|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
89-556 |
1.81e-10 |
|
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: 63.89 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 89 RQILDKSYYLGLLRSKISELTTEINKLQKEIEMYNQENSVYLSYEKRAETLAVEIKDFQGQLADYNMLVDKLntNTEMEE 168
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK--QQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 169 VMSDYNMLKAQNDRETQSMDVIFTERQAKEKQIrsveeeveqekQAADGIIKNMspEKQVKYIEMKTT---NEKLLQELD 245
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL-----------EQNNKKIKEL--EKQLNQLKSEISdlnNQKEQDWNK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 246 TLQQQLDSLNMKKESLETEIahSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQ----EIAS 321
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQI--SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykqEIKN 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 322 MERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIE------ASIIT 395
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnldntrESLET 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 396 LLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNKIK 475
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 476 QMTADLeTYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTSDYDTLKTQLQDNEThaQLTNLERKWQHLEQN 555
Cdd:TIGR04523 549 KDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK--KISSLEKELEKAKKE 625
|
.
gi 148698986 556 N 556
Cdd:TIGR04523 626 N 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
303-594 |
8.62e-10 |
|
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: 62.00 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 303 EERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQE 382
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 383 LERKAQIEASIITlLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESK 462
Cdd:TIGR02168 319 EELEAQLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 463 MTEEQQSLKNKIKQMTADLE-------------TYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKI---MEKLTSDY 526
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRErlqqeieellkklEEAELKELQAELEELEEELEELQEELERLEEALEELreeLEEAEQAL 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148698986 527 DTLKTQLQdnETHAQLTNLERKWQHLEQNNFVMKEFIATKSQESDYQPVIKNVMKQIAEYNKTIMDAL 594
Cdd:TIGR02168 478 DAAERELA--QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAL 543
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-505 |
2.56e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 225 EKQVKYIEMKTT-----NEKLLQELDTLQQQLDSLNMKKESLETEIAHSQVKQEAVllyEKlyELESHRDQMIAEDksmg 299
Cdd:COG1196 210 EKAERYRELKEElkeleAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL---EA--ELEELRLELEELE---- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 300 spmEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQgemnqkyKELKKREENMDAFIETFEETK 379
Cdd:COG1196 281 ---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-------EELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 380 NQELERKAQIEASIITLLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELL 459
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 148698986 460 ESKMTEEQQSLKNKIKQMTADLETYSDLAALKSSAEEKKKKLHQER 505
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
238-590 |
3.40e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 238 EKLLQELDTLQQQLDSLNMKKESLETEiaHSQVKQEAVLLYEklyELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQ 317
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKE--LEELEEELEQLRK---ELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 318 EIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETkNQELERKAQIEASIITLL 397
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-NEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 398 EHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNKIKQM 477
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 478 TADLEtysdlaalkssaeEKKKKLHQERTVLSTHRNAFKKIMEKLTSDYDTL---------KTQLQDNETHAQLTNLERK 548
Cdd:TIGR02168 914 RRELE-------------ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenKIEDDEEEARRRLKRLENK 980
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 148698986 549 WQHLEQNNF-VMKEFIATK-------SQESDYQPVIKNVMKQIAEYNKTI 590
Cdd:TIGR02168 981 IKELGPVNLaAIEEYEELKerydfltAQKEDLTEAKETLEEAIEEIDREA 1030
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
238-490 |
3.73e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 238 EKLLQELDTLQQQLDSLNMKKESLETEIA------------HSQVKQEAVLLYEKLYELESHRDQMIAEDKSMgspMEER 305
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAeleaeleelrleLEELELELEEAQAEEYELLAELARLEQDIARL---EERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 306 ERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELER 385
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 386 KAQiEASIITLLEHCSRNINRMKQISSITNQELKMMQDDLsfkSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTE 465
Cdd:COG1196 392 LRA-AAELAAQLEELEEAEEALLERLERLEEELEELEEAL---AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260
....*....|....*....|....*
gi 148698986 466 EQQSLKNKIKQMTADLETYSDLAAL 490
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-392 |
3.96e-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: 56.61 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 101 LRSKISELTTEINKLQKEIEMYNQEnsvYLSYEKRAETLAVEIKDFQGQladynmlvDKLNTNTEMEEVMSDYNMLKAQN 180
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKR---LEEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 181 DRETQSMDviftERQAKEKQIRSVEEEVEQEKQAADGIIKnmspEKQVKYIEMKTTNEKLLQELDTLQQQLDSLNmkKES 260
Cdd:TIGR02169 311 AEKERELE----DAEERLAKLEAEIDKLLAEIEELEREIE----EERKRRDKLTEEYAELKEELEDLRAELEEVD--KEF 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 261 LETEIAHSQVKQEAVLLYEKLYELESHRDqmiaedksmgspmeereRLLKQVKEDNQEIASMERQLTDIKEKINQFSEEI 340
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELD-----------------RLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 148698986 341 RQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFE--ETKNQELERK-AQIEAS 392
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDrvEKELSKLQRElAEAEAQ 498
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
239-398 |
9.97e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 53.00 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 239 KLLQELDTLQQQLDSLNMKKESLETEIAhsQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKeDNQE 318
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELA--ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 319 IASMERQLTDIKEKINQFSEEIRQLDMDLEEHQgemnqkyKELKKREENMDAFIETFEETKNQELERKAQIEASIITLLE 398
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELE-------EELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-409 |
3.74e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 101 LRSKISELTTEINKLQKEIEMYNQENSvylSYEKRAETLAVEIKDFQGQLADYNMLVDKLNTNTEMEEVMSdynmlkAQN 180
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI------AQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 181 DRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAADGIIKNMSPEKQvkyiEMKTTNEKLLQELDTLQQQLDSLNMKKES 260
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 261 LETEIAhsQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEE----RERLLKQVKEDNQEIASMERQLTDIKEKINQF 336
Cdd:TIGR02168 829 LERRIA--ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseLEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148698986 337 SEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIEASIITLLEHCSRNINRMKQ 409
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
283-394 |
7.06e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 283 ELESHRDQMIAEDKSMGspMEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELK 362
Cdd:PRK12704 50 EAEAIKKEALLEAKEEI--HKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 148698986 363 KREENMDAFIE------------TFEETKNQ---ELERKAQIEASII 394
Cdd:PRK12704 128 KKEEELEELIEeqlqelerisglTAEEAKEIlleKVEEEARHEAAVL 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-526 |
1.79e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 104 KISELTTEINKLQKEIEMYNQENSVYLSYEKRAETLAVEIKDFQGQLADYNMLVDKLNTNTEMEEVmsdyNMLKAQNDRE 183
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL----EAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 184 TQSMDVIFTERQAKEKQIRSVEEEVEQEKQAADGIIKNMSPEKQVKYIEMKTTNEKLLQELDTLQQQLDSLNMKKESLET 263
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 264 EIAHSQVKQEAVLLYEKLYELESHR-----------------------------------DQMIAEDKSMGSPMEERERL 308
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 309 LKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQgEMNQKYKELKKREEnmdafIETFEETKNQELER-KA 387
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQ-----LEELEQEIAALLAEaGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 388 QIEASIITLLEHCSRNINRMKQISSITNQElkmmqdDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQ 467
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQL------EELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 148698986 468 QSLKNKIKQMTADlETYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTSDY 526
Cdd:COG4717 456 AELEAELEQLEED-GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
283-489 |
2.57e-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: 50.15 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 283 ELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELK 362
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 363 K------REENMDAFIETFEETKNQELERKAQIEASIITLLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQ 436
Cdd:COG4942 108 EllralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148698986 437 TTARNLTSDSQRLQLDLQKMELLESK----MTEEQQSLKNKIKQMTADLETYSDLAA 489
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAelaeLQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
77-482 |
4.04e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.12 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 77 LSGMKTGMKGPQRQILDKSYYLGLLRSKISELTTEINKLQKEIEMYNQENSVYLSYEKRAETLAVEIKDFQGQLADYNML 156
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 157 VDKLNTNTEmeevmsDYNMLKAQNDRETQSMDViftERQAKEKQIRSVEEEveqekqaadgiiknmspekqvkyiemktt 236
Cdd:pfam15921 564 IEILRQQIE------NMTQLVGQHGRTAGAMQV---EKAQLEKEINDRRLE----------------------------- 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 237 neklLQELDTLQQQLDSlnmKKESLETEIahSQVKQEAVllyeKLYELESHRDQMIAEDKsmgspmEERERLLKQVKEDN 316
Cdd:pfam15921 606 ----LQEFKILKDKKDA---KIRELEARV--SDLELEKV----KLVNAGSERLRAVKDIK------QERDQLLNEVKTSR 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 317 QEIASMERQLTDIKEKINQFSEEIR----QLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIEA- 391
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDAl 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 392 -SIITLLEHCSRNINRMKQissITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMT------ 464
Cdd:pfam15921 747 qSKIQFLEEAMTNANKEKH---FLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASlqfaec 823
|
410 420
....*....|....*....|....
gi 148698986 465 ------EEQQSLKNKIkQMTADLE 482
Cdd:pfam15921 824 qdiiqrQEQESVRLKL-QHTLDVK 846
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
238-384 |
7.37e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 238 EKLLQELDTLQQQLDSLNMKKESLETEIAHSQVKQEAvllYEKLyeleshrDQMIAEDKSMGSPMEERERL---LKQVKE 314
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA---LQRL-------AEYSWDEIDVASAEREIAELeaeLERLDA 682
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 315 DNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELE 384
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-366 |
1.49e-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: 48.13 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 101 LRSKISELTTEINKLQKEIEMYNQENSvylSYEKRAETLAVEIKDFQGQLADYNMlvDKLNTNTEMEEVMSDYNMLKAQN 180
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVS---ELEEEIEELQKELYALANEISRLEQ--QKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 181 DRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAADgiiknmspEKQVKYIEMKTTNEKLLQELDT-------LQQQLDS 253
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELE--------ELEAELEELESRLEELEEQLETlrskvaqLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 254 LNMKKESLETEIAHSQV-----KQEAVLLYEKLYELESHRDQMIAEDKSMG--SPMEERERLLKQVKEDNQEIASMERQL 326
Cdd:TIGR02168 398 LNNEIERLEARLERLEDrrerlQQEIEELLKKLEEAELKELQAELEELEEEleELQEELERLEEALEELREELEEAEQAL 477
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148698986 327 TDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREE 366
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
103-590 |
1.78e-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: 47.71 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 103 SKISELTTEINKLQKEIEMYNQE----NSVYLSYEKRAETLAVEIKDFQGQLADYNmlvDKLNTNTEM-EEVMSDYNMLK 177
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKElknlDKNLNKDEEKINNSNNKIKILEQQIKDLN---DKLKKNKDKiNKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 178 AQNDRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAadgiIKNMspEKQVKYIEMKttNEKLLQELDTLQQQLDSLNMK 257
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE----IKKK--EKELEKLNNK--YNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 258 KESLETEIahSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQEIASMERQLTDIKEKINQFS 337
Cdd:TIGR04523 182 KLNIQKNI--DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 338 EEIRQLDMDLEEHQGEM---NQKYKELKKREENMDAFIETFEETKNQELERK-----AQIEASIITLLEHCSRN---INR 406
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNnkiISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 407 MKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMEL----LESKMTEEQQSLKNKIKQMTADLE 482
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESqindLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 483 TYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTSDYDTLKTQLQD--NETHAQLTNLERKWQHLEQNNfvmK 560
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVlsRSINKIKQNLEQKQKELKSKE---K 496
|
490 500 510
....*....|....*....|....*....|
gi 148698986 561 EFIATKSQESDYQPVIKNVMKQIAEYNKTI 590
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-473 |
2.11e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 88 QRQILDKSYYLGLLRSKISELTTEINKLQKEIEMYNQEnsvYLSYEKRAETLAVEIKDFQGQLADYNMLVDKL-NTNTEM 166
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKE---VKELEELKEEIEELEKELESLEGSKRKLEEKIrELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 167 EEVMSDYNMLKAQNDRetqsmdviFTERQAKEKQIRSVEEEVEQEKQAADGIIKNMSpekqvKYIEMKTTNEKLLQELDT 246
Cdd:PRK03918 269 EELKKEIEELEEKVKE--------LKELKEKAEEYIKLSEFYEEYLDELREIEKRLS-----RLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 247 LQQQLDSLNMKKESLETEIAhsqVKQEAVLLYEKLYELESHRDQMIAEDKsmGSPMEERERLLKQVKEDNQEIasmERQL 326
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLE---ELEERHELYEEAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEI---EEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 327 TDIKEKINQFSEEIRQLDMDL------------------EEHQGEMNQKY-KELKKREENMDAFIETFEETKNQ--ELER 385
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIeelkkakgkcpvcgreltEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKElrELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 386 KAQIEASIITLLEhcsrninRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTE 465
Cdd:PRK03918 488 VLKKESELIKLKE-------LAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
....*...
gi 148698986 466 EQQSLKNK 473
Cdd:PRK03918 561 LEKKLDEL 568
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
127-391 |
2.32e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 127 SVYLSYEKRAETLAVEIKDFQGQLADynmLVDKLNtntemeEVMSDYNMLKAQNDRETQSMDVIFTERQAKEKQIRsvee 206
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSS---LQSELR------RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEE---- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 207 eveqekqAADGIIKNMspEKQVKYIEMKTTNEK-----LLQELDTLQQQLDSLNMKKESLETEIAHSQVKQ--------- 272
Cdd:TIGR02169 734 -------KLKERLEEL--EEDLSSLEQEIENVKselkeLEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelskle 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 273 -EAVLLYEKLYELES-----HRDQMIAEDKSMGspMEERERLLK-QVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDM 345
Cdd:TIGR02169 805 eEVSRIEARLREIEQklnrlTLEKEYLEKEIQE--LQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 148698986 346 DLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIEA 391
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA 928
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
302-490 |
2.66e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 302 MEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLD----------MDLEEHQGEMNQKYKELKKREENMDAF 371
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELReeleklekevKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 372 IETFEETKNQELERKAQIEAsiitlLEHCSRNINRMKQiSSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQL 451
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEE-----LEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 148698986 452 DLQKMELLESKMTEEQQSLKNKIKQMTADLETYSDLAAL 490
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
304-548 |
4.58e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 304 ERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMN---QKYKELKKREENMDAFIETFEETKN 380
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEeaqAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 381 QELERKAQIEASIITLLEHCSRNINRMKQIssitNQELKMMQDDLsfKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLE 460
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEEL----EEELEEAEEEL--EEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 461 SKMTEEQQ--SLKNKIKQMTADLETY-SDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTSDYDTLKTQLQDNE 537
Cdd:COG1196 387 ELLEALRAaaELAAQLEELEEAEEALlERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250
....*....|.
gi 148698986 538 THAQLTNLERK 548
Cdd:COG1196 467 ELLEEAALLEA 477
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
231-398 |
1.08e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 45.24 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 231 IEMKTTNEKLLQELDTLQQQLDSLNMKKESlETEIAHSQVKQEAvllyeklyELESHRDQMIAEDKSmgSPMEERERLLK 310
Cdd:PRK00106 22 ISIKMKSAKEAAELTLLNAEQEAVNLRGKA-ERDAEHIKKTAKR--------ESKALKKELLLEAKE--EARKYREEIEQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 311 QVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENmdafIETFEETKNQELERKA--- 387
Cdd:PRK00106 91 EFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQ----VEKLEEQKKAELERVAals 166
|
170
....*....|.
gi 148698986 388 QIEASIITLLE 398
Cdd:PRK00106 167 QAEAREIILAE 177
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
290-470 |
1.23e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 290 QMIAE-DKSMGSPMEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKReenM 368
Cdd:PRK11637 54 QDIAAkEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQ---L 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 369 DAFIETFEET------KNQELERKAQIEASIITLlehcsrNINRMKQISsitnqELKMMQDDLSFKSTEMQKSQTTARNL 442
Cdd:PRK11637 131 DAAFRQGEHTglqlilSGEESQRGERILAYFGYL------NQARQETIA-----ELKQTREELAAQKAELEEKQSQQKTL 199
|
170 180 190
....*....|....*....|....*....|....*....
gi 148698986 443 TSDSQRLQldlQKMEL-----------LESKMTEEQQSL 470
Cdd:PRK11637 200 LYEQQAQQ---QKLEQarnerkktltgLESSLQKDQQQL 235
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
242-427 |
1.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 242 QELDTLQQQLDSLNMKKESLETEIAhsQVKQEAVLLYEKLYELESHRDQmiaedksmgSPMEERERLlkqvkedNQEIAS 321
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELE--RLEARLDALREELDELEAQIRG---------NGGDRLEQL-------EREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 322 MERQLTDIKEKINQFSEEIRQLDMDLEEHQgemnqkyKELKKREENMDAFIETFEETKNQELERKAQIEASIITL---LE 398
Cdd:COG4913 350 LERELEERERRRARLEALLAALGLPLPASA-------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrreLR 422
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148698986 399 HCSRNINRMKQ-ISSIT----------NQELKMMQDDLSF 427
Cdd:COG4913 423 ELEAEIASLERrKSNIParllalrdalAEALGLDEAELPF 462
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
238-585 |
1.76e-04 |
|
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: 44.67 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 238 EKLLQELDTLQQQLDSLNMKKESLETEIAHSQVKQEAVLLYEKLyeleshrdQMIAEDKSMGSPMEERERLLKQVKEDNQ 317
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAL--------LKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 318 EIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNqkykelKKREENMDAFIETFEETKNQelerKAQIEASIITLL 397
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK------DLGEEEQLRVKEKIGELEAE----IASLERSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 398 EHCSRNINRMKQI-SSITNQELKMMQDDLSFKSTEMQKSQTTARnLTSDSQRLQLDLQKMELLESKMTE---EQQSLKNK 473
Cdd:TIGR02169 315 RELEDAEERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEE-YAELKEELEDLRAELEEVDKEFAEtrdELKDYREK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 474 IKQMTADLETysdlaaLKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTsDYDTLKTQLQDnETHAQLTNLERKWQHLE 553
Cdd:TIGR02169 394 LEKLKREINE------LKRELDRLQEELQRLSEELADLNAAIAGIEAKIN-ELEEEKEDKAL-EIKKQEWKLEQLAADLS 465
|
330 340 350
....*....|....*....|....*....|..
gi 148698986 554 QnnfVMKEFIATKSQESDYQPVIKNVMKQIAE 585
Cdd:TIGR02169 466 K---YEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| TTC8_N |
cd21341 |
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 ... |
7-63 |
1.96e-04 |
|
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 (TTC80), also known a BBS8, has been directly linked to Bardet-Biedl syndrome, an autosomal recessive ciliopathy characterized by retinal degeneration, renal failure, obesity, diabetes, male infertility, polydactyly and cognitive impairment. Mutations in BBS8 cause early vision loss. In addition to C-terminal tetratricopeptide repeats, TTC8 also contains an N-terminal domain of unknown function.
Pssm-ID: 411061 [Multi-domain] Cd Length: 139 Bit Score: 41.90 E-value: 1.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148698986 7 SSAPRPISRGGIGLTG--RP-PSGIRPPSGNVRVATAMPPTTARPGS----RGGPLGTGGVLSS 63
Cdd:cd21341 66 SQAMRPTTSSGRPITGfvRPgTQSGRPGTSRQALRTPRRAGTARPVTsasgRFVRLGTASMLSG 129
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-349 |
2.40e-04 |
|
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: 43.60 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 103 SKISELTTEINKLQKEIEmynQENSVYLSYEKRAETLAVEIKDFQGQLADYNMLVDKLNTntEMEEVMSDYNMLKAQNDR 182
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ--ELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 183 ETQSMDvifTERQAKEKQIRSVEEEVEQEKQAAdgIIKNMSPEKQVKYIE-MKTTNEKLLQELDTLQQQLDSLNMKKESL 261
Cdd:COG4942 95 LRAELE---AQKEELAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 262 ETEIAhsqvkqeavllyeklyELESHRDQMIAEDKSMGSPMEERERLLKQVkedNQEIASMERQLTDIKEKINQFSEEIR 341
Cdd:COG4942 170 EAERA----------------ELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIA 230
|
....*...
gi 148698986 342 QLDMDLEE 349
Cdd:COG4942 231 RLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
229-483 |
2.61e-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: 44.19 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 229 KYIEMKTTNEKLLQELdtLQQQLDSLNMKKESLETEIAHSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSpMEERERL 308
Cdd:TIGR00618 598 DLTEKLSEAEDMLACE--QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI-RVLPKEL 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 309 LKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQldmdLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQ 388
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE----LETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 389 IEASIITLLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSD-SQRLQLDLQKMELLESKMTEEQ 467
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEiGQEIPSDEDILNLQCETLVQEE 830
|
250
....*....|....*.
gi 148698986 468 QSLKNKIKQMTADLET 483
Cdd:TIGR00618 831 EQFLSRLEEKSATLGE 846
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
304-489 |
2.68e-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: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 304 ERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETkNQEL 383
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-ARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 384 ERKAQIEASIITLLEhcSRN----INRMKQISSITNQELKMMQDDlsfkSTEMQKSQTTARNLTSDSQRLQLDLQKMELL 459
Cdd:COG3883 96 YRSGGSVSYLDVLLG--SESfsdfLDRLSALSKIADADADLLEEL----KADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190
....*....|....*....|....*....|
gi 148698986 460 ESKMTEEQQSLKNKIKQMTADLETYSDLAA 489
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-554 |
3.78e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 225 EKQVKYIEMKTTNEKLLQELDTLQQQLDSLNMKKESLETEIAHSQVKQEAvlLYEKLYELESHRDQMIAEDKSMGSPMEE 304
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE--LEELEAELAELQEELEELLEQLSLATEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 305 R-ERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQEL 383
Cdd:COG4717 193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 384 ERKAQIEASIITLLEHCSRNINRMKQ--------------ISSITNQELKMMQDDLSFKST--------------EMQKS 435
Cdd:COG4717 273 LTIAGVLFLVLGLLALLFLLLAREKAslgkeaeelqalpaLEELEEEELEELLAALGLPPDlspeellelldrieELQEL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 436 QTTARNLTSDSQRLQLDLQKMELLES-------------KMTEEQQSLKNKIKQMTADLETYSDlAALKSSAEEKKKKLH 502
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEagvedeeelraalEQAEEYQELKEELEELEEQLEELLG-ELEELLEALDEEELE 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 148698986 503 QERTVLSTHRNAFKKIMEKLTSDYDTLKTQLQDNETHAQLTNLERKWQHLEQ 554
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKA 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-353 |
4.53e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 98 LGLLRSKISELTTEINKLQKEIEMYNQEnsvYLSYEKRAETLAVEIKDFQGQLADYnmLVDKLNTNTEMEEVMSDYNMLK 177
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAE---EYELLAELARLEQDIARLEERRREL--EERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 178 AQNDRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAADGIIKNMSpEKQVKYIEMKTTNEKLLQELDTLQQQLDSLNMK 257
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 258 KESLETEI-AHSQVKQEAVLLYEKLYELESHRDQMIAEDKsmgspmEERERLLKQVKEDNQEIASMERQLTDIKEKINQF 336
Cdd:COG1196 416 LERLEEELeELEEALAELEEEEEEEEEALEEAAEEEAELE------EEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250
....*....|....*..
gi 148698986 337 SEEIRQLDMDLEEHQGE 353
Cdd:COG1196 490 AARLLLLLEAEADYEGF 506
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
232-391 |
4.98e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 232 EMKTTNEKLLQELDTLQQQLDSLNMKKESLETEiaHSQVKQEAVLLYEKLYELESHRDQMIAEdKSMGSPmeERERLLKQ 311
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETERE--REELAEEVRDLRERLEELEEERDDLLAE-AGLDDA--DAEAVEAR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 312 VKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIEA 391
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
243-477 |
7.35e-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: 42.80 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 243 ELDTLQQQLDSLNMKKESLET--EIAHSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEER-ERLLKQVKEDNQEi 319
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSqlEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKiEELEKQLVLANSE- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 320 asmerqLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELK-KREEN-------------MDAFIETFEEtKNQELER 385
Cdd:pfam15921 358 ------LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlEKEQNkrlwdrdtgnsitIDHLRRELDD-RNMEVQR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 386 kaqIEASIITLLEHCSRNINR-----------MKQISSITNQ------ELKMMQDDLSFKSTEMQKSQTTARNLTSDsqr 448
Cdd:pfam15921 431 ---LEALLKAMKSECQGQMERqmaaiqgknesLEKVSSLTAQlestkeMLRKVVEELTAKKMTLESSERTVSDLTAS--- 504
|
250 260
....*....|....*....|....*....
gi 148698986 449 LQLDLQKMELLESKMTEEQQSLKNKIKQM 477
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQEL 533
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
101-475 |
1.23e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 101 LRSKISELTTEINKLQKEIEMYNQENSvylSYEKRAETLAVEIKDFQGQLADYNMLVDKLNTN-----TEMEEVMSDYNM 175
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQ---SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQikklqQEKELLEKEIER 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 176 LKAQNDRETQSMDVIFTERQAKEKQIRSVEEEVEqekqaadgIIKNMSPEKQVKYIEMKTTNEKLLQELDTLQQQLDSLN 255
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE--------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 256 MKKESLETEIahSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEE------RERLLKQVKEDNQEIA-------SM 322
Cdd:TIGR04523 503 EEKKELEEKV--KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelkKENLEKEIDEKNKEIEelkqtqkSL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 323 ERQLTDIKEKINQFSEEIRQLDMDLEEH---QGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIEASIITLLEH 399
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKEKKDLIKEIEEKekkISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148698986 400 CSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKsQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNKIK 475
Cdd:TIGR04523 661 WPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKK-YITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIK 735
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-537 |
1.24e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 238 EKLLQELDTLQQQLDSLNMKKESLETEIAhsqVKQEAVLLYEKLYELESHRDQMIAEDKsmGSPMEERERLLKQVKEDNQ 317
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLE---ELEERHELYEEAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 318 EIasmERQLTDIKEKINQFSEEIRQLDMDL------------------EEHQGEMNQKY-KELKKREENMDAFIETFEET 378
Cdd:PRK03918 402 EI---EEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgreltEEHRKELLEEYtAELKRIEKELKEIEEKERKL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 379 KNQ--ELERKAQIEASIITLLEhcsrninRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKM 456
Cdd:PRK03918 479 RKElrELEKVLKKESELIKLKE-------LAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 457 ELLESKMTEeqqsLKNKIKQmtadletysdlaalkssaeekkkkLHQERTvlsthrNAFKKIMEKLTSDYDTLKTQLQDN 536
Cdd:PRK03918 552 EELKKKLAE----LEKKLDE------------------------LEEELA------ELLKELEELGFESVEELEERLKEL 597
|
.
gi 148698986 537 E 537
Cdd:PRK03918 598 E 598
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
244-550 |
1.27e-03 |
|
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: 42.03 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 244 LDTLQQQLDSLNMKKESLETeiahsqvkqeavLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQEIASME 323
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEA------------LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 324 RQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELE-RKAQIEASIITLlehcsr 402
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHlRNVQTECEALKL------ 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 403 NINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNKIkqmtADLE 482
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV----SDLE 631
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148698986 483 TYS-DLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTSDYDTLKTQLQDNETHAQLTNLERKWQ 550
Cdd:pfam15921 632 LEKvKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ 700
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
242-362 |
1.30e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 242 QELDTLQQQLDSLNMKKESLeteiahsqVKQEAVLLYEKLYELESHRDQMIaedksmgspmEERERLLKQVKEDNQEIAs 321
Cdd:COG0542 411 EELDELERRLEQLEIEKEAL--------KKEQDEASFERLAELRDELAELE----------EELEALKARWEAEKELIE- 471
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 148698986 322 merQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELK 362
Cdd:COG0542 472 ---EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
316-554 |
1.42e-03 |
|
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: 41.29 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 316 NQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEM---NQKYKELKKREENMDAFIETFEETKNQELERKAQIEAS 392
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLaalERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 393 IITLLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKN 472
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 473 KIKQMTadletysdlaalkssaeekkkklhQERTVLSTHRNAFKKIMEKLTSDYDTLKTQLQDNETHAQltNLERKWQHL 552
Cdd:COG4942 179 LLAELE------------------------EERAALEALKAERQKLLARLEKELAELAAELAELQQEAE--ELEALIARL 232
|
..
gi 148698986 553 EQ 554
Cdd:COG4942 233 EA 234
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
225-340 |
1.49e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 225 EKQVKYIEMKTTNEKLLQELDTLQQQLDSLNMKKESLETEIAHSQVKQEAVLlyEKLYELESHRDQMIAE-DKSMGSPME 303
Cdd:PRK12704 76 ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE--KKEEELEELIEEQLQElERISGLTAE 153
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 148698986 304 E-RERLLKQVKED-NQEIASMERQL-TDIKEKINQFSEEI 340
Cdd:PRK12704 154 EaKEILLEKVEEEaRHEAAVLIKEIeEEAKEEADKKAKEI 193
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
302-569 |
1.87e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 302 MEERERLLKQVKEDNQEIA----SMERQLTDIKEKINQFSEEIRQLDMDLEEhqgeMNQKYKELKKREENMDAFIETFEE 377
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKrdreQWERQRRELESRVAELKEELRQSREKHEE----LEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 378 TKNQELERKAQIEASIITLLEHC---SRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQldlq 454
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVlerETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR---- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 455 kmELLESKMTEEQQsLKNKIKQMTADLETYSDLAALKSSAEEKKKKLhQERTVLSTHR-NAFKKIMEKLTSDYDTLKTQL 533
Cdd:pfam07888 199 --NSLAQRDTQVLQ-LQDTITTLTQKLTTAHRKEAENEALLEELRSL-QERLNASERKvEGLGEELSSMAAQRDRTQAEL 274
|
250 260 270
....*....|....*....|....*....|....*.
gi 148698986 534 QDNETHAQLTNLErkwqhLEQNNFVMKEFIATKSQE 569
Cdd:pfam07888 275 HQARLQAAQLTLQ-----LADASLALREGRARWAQE 305
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
323-556 |
2.24e-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: 41.20 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 323 ERQLTDIKEKINQFSEEIRQLDMDLE--EHQGEMNQKYKELKKREENMDAFIETFE-ETKNQELERKAQIEASIITLLEH 399
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKslERQAEKAERYKELKAELRELELALLVLRlEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 400 CSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSD----SQRLQLDLQKMELLESKMTEEQQSLKNKIK 475
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 476 QMTADLETYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTSDYDTLKTQLQDNEthAQLTNLERKWQHLEQN 555
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN--NEIERLEARLERLEDR 415
|
.
gi 148698986 556 N 556
Cdd:TIGR02168 416 R 416
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
223-381 |
2.68e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 40.01 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 223 SPEKQVKYIEMKTTNEKLLQeLDTLQQQLDSLNMKKESLETEiaHSQVKQEAVLLYEKLYELESHRDQMIAE-DKSMGSP 301
Cdd:pfam04849 146 SCSTPLRRNESFSSLHGCVQ-LDALQEKLRGLEEENLKLRSE--ASHLKTETDTYEEKEQQLMSDCVEQLSEaNQQMAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 302 MEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDL---EEHQGEMNQKYKELKKR-EENMDAFIETFEE 377
Cdd:pfam04849 223 SEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLqasKEAQRQLTSELQELQDRyAECLGMLHEAQEE 302
|
....
gi 148698986 378 TKNQ 381
Cdd:pfam04849 303 LKEL 306
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
238-421 |
4.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 238 EKLLQELDTLQQQLDSLNMKKESLETEIAHSQVKQEAV--LLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKED 315
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLeeELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 316 NQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIEASIIT 395
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEE 200
|
170 180
....*....|....*....|....*.
gi 148698986 396 LLEHCSRNINRMKQISSITNQELKMM 421
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDS 226
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
157-551 |
4.15e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 157 VDKLNTNTEMEEVMSDYNMLKAQNDRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAADGIIKNMSPEKQVKYIEMKTT 236
Cdd:COG5185 204 VNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNEN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 237 NEKLLQELDTLQQQLDSlNMKKESLETEIAHSQVKQEAVLLYEKLYELESHRDQMIAEDKSmgSPMEERERLLKQVKEDN 316
Cdd:COG5185 284 ANNLIKQFENTKEKIAE-YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTA--EIEQGQESLTENLEAIK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 317 QEIASM--ERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKE-LKKREENMDAFIETFEETKNQELERKAQIEASI 393
Cdd:COG5185 361 EEIENIvgEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEiLATLEDTLKAADRQIEELQRQIEQATSSNEEVS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 394 ITLLEHCSRNINRMKQISSITNQELKMMQDDLsfKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNK 473
Cdd:COG5185 441 KLLNELISELNKVMREADEESQSRLEEAYDEI--NRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSK 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148698986 474 IKQMTADLETYSDLAalkssAEEKKKKLHQERTVLSTHRNAFKKIMEKLTSDYDTLKTQLQDNETHAQLTNLERKWQH 551
Cdd:COG5185 519 LDQVAESLKDFMRAR-----GYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPIP 591
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
304-538 |
4.27e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 304 ERERLLK-QVKEDNQEIASMERQLTDIKEKINQFseeirqldmdlEEHQGEMNQKYKELKKREENMdafietFEETKNQE 382
Cdd:PHA02562 167 EMDKLNKdKIRELNQQIQTLDMKIDHIQQQIKTY-----------NKNIEEQRKKNGENIARKQNK------YDELVEEA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 383 LERKAQIEASIITLLEHCSRNINRMKQISSITNQELKM-MQDDLSFKSTEMQKSQTTARNLTsdsQRLQLDLQKMELLES 461
Cdd:PHA02562 230 KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkSKIEQFQKVIKMYEKGGVCPTCT---QQISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 462 KMTEEQQSLKNKIKQMTADLETYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKI---MEKLTS---DYDTLKTQLQD 535
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVkaaIEELQAefvDNAEELAKLQD 386
|
...
gi 148698986 536 NET 538
Cdd:PHA02562 387 ELD 389
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
238-452 |
4.65e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 238 EKLLQELDTLQQQLDSLNMK-KESLETEIAHSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQ----V 312
Cdd:PLN02939 159 EKILTEKEALQGKINILEMRlSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEenmlL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 313 KEDNQEIASMERQLTDIKEKINQFSEE-------IRQLDMDLEEHQGEMNQ----KYKELKKREENMDAFIETFEET--- 378
Cdd:PLN02939 239 KDDIQFLKAELIEVAETEERVFKLEKErslldasLRELESKFIVAQEDVSKlsplQYDCWWEKVENLQDLLDRATNQvek 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 379 ------KNQELERKA-QIEASI--ITLLEHCSRNINRMKqissitnQELKMMQDDLSFKSTEM-----------QKSQTT 438
Cdd:PLN02939 319 aalvldQNQDLRDKVdKLEASLkeANVSKFSSYKVELLQ-------QKLKLLEERLQASDHEIhsyiqlyqesiKEFQDT 391
|
250
....*....|....
gi 148698986 439 ARNLTSDSQRLQLD 452
Cdd:PLN02939 392 LSKLKEESKKRSLE 405
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
303-419 |
5.54e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.69 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 303 EERERLLKQVKEDNQEIasMERQLTDIKEKINQFSEEIRQldmDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQE 382
Cdd:PRK12705 33 KEAERILQEAQKEAEEK--LEAALLEAKELLLRERNQQRQ---EARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110
....*....|....*....|....*....|....*..
gi 148698986 383 LERKAQIEASIITLLEHCSRNINRMKQISSITNQELK 419
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRVAGLTPEQAR 144
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
303-421 |
6.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 303 EERERLLKQVKEDNQEIAsmERQLTDIKEKI----NQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEET 378
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIK--KEALLEAKEEIhklrNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKK 115
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 148698986 379 KNQELERKAQIEASIITLLEHCSRNINRMKQISSITNQELKMM 421
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEI 158
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
238-392 |
9.45e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 238 EKLLQELDTLQQQLDSLNMKKESLETEIAH--SQVKQEAVLLYEKLYE-------LESHR-DQMIAEDKSMGSPMEERER 307
Cdd:COG3883 54 NELQAELEALQAEIDKLQAEIAEAEAEIEErrEELGERARALYRSGGSvsyldvlLGSESfSDFLDRLSALSKIADADAD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 308 LLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKA 387
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
....*
gi 148698986 388 QIEAS 392
Cdd:COG3883 214 AAAAA 218
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
102-590 |
9.48e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 38.85 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 102 RSKISELTTEINKLQKEIEmynqENsvylsyEKRAETLAVEIKDFQGQLADYNmlVDKLNTNTEMEEVMSDYNMLKAQND 181
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKK----EN------KKNIDKFLTEIKKKEKELEKLN--NKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 182 RETQSMDVIFTERQAKEKQIRSVEEEveqekqaadgIIKNMSPEKQVKyiEMKTTNEKLLQELDTLQQQLDSLNMKKESL 261
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKK----------IQKNKSLESQIS--ELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 262 ETEIAHSQVKQEAVL--LYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKED-----NQEIASMERQLTDIK---- 330
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwnkelKSELKNQEKKLEEIQnqis 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 331 ---EKINQFSEEIRQLDMDL-------EEHQGEMNQKYKELKKREENMDAFIETFEETKNQ--ELERK--------AQIE 390
Cdd:TIGR04523 332 qnnKIISQLNEQISQLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQinDLESKiqnqeklnQQKD 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 391 ASIITL---LEHCSRNINRMKQISSITNQELKMMQDDLSFK---------STEMQKSQTTARNLTSDSQRLQLDLQKMEL 458
Cdd:TIGR04523 412 EQIKKLqqeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKeliiknldnTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148698986 459 LE-----SKMTEEQQSLKNKIKQMTadletySDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTsdYDTLKTQL 533
Cdd:TIGR04523 492 KSkekelKKLNEEKKELEEKVKDLT------KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEI 563
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 148698986 534 QDNEThaQLTNLERKWQHLEQNNFVMKEFIATKSQEsdyqpvIKNVMKQIAEYNKTI 590
Cdd:TIGR04523 564 DEKNK--EIEELKQTQKSLKKKQEEKQELIDQKEKE------KKDLIKEIEEKEKKI 612
|
|
| |
