRLASKVHKNEQRTSILQTLCEQLRK---ENEALKAKLdkglEQRDQAAERLREENLELKKLLMSNGNKEGA------ 208
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAmqveka 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 209 --SGQPGSPKME-------GAGKKAVAGQQQASVTAGKVPEVAALGAAEKK---VKMLEQQRSELLEVNKQWDQHFRSMK 276
Cdd:pfam15921 594 qlEKEINDRRLElqefkilKDKKDAKIRELEARVSDLELEKVKLVNAGSERlraVKDIKQERDQLLNEVKTSRNELNSLS 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 277 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSkieMEETD----------KEQLTAEAKE---LRQKV 343
Cdd:pfam15921 674 EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS---MEGSDghamkvamgmQKQITAKRGQidaLQSKI 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 344 KYLQDQLSPLTRQREYQEKEIQRLNKALeealsiqtppSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQR 423
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLSQEL----------STVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622947865 424 ERSDR--ERMNEEKEELKKQ----VEKLQAQVTLSNAQLK 457
Cdd:pfam15921 821 AECQDiiQRQEQESVRLKLQhtldVKELQGPGYTSNSSMK 860
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
243-347 |
5.93e-05 |
|
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: 45.36 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 243 ALGAAEKKVKM-------LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkl 315
Cdd:pfam02841 198 ALTAKEKAIEAerakaeaAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEK----------MEAEREQLLAEQER-- 265
|
90 100 110
....*....|....*....|....*....|..
gi 1622947865 316 LLAKSKIEMEETDKEQLTAEAKELRQKVKYLQ 347
Cdd:pfam02841 266 MLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
280-476 |
5.96e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 280 EQKITELRQKLADLQKQVTDLEAEREQKQRDFD--RKLLLAKSKIEM---EETDKEQLTAEAKELRQKVKYL---QDQLS 351
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEyswDEIDVASAEREIAELEAELERLdasSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 352 PLTRQREYQEKEIQRLNKALEealsiqtppsspptafgspegagallrkqELVTQNELLKQQVKIFEEDFQRERSDRERM 431
Cdd:COG4913 689 ALEEQLEELEAELEELEEELD-----------------------------ELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622947865 432 NE-EKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKA 476
Cdd:COG4913 740 EDlARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRA 785
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
237-367 |
6.28e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 237 KVPEVAALGAAEKKVKMLEQQRSE--------LLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVtdleaerEQKQ 308
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEaeaikkeaLLEAKEEIHK----LRNEFEKELRERRNELQKLEKRL-------LQKE 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947865 309 RDFDRKLLLAKSKiemeetdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL 367
Cdd:PRK12704 96 ENLDRKLELLEKR-------EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
71-464 |
6.70e-05 |
|
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: 45.88 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 71 EFEVVTPEEQSSPPENSSHANETVLGPLPHEDGNLMLHLQRLETTLSVCAEEPDhsqlfthlGRMALEFNRLASKVHKNE 150
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQ--------GQMERQMAAIQGKNESLE 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 151 QRTSI---LQTLCEQLRKENEALKAK-------------LDKGLEQRDQAAERLREE--------NLELKKL--LMSNGN 204
Cdd:pfam15921 462 KVSSLtaqLESTKEMLRKVVEELTAKkmtlessertvsdLTASLQEKERAIEATNAEitklrsrvDLKLQELqhLKNEGD 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 205 K-EGASGQPGSPKMEGAGKKAVAG---QQQASVT--AGKVPEVAALGAAEKKV--KMLEQQRSELlevnkqwdQHFRSMK 276
Cdd:pfam15921 542 HlRNVQTECEALKLQMAEKDKVIEilrQQIENMTqlVGQHGRTAGAMQVEKAQleKEINDRRLEL--------QEFKILK 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 277 QQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllAKSKIEMEetdKEQLTAEAKELRQKVKYLQDQLSPLTRQ 356
Cdd:pfam15921 614 DKKDAKIRELEARVSDLELEKVKLVNAGSERLR--------AVKDIKQE---RDQLLNEVKTSRNELNSLSEDYEVLKRN 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 357 REYQEKEIQRLNKALEEAL-SIQTPPSSPPTAFGSPEGAGALLRKQELVTQNEL---------LKQQVKIFEEDFQRERS 426
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLkSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQItakrgqidaLQSKIQFLEEAMTNANK 762
|
410 420 430
....*....|....*....|....*....|....*...
gi 1622947865 427 DRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEK 464
Cdd:pfam15921 763 EKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-482 |
7.38e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 287 RQKLADLQKQVTDLEAEREQkqrdfdrklllakskiemeetdkeqLTAEAKELRQKVKYLQDQLSPLTRQREYQ------ 360
Cdd:COG4913 609 RAKLAALEAELAELEEELAE-------------------------AEERLEALEAELDALQERREALQRLAEYSwdeidv 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 361 ---EKEIQRLNKALEEALSiqtppsspptafGSPEgagalLRKqelvtqnelLKQQVKIFEEDFQRERSDRERMNEEKEE 437
Cdd:COG4913 664 asaEREIAELEAELERLDA------------SSDD-----LAA---------LEEQLEELEAELEELEEELDELKGEIGR 717
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622947865 438 LKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKASGER 482
Cdd:COG4913 718 LEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
230-332 |
8.51e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 230 QASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR 309
Cdd:PRK11448 140 PENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRK 219
|
90 100
....*....|....*....|...
gi 1622947865 310 DFDRKlllAKSKIEMEETDKEQL 332
Cdd:PRK11448 220 EITDQ---AAKRLELSEEETRIL 239
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
258-461 |
9.15e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 258 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKqvtdleaeREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 337
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAEQ-LQQLRMRLSELEQ--------RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 338 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLnKALEEALSIQTPpsspptAFGSPEGAGALLRKQ---ELVTQNEL--LKQ 412
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQL-QARIQRLAARAP------AWLAAQDALARLREQsgeEFEDSQDVteYMQ 634
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622947865 413 QVKIFEEDFQRErsdRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 461
Cdd:PRK04863 635 QLLERERELTVE---RDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
109-492 |
1.02e-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: 45.49 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 109 LQRLETTLsVCAEEPDHSQLFTHLGRMALEFNRLASKVHKneqrtsilqtLCEQLRKENEALKAKLdkgLEQRDQAAERL 188
Cdd:pfam15921 186 LQEIRSIL-VDFEEASGKKIYEHDSMSTMHFRSLGSAISK----------ILRELDTEISYLKGRI---FPVEDQLEALK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 189 REENLELKKLLMSNGNKEGASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQW 268
Cdd:pfam15921 252 SESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE--QARNQNSMYMRQLSDLESTVSQL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 269 DQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQR------DFDRKLLLAKSKIEME-ETDKEQltaeAKELRQ 341
Cdd:pfam15921 330 RSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnldDQLQKLLADLHKREKElSLEKEQ----NKRLWD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 342 KVKYLQDQLSPLTRQREYQEKEIQRLNkaleealsiqtppsspptafgspegagALLRKQELVTQNELLKQQVKI--FEE 419
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNMEVQRLE---------------------------ALLKAMKSECQGQMERQMAAIqgKNE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 420 DFQRERSDRERMNEEKEELKKQVEKLQA-QVTLSNAQ------LKAFKDEEKAREANRQQKRKAKAS-----GERYHVEP 487
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEMLRKVVEELTAkKMTLESSErtvsdlTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKN 538
|
....*
gi 1622947865 488 HPEHL 492
Cdd:pfam15921 539 EGDHL 543
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
144-396 |
1.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 144 SKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLlmsngNKEGASGQPGSPKMEGAGKK 223
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL-----QAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 224 AVAGQQQASVTAGKVPEV-------AALGAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQ 296
Cdd:COG3883 91 RARALYRSGGSVSYLDVLlgsesfsDFLDRLSALSKIADADADLLEELKAD--------KAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 297 VTDLEAEREQKQrdfdrklllakskiemeeTDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALS 376
Cdd:COG3883 163 KAELEAAKAELE------------------AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
250 260
....*....|....*....|
gi 1622947865 377 IQTPPSSPPTAFGSPEGAGA 396
Cdd:COG3883 225 AAAAAAAAAAAAAAAAAAAA 244
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
248-475 |
1.18e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 248 EKKVKMLEQQRSELLEvnkqwDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK------ 321
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLK-----LELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTqtqlnq 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 322 -IEMEETDKEQLTAEAKELRQ---KVKYLQDQLSPLTRQRE--YQEKEiQRLNKALEEALSIQtppsspptafgspegag 395
Cdd:TIGR04523 258 lKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISdlNNQKE-QDWNKELKSELKNQ----------------- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 396 allRKQELVTQNEL---------LKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAR 466
Cdd:TIGR04523 320 ---EKKLEEIQNQIsqnnkiisqLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
....*....
gi 1622947865 467 EANRQQKRK 475
Cdd:TIGR04523 397 ESKIQNQEK 405
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
244-484 |
1.83e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 244 LGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFdRKLLLAKSKIE 323
Cdd:PHA02562 190 IDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAAL-NKLNTAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 324 MEetdKEQLTAEAKELRQ----------------KVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppssppta 387
Cdd:PHA02562 269 SK---IEQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK-------- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 388 fgspegagallRKQELVTQNELLKQQVKifeedfqrersdreRMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKARe 467
Cdd:PHA02562 338 -----------KLLELKNKISTNKQSLI--------------TLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI- 391
|
250
....*....|....*..
gi 1622947865 468 anrqQKRKAKASGERYH 484
Cdd:PHA02562 392 ----VKTKSELVKEKYH 404
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
162-199 |
1.87e-04 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 43.43 E-value: 1.87e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1622947865 162 QLRKENEALKAKLDKgLEQRDQAAERLREENLELKKLL 199
Cdd:PRK13922 73 DLREENEELKKELLE-LESRLQELEQLEAENARLRELL 109
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
140-444 |
1.91e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 140 NRLASKVHKNEQRTSILQTLCEQLRKENEALkakldkgleqrDQAAERLREENLELKKLLMSNGNKEGASgqpgSPKMEG 219
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELL-----------EKEIERLKETIIKNNSEIKDLTNQDSVK----ELIIKN 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 220 AGKKAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQwdqhfrsmKQQYEQKITELRQKLADLQKQVTD 299
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQ--NLEQKQKELKSKEKELKKLNEE--------KKELEEKVKDLTKKISSLKEKIEK 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 300 LEAE---REQKQRDFDRKLL-----LAKSKIEME-----------ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQ 360
Cdd:TIGR04523 529 LESEkkeKESKISDLEDELNkddfeLKKENLEKEideknkeieelKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 361 EKEIQRLNKALEEAlsiqtppsspptafgSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKK 440
Cdd:TIGR04523 609 EKKISSLEKELEKA---------------KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
....
gi 1622947865 441 QVEK 444
Cdd:TIGR04523 674 KIDD 677
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
122-396 |
2.24e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 122 EPDHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMS 201
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 202 NgNKEGASGQPGSpkmegagkkAVAGQQQASVTAGKVPEVAALGAAEKkvKMLEQQRSELLEVNKQwdqhfrsmKQQYEQ 281
Cdd:COG3883 95 L-YRSGGSVSYLD---------VLLGSESFSDFLDRLSALSKIADADA--DLLEELKADKAELEAK--------KAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 282 KITELRQKLADLQKQVTDLEAEREQKQrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQE 361
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQE----ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1622947865 362 KEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGA 396
Cdd:COG3883 231 AAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAA 265
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
161-433 |
2.75e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 161 EQLRKENEALKAKLDKGLEQRDQAaERLREENLELKKLLmsngnkegasgqpgspkmegagkkAVAGQQQASVTAgkvpE 240
Cdd:PRK11281 52 KLLEAEDKLVQQDLEQTLALLDKI-DRQKEETEQLKQQL------------------------AQAPAKLRQAQA----E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 241 VAALGAAEKKVKmleQQRSELLEVnkqwdqhfrsmkQQYEQKITELRQKLADLQKQVTDLEA---------EREQK---- 307
Cdd:PRK11281 103 LEALKDDNDEET---RETLSTLSL------------RQLESRLAQTLDQLQNAQNDLAEYNSqlvslqtqpERAQAalya 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 308 --QRDFDRKLLLAKSKIE---MEETDKEQLTAEAKELRQKVKYLQ------DQLSPL-TRQREYQEKEIQRLNK---ALE 372
Cdd:PRK11281 168 nsQRLQQIRNLLKGGKVGgkaLRPSQRVLLQAEQALLNAQNDLQRkslegnTQLQDLlQKQRDYLTARIQRLEHqlqLLQ 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947865 373 EALSIQTPPSSPPTA--FGSPEGAGAllrkqelVTQNELLKQqvkifEEDFQRERSDR-----ERMNE 433
Cdd:PRK11281 248 EAINSKRLTLSEKTVqeAQSQDEAAR-------IQANPLVAQ-----ELEINLQLSQRllkatEKLNT 303
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
132-373 |
2.92e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 132 LGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQ 211
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 212 PGSPKMEGAGKKAVAGQQQASVtAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLA 291
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE-YLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 292 DLQKQVTDLEA------EREQKQRDFDRKL--------LLAKSKIEMEETDK----------EQLTAEAKELRQKVKYLQ 347
Cdd:PRK03918 325 GIEERIKELEEkeerleELKKKLKELEKRLeeleerheLYEEAKAKKEELERlkkrltgltpEKLEKELEELEKAKEEIE 404
|
250 260
....*....|....*....|....*.
gi 1622947865 348 DQLSPLTRQREYQEKEIQRLNKALEE 373
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEE 430
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
145-447 |
3.13e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 145 KVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLmSNGNKEGASGQPGSPKMEgagkka 224
Cdd:PRK03918 487 KVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLA------ 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 225 vagqqqasvtagkvpevaalgAAEKKVKMLEQQRSELLevNKQWDQHFRSMKQqYEQKITELR---QKLADLQKQVTDLE 301
Cdd:PRK03918 560 ---------------------ELEKKLDELEEELAELL--KELEELGFESVEE-LEERLKELEpfyNEYLELKDAEKELE 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 302 AEREqkqrdfdrKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQdqlspltrqREYQEKEIQRLNKALEEAlsiqtpp 381
Cdd:PRK03918 616 REEK--------ELKKLEEELDKAFEELAETEKRLEELRKELEELE---------KKYSEEEYEELREEYLEL------- 671
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622947865 382 sspptafgSPEGAGALLRKQELvtqnELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQA 447
Cdd:PRK03918 672 --------SRELAGLRAELEEL----EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
120-448 |
3.30e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 3.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 120 AEEPDHSQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKaKLDKGLEQRDQAAERLREEnlelkkll 199
Cdd:pfam17380 327 AEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMR-ELERLQMERQQKNERVRQE-------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 200 msngnkegasgqpgspkMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSEllEVNKQWDQHFRSMKQQY 279
Cdd:pfam17380 398 -----------------LEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLE--EERAREMERVRLEEQER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 280 EQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllakskieMEETDKEQLTAEAKELRQKVkyLQDQlspltRQREY 359
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKRDRKR--------------AEEQRRKILEKELEERKQAM--IEEE-----RKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 360 QEKEIQRLNKALEEALSIQTppsspptafgspegAGALLRKQELVTQNELLKQQVKIFEEdfqrERSDRERMNEEKEELK 439
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRRE--------------AEEERRKQQEMEERRRIQEQMRKATE----ERSRLEAMEREREMMR 579
|
....*....
gi 1622947865 440 KQVEKLQAQ 448
Cdd:pfam17380 580 QIVESEKAR 588
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-435 |
3.67e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 134 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERlreENLELKKLLMSNGNKEGASGQPG 213
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED---KNMALRKAEEAKKAEEARIEEVM 1598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 214 SPKMEGAGKKAvagqQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADL 293
Cdd:PTZ00121 1599 KLYEEEKKMKA----EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEENKIKAAEEAKKAEED 1673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 294 QKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDK--EQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL 371
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKkeAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE 1753
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622947865 372 EEALSIQTppsspptafgspegagalLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEK 435
Cdd:PTZ00121 1754 EEKKKIAH------------------LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
162-343 |
4.03e-04 |
|
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: 42.22 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 162 QLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQpgspkmeGAGKKAVAGQQQASVTAGKvpEV 241
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE-------VEARIKKYEEQLGNVRNNK--EY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 242 AALgaaEKKVKMLEQQRSELlevnkqwdqhfrsmkqqyEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSK 321
Cdd:COG1579 92 EAL---QKEIESLKRRISDL------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 1622947865 322 IEMEETDKEQLTAEAKELRQKV 343
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
263-373 |
4.68e-04 |
|
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: 40.64 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 263 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDL-EAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQ 341
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKK---------------------VQEFQR 76
|
90 100 110
....*....|....*....|....*....|..
gi 1622947865 342 KVKYLQDQLSplTRQREYQEKEIQRLNKALEE 373
Cdd:smart00935 77 KQQKLQQDLQ--KRQQEELQKILDKINKAIKE 106
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
254-375 |
4.90e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 254 LEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAeREQKQRDFDRKLLLAKSKIEMEETDKEQLT 333
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPELE 491
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 334 AEAKELRQKVKYLQDQLS------------------PLTRqreYQEKEIQRLNKaLEEAL 375
Cdd:COG0542 492 KELAELEEELAELAPLLReevteediaevvsrwtgiPVGK---LLEGEREKLLN-LEEEL 547
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
252-374 |
5.74e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 252 KMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRdfdrklllaksKIEMEEtdkEQ 331
Cdd:COG2433 384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE-----------RIERLE---RE 449
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622947865 332 LTAEAKELRQKVKylqdqlspltRQREYQ--EKEIQRLNKALEEA 374
Cdd:COG2433 450 LSEARSEERREIR----------KDREISrlDREIERLERELEEE 484
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
242-369 |
6.16e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 242 AALGAAEKKVKMLEQQRSELL-EVNKQwdQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDR-KLLLAK 319
Cdd:pfam00529 58 AALDSAEAQLAKAQAQVARLQaELDRL--QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrRVLAPI 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622947865 320 SKIEMEETDKEQltAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNK 369
Cdd:pfam00529 136 GGISRESLVTAG--ALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVR 183
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
250-482 |
6.23e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.21 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 250 KVKMLEQQRSELLEVNKQWDQHF----RSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRklllAKSKIEME 325
Cdd:pfam00038 19 KVRFLEQQNKLLETKISELRQKKgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAED----FRQKYEDE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 326 ETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAgallRKQELVT 405
Cdd:pfam00038 95 LNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAA----RKLDLTS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 406 QNELLKQQvkiFEEDFQRERSDRErmneekEELKKQVEKLQAQVTLSNAQLKAFKDEEK-------AREANRQQKRKAKA 478
Cdd:pfam00038 171 ALAEIRAQ---YEEIAAKNREEAE------EWYQSKLEELQQAAARNGDALRSAKEEITelrrtiqSLEIELQSLKKQKA 241
|
....
gi 1622947865 479 SGER 482
Cdd:pfam00038 242 SLER 245
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
142-488 |
9.30e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 142 LASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSngnkegasgQPGSPKMEGAG 221
Cdd:TIGR00618 192 LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREA---------QEEQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 222 KKAVAGQQQASVTAGKVPEV-AALGAAEKKVKMLEQQRSeLLEVNKQWDQHFRSMKQQyEQKITELRQKLADLQKQVTDL 300
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETqERINRARKAAPLAAHIKA-VTQIEQQAQRIHTELQSK-MRSRAKLLMKRAAHVKQQSSI 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 301 EAEREQKQRDFDRKLLLAKSKiEMEETDKEQLTaEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNkalEEALSIQTP 380
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAH-EVATSIREISC-QQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQ---REQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 381 PSSpptaFGSPEGAGALLRKQELVTQNELLKQQVKIfEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSnaQLKAFK 460
Cdd:TIGR00618 416 TSA----FRDLQGQLAHAKKQQELQQRYAELCAAAI-TCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH--LQETRK 488
|
330 340
....*....|....*....|....*...
gi 1622947865 461 DEEKAREANRQQKRKAKASGERYHVEPH 488
Cdd:TIGR00618 489 KAVVLARLLELQEEPCPLCGSCIHPNPA 516
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
256-473 |
9.56e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 256 QQRSELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLADLQKQVTDLEAEREQKQRDfdrkllLAKSKIEMEETDK 329
Cdd:PRK11281 42 QAQLDALNKQKLLEAEDKLVQQDLEQtlalldKIDRQKEETEQLKQQLAQAPAKLRQAQAE------LEALKDDNDEETR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 330 EQL-TAEAKELRQKVKYLQDQLspltrqreyqekeiQRLNKALEEA----LSIQTPPSSPPTA---------------FG 389
Cdd:PRK11281 116 ETLsTLSLRQLESRLAQTLDQL--------------QNAQNDLAEYnsqlVSLQTQPERAQAAlyansqrlqqirnllKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 390 SPEGAGALL--RKQELVTQNELLKQQVkifeeDFQR------------ERSDRERMNEEKEELKKQVEKLQAqvTLSNAQ 455
Cdd:PRK11281 182 GKVGGKALRpsQRVLLQAEQALLNAQN-----DLQRkslegntqlqdlLQKQRDYLTARIQRLEHQLQLLQE--AINSKR 254
|
250
....*....|....*...
gi 1622947865 456 LKAFkdEEKAREANRQQK 473
Cdd:PRK11281 255 LTLS--EKTVQEAQSQDE 270
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
156-473 |
9.68e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 156 LQTLCEQLRKENEALKAKLdKGLEQRDQAAERLREENLELKKllmsnGNKEGASGQP--GSPKMEGAGKK---------- 223
Cdd:PRK02224 410 AEDFLEELREERDELRERE-AELEATLRTARERVEEAEALLE-----AGKCPECGQPveGSPHVETIEEDrerveeleae 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 224 -AVAGQQQASVTAgKVPEVAALGAAEKKVKMLEQQRSELLEvnkqwdqhfrsMKQQYEQKITELRQKLADLQKQVTDLEA 302
Cdd:PRK02224 484 lEDLEEEVEEVEE-RLERAEDLVEAEDRIERLEERREDLEE-----------LIAERRETIEEKRERAEELRERAAELEA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 303 EREQKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVKYLQDQLSpltrQREYQEKEIQRLNKALEEALSIQTpps 382
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLERIRTLLA----AIADAEDEIERLREKREALAELND--- 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 383 spptafgspegagalLRKQELVTQNELLKQQVKIFEED-FQRERSDRER-------MNEEKEELKKQVEKLQAQVTLSNA 454
Cdd:PRK02224 624 ---------------ERRERLAEKRERKRELEAEFDEArIEEAREDKERaeeyleqVEEKLDELREERDDLQAEIGAVEN 688
|
330 340
....*....|....*....|.
gi 1622947865 455 QLKAFKD--EEKAREANRQQK 473
Cdd:PRK02224 689 ELEELEElrERREALENRVEA 709
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
263-373 |
1.06e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.48 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 263 EVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKlllakskiemeetdkeqltaeAKELRQK 342
Cdd:pfam03938 19 AAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKK---------------------EQELQQL 77
|
90 100 110
....*....|....*....|....*....|.
gi 1622947865 343 VKYLQDQLSplTRQREYQEKEIQRLNKALEE 373
Cdd:pfam03938 78 QQKAQQELQ--KKQQELLQPIQDKINKAIKE 106
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
242-358 |
1.06e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 242 AALGAAEKKVKMLEQ----QRSELLEVNKQWDQHfRSMKQQYEQKITELRQKLADLQKQVTD-LEAEREQKQRDFDRKLL 316
Cdd:COG1842 16 ALLDKAEDPEKMLDQairdMEEDLVEARQALAQV-IANQKRLERQLEELEAEAEKWEEKARLaLEKGREDLAREALERKA 94
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622947865 317 LAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQRE 358
Cdd:COG1842 95 ELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKD 136
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
134-373 |
1.14e-03 |
|
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: 41.97 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 134 RMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPg 213
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL- 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 214 SPKMEGAGKKAVAGQQQASVTAGKVPEVAAlgAAEKKVKMLEQQRSELLEVNKQWDQHFRSMK-------------QQYE 280
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAA--EIEELEELIEELESELEALLNERASLEEALAllrseleelseelRELE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 281 QKITELRQKLADLQKQVTDLEAEREQKQRDFDRKL--LLAKSKIEMEETDKEQ--------------------------- 331
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerLSEEYSLTLEEAEALEnkieddeeearrrlkrlenkikelgpv 987
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622947865 332 -LTA--EAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEE 373
Cdd:TIGR02168 988 nLAAieEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
246-347 |
1.38e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 246 AAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKladlqkqvtdLEAEREQKQRDFDRkLLLAKSKiEME 325
Cdd:cd16269 202 AERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEK----------MEEERENLLKEQER-ALESKLK-EQE 269
|
90 100
....*....|....*....|..
gi 1622947865 326 ETDKEQLTAEAKELRQKVKYLQ 347
Cdd:cd16269 270 ALLEEGFKEQAELLQEEIRSLK 291
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
254-474 |
1.71e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 254 LEQQRSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKE 330
Cdd:COG4372 40 LDKLQEELEQLREELEQ-AREELEQLEEELEQARSELEQLEEELEELNEQLQAAQaelAQAQEELESLQEEAEELQEELE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 331 QLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKAL----EEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQ 406
Cdd:COG4372 119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLeslqEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947865 407 NELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKR 474
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
277-481 |
1.98e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 277 QQYEQKIT-------ELRQKLADLQKQVTDLEAerEQKQRDFDRKLLLAKSkiemeetdkeQLTAEAKELRQ---KVKYL 346
Cdd:PRK10929 68 KQYQQVIDnfpklsaELRQQLNNERDEPRSVPP--NMSTDALEQEILQVSS----------QLLEKSRQAQQeqdRAREI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 347 QDQLSPLTRQREyqekEIQRLNKALEEALSIQTPPSSPptafgspegagaLLRKQELVTQNELLKQQVKIFEEDF-QRER 425
Cdd:PRK10929 136 SDSLSQLPQQQT----EARRQLNEIERRLQTLGTPNTP------------LAQAQLTALQAESAALKALVDELELaQLSA 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947865 426 SDRERMNEEKEEL-KKQVEKLQAQVTLSNAQLKAFKDEEkAREANRQQKRKAKASGE 481
Cdd:PRK10929 200 NNRQELARLRSELaKKRSQQLDAYLQALRNQLNSQRQRE-AERALESTELLAEQSGD 255
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
332-452 |
2.12e-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: 40.51 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 332 LTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRL-NKALEEALSIQTPPSSPPTAFgspegAGALLRKQELVTQNELL 410
Cdd:pfam09787 45 LTLELEELRQERDLLREEIQKLRGQIQQLRTELQELeAQQQEEAESSREQLQELEEQL-----ATERSARREAEAELERL 119
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622947865 411 KQQVKIFEEDFQRERSDRERMNEEKEelkKQVEKLQAQVTLS 452
Cdd:pfam09787 120 QEELRYLEEELRRSKATLQSRIKDRE---AEIEKLRNQLTSK 158
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
275-482 |
2.36e-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: 41.11 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 275 MKQQYEQKITELRQKLADLQKQVTDLEAEREQkqrdfdRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLT 354
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQ------ELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 355 RQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNElLKQQVKIFEEDFQRERSDRERMNEE 434
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE-EEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622947865 435 KEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREANRQQKRKAKASGER 482
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
179-466 |
2.41e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 179 EQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMegagkkavagQQQASVTAGKVPEVAALGAAEKKVKMLEQQR 258
Cdd:pfam05483 265 ESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKM----------SLQRSMSTQKALEEDLQIATKTICQLTEEKE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 259 SELLEVNKQWDQH-----------------FRSMKQQYEQKITELRQKLADLQKQVTDLEAE---REQKQRDFD--RKLL 316
Cdd:pfam05483 335 AQMEELNKAKAAHsfvvtefeattcsleelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMtkfKNNKEVELEelKKIL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 317 LAKSKIEMEETDKEQLTAEAKELRQKVKYL-----------QDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPP 385
Cdd:pfam05483 415 AEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarekeihdlEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 386 TAFgspegagaLLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKA 465
Cdd:pfam05483 495 DKL--------LLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKC 566
|
.
gi 1622947865 466 R 466
Cdd:pfam05483 567 K 567
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-462 |
3.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 104 NLMLHLQRLETTLSVCAEEPDHSQLFTHLgRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKglEQRDQ 183
Cdd:COG4717 160 ELEEELEELEAELAELQEELEELLEQLSL-ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ--LENEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 184 AAERLREENLELKKLLMSNG---NKEGASGQPGSPKMEGAGKKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSe 260
Cdd:COG4717 237 EAAALEERLKEARLLLLIAAallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE- 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 261 lLEvNKQWDQHFRSMKQQYEQKITELR------QKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEET--DKEQL 332
Cdd:COG4717 316 -LE-EEELEELLAALGLPPDLSPEELLelldriEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEElrAALEQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 333 TAEAKELRQKVKYLQDQLSPLTRQREYQ---------EKEIQRLNKALEEalsiqtppsspptafgspegagalLRKQEL 403
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELlealdeeelEEELEELEEELEE------------------------LEEELE 449
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947865 404 VTQNEL--LKQQVKIFEED--FQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDE 462
Cdd:COG4717 450 ELREELaeLEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-449 |
3.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 134 RMALEFNRLASKVHKNEQRTSilqtlCEQLRKENEALKAKLDKGLEQRDQAAERLREEnlELKKllmSNGNKEGASGQPG 213
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKK-----ADEAKKAEEAKKADEAKKAEEKKKADELKKAE--ELKK---AEEKKKAEEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 214 SPKMEGAGKKAVAGQQqasVTAGKVPEVAALGAAEKKVKM-----LEQQRSELLEVNKQwdQHFRSMKQQYEQKITELRQ 288
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKK---AEEARIEEVMKLYEEEKKMKAeeakkAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEKK 1647
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 289 KLADLQK--QVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQR 366
Cdd:PTZ00121 1648 KAEELKKaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 367 LNKALEEAlsiqtppsspptafgsPEGAGALLRKQELVTQNELLKQQVK--IFEEDFQRERSDRERMNEEKEELKKQVEK 444
Cdd:PTZ00121 1728 NKIKAEEA----------------KKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIEEELDEEDEK 1791
|
....*
gi 1622947865 445 LQAQV 449
Cdd:PTZ00121 1792 RRMEV 1796
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
249-445 |
3.52e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 249 KKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQK------ITELRQKLADLQKQ----VTDLEAERE------------- 305
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRKELAELnkaggsIDKLRKEIERLEWRqqteVLSPEEEKElvekikelekele 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 306 --QKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAlsiqtppss 383
Cdd:COG1340 151 kaKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEA--------- 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622947865 384 pptafgspEGAGALLRKQELVTQNELLKQQVKIFEedfQRERSDRERMNEEKEELKKQVEKL 445
Cdd:COG1340 222 --------QEKADELHEEIIELQKELRELRKELKK---LRKKQRALKREKEKEELEEKAEEI 272
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
258-461 |
4.40e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 4.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 258 RSELLEVNKQWDQHFRSMKQQYEQkITELRQKLADLQKQVTDLEAEREQkQRDFDRKLLLAKSKIEMEETDKEQLTAEAK 337
Cdd:COG3096 490 RSQAWQTARELLRRYRSQQALAQR-LQQLRAQLAELEQRLRQQQNAERL-LEEFCQRIGQQLDAAEELEELLAELEAQLE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 338 ELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIF 417
Cdd:COG3096 568 ELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQD----------------ALERLREQSGEALADSQEVTAA 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622947865 418 -EEDFQRERS---DRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKD 461
Cdd:COG3096 632 mQQLLEREREatvERDELAARKQALESQIERLSQPGGAEDPRLLALAE 679
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
161-482 |
4.60e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 161 EQLRKENEALKAKLDKGLEQRDQAAERLREENL----ELKKLLMSNG-----------NKEGASGQPGSPKMEGAGKKAV 225
Cdd:PTZ00121 1137 EDARKAEEARKAEDAKRVEIARKAEDARKAEEArkaeDAKKAEAARKaeevrkaeelrKAEDARKAEAARKAEEERKAEE 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 226 AGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQklADLQKQVTDLEAERE 305
Cdd:PTZ00121 1217 ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARK--ADELKKAEEKKKADE 1294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 306 QKQRDFDRKLLLAKSKIEmEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALsiQTPPSSPP 385
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAE-EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE--EKAEAAEK 1371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 386 TAFGSPEGAGALLRKQELVTQNELLKQQVkifEEDFQRERSDRERMNEEK--EELKKQVEKLQAQVTLSNAQLKAFKDEE 463
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKA---EEDKKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKKKAEEAKKADE 1448
|
330 340
....*....|....*....|..
gi 1622947865 464 ---KAREANRQQKRKAKASGER 482
Cdd:PTZ00121 1449 akkKAEEAKKAEEAKKKAEEAK 1470
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
282-471 |
4.64e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 38.73 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 282 KITELRQKLADLQKQVTDLEAErEQKQRDFDRKLLLAKSKIEMEETDKEQL----TAEAKELRQKVKYLQDQLSPLTRQR 357
Cdd:pfam15619 12 KIKELQNELAELQSKLEELRKE-NRLLKRLQKRQEKALGKYEGTESELPQLiarhNEEVRVLRERLRRLQEKERDLERKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 358 EYQEKEIQRLNKALE--EALSIQTppsspptafgspegagALLRKQELVTQNELLKQQVKIFEEDFQR-----ERSDRER 430
Cdd:pfam15619 91 KEKEAELLRLRDQLKrlEKLSEDK----------------NLAEREELQKKLEQLEAKLEDKDEKIQDlerklELENKSF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622947865 431 MNEEKEELKKQVEklqAQVTLSNAQLKAFKDEEKAREANRQ 471
Cdd:pfam15619 155 RRQLAAEKKKHKE---AQEEVKILQEEIERLQQKLKEKERE 192
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
312-458 |
4.78e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.65 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 312 DRKLLLAKSKIEMEETDKE------QLTAEAKELRQKVKYLQDQlspltrQREYQEKEIQRLNKAlEEALSIQtppsspp 385
Cdd:COG1842 23 DPEKMLDQAIRDMEEDLVEarqalaQVIANQKRLERQLEELEAE------AEKWEEKARLALEKG-REDLARE------- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947865 386 tafgspegagALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKA 458
Cdd:COG1842 89 ----------ALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKV 151
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
254-375 |
5.58e-03 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 39.57 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 254 LEQQRSELLEVNKQWD----QHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLL-------AKSKI 322
Cdd:pfam14643 243 VEEWWASLEALNEQLDqyhdQCMTKLRAEYEEVWQECLARVQKLKQELLDYKVCSEEEAEALVNEEFLplvgklqRDAED 322
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622947865 323 EMEETDK--EQLtaeAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEAL 375
Cdd:pfam14643 323 ELEKLDKflEEL---AKQTEAQSEDLFKFFREAAQLWDVHQTELAKQELELEKKL 374
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
278-458 |
6.23e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 38.94 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 278 QYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKskiemeetDKEQLTAEAKELRQKVKYLQDQLSPLTRQR 357
Cdd:pfam00529 55 DYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQ--------DYDGATAQLRAAQAAVKAAQAQLAQAQIDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 358 EYQEkeiQRLNKALEEALSIQTppsspptafgspegAGALLRKQE-----LVTQNELLKQQVKIFEEDFQRE-RSDRERM 431
Cdd:pfam00529 127 ARRR---VLAPIGGISRESLVT--------------AGALVAQAQanllaTVAQLDQIYVQITQSAAENQAEvRSELSGA 189
|
170 180
....*....|....*....|....*..
gi 1622947865 432 NEEKEELKKQVEklQAQVTLSNAQLKA 458
Cdd:pfam00529 190 QLQIAEAEAELK--LAKLDLERTEIRA 214
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
242-376 |
7.34e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 242 AALGAAEKKVKMLEQQ----RSELLEVNKQWDQhFRSMKQQYEQKITELRQKLADLQKQVTDLEAERE----QKQRDFDR 313
Cdd:COG1579 24 HRLKELPAELAELEDElaalEARLEAAKTELED-LEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyealQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947865 314 KLLLAKSKIEMEETDK-EQLTAEAKELRQKVKYLQDQLSPLTRQRE----YQEKEIQRLNKALEEALS 376
Cdd:COG1579 103 RRISDLEDEILELMERiEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAEREELAA 170
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
154-441 |
7.95e-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: 39.03 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 154 SILQTLCEQL-RKEN--EALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGQPGSPKMEGAGKKAVAGQQQ 230
Cdd:pfam10174 436 TALTTLEEALsEKERiiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKK 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 231 ASvtagkvpevaalgaaekKVKMLE---QQRSEllEVNKQWDQHFRSMKQQYEQKIT-ELRQKLADLQKQVTDLEAEREQ 306
Cdd:pfam10174 516 DS-----------------KLKSLEiavEQKKE--ECSKLENQLKKAHNAEEAVRTNpEINDRIRLLEQEVARYKEESGK 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 307 KQRDFDRkLLLAKSKIEMEETDKEQLTAEAKELrqKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPT 386
Cdd:pfam10174 577 AQAEVER-LLGILREVENEKNDKDKKIAELESL--TLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQ 653
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947865 387 AFGSPEGAGALLR-KQEL-VTQNELLKQQVKIFEED--FQRERSDRERMNEEKEELKKQ 441
Cdd:pfam10174 654 QLQLEELMGALEKtRQELdATKARLSSTQQSLAEKDghLTNLRAERRKQLEEILEMKQE 712
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
237-475 |
8.16e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 237 KVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQyeqkITELRQKLADLQKQVTDLEAEREQKQrdfDRKLL 316
Cdd:pfam01576 126 KVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN----LAEEEEKAKSLSKLKNKHEAMISDLE---ERLKK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 317 LAKSKIEMEETdKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEalsiqtppsspptafgspEGAga 396
Cdd:pfam01576 199 EEKGRQELEKA-KRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEE------------------ETA-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 397 llRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQV--TL--SNAQL--------------KA 458
Cdd:pfam01576 258 --QKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELedTLdtTAAQQelrskreqevtelkKA 335
|
250
....*....|....*..
gi 1622947865 459 FKDEEKAREANRQQKRK 475
Cdd:pfam01576 336 LEEETRSHEAQLQEMRQ 352
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
222-374 |
8.17e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 38.92 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 222 KKAVAGQQQASVTAGKVPEVAALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQ------KITELRQKLADLQK 295
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQldaraeKLDNLENQLEEREK 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947865 296 QVTDLEAEREQKQRDFDRKLLlakskiemeetDKEQLTAEakELRQKVkylqdqLSPLtrQREYQEKEIQRLNKALEEA 374
Cdd:PRK12705 113 ALSARELELEELEKQLDNELY-----------RVAGLTPE--QARKLL------LKLL--DAELEEEKAQRVKKIEEEA 170
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
262-478 |
8.81e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.00 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 262 LEVNKQwdqhfrSMKQQYEQKIT----ELRQKLADLQKQVTDLEAER--EQKQRDfdrKLLLAKSKIEMEETDKE-QLTA 334
Cdd:pfam01576 718 LEVNMQ------ALKAQFERDLQardeQGEEKRRQLVKQVRELEAELedERKQRA---QAVAAKKKLELDLKELEaQIDA 788
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 335 EAK---ELRQKVKYLQDQLSPLTRQRE----------YQEKEIQRLNKALE-EALSIQTPPSSPPTAFG---------SP 391
Cdd:pfam01576 789 ANKgreEAVKQLKKLQAQMKDLQRELEearasrdeilAQSKESEKKLKNLEaELLQLQEDLAASERARRqaqqerdelAD 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 392 EGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTlsnAQLKAFKDEEKAREANRQ 471
Cdd:pfam01576 869 EIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA---AERSTSQKSESARQQLER 945
|
....*..
gi 1622947865 472 QKRKAKA 478
Cdd:pfam01576 946 QNKELKA 952
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
254-351 |
8.83e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 36.39 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 254 LEQQRSELLEVNKQWDQhfrsMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQ---RDFDRKLLLAKSKIEMEETDKE 330
Cdd:pfam13863 1 LLEKKREMFLVQLALDA----KREEIERLEELLKQREEELEKKEQELKEDLIKFDkflKENDAKRRRALKKAEEETKLKK 76
|
90 100
....*....|....*....|.
gi 1622947865 331 QLTAEAKELRQKVKYLQDQLS 351
Cdd:pfam13863 77 EKEKEIKKLTAQIEELKSEIS 97
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
236-362 |
9.33e-03 |
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DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 38.48 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947865 236 GKVPE-VAALGAAEKKVKML-EQQRSelleVNKQwdqHFRSMkQQYEQKITELRQKLADLQKQVTDLEAEREQKqRDFDR 313
Cdd:smart00435 245 GNVAEkILAYNRANREVAILcNHQRT----VSKT---HEKSM-EKLQEKIKALKYQLKRLKKMILLFEMISDLK-RKLKS 315
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622947865 314 KLLLAKSKIEME-ETDKEQLTAEAKELRQkVKYLQDQLSPLTRQREYQEK 362
Cdd:smart00435 316 KFERDNEKLDAEvKEKKKEKKKEEKKKKQ-IERLEERIEKLEVQATDKEE 364
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