|
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 |
1.86e-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: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 89 RQILDKSYYLGLLRSKISELTTEINKLQKEIEMYNQENSVYLSYEKRAETLAVEIKDFQGQLADYNMLVDKLntNTEMEE 168
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK--QQEINE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 169 VMNDYNMLKAQNDRETQSMDVIFTERQAKEKQIrsveeeveqekQAADGIIKNMspEKQVKYIEMKTT---NEKLLQELD 245
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL-----------EQNNKKIKEL--EKQLNQLKSEISdlnNQKEQDWNK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 246 TLQQQLDSLNIKKESLETEIahSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQ----EIAS 321
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQI--SQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykqEIKN 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 322 MERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIE------TSIIT 395
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKnldntrESLET 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 396 LLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNKIK 475
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 476 QMTADLeTYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTTDYEALKTQLQDNEThaQLTNLERKWQHLEQN 555
Cdd:TIGR04523 549 KDDFEL-KKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK--KISSLEKELEKAKKE 625
|
.
gi 1046888387 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 |
4.98e-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: 62.77 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 303 EERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQE 382
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 383 LERKAQIETSIITlLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESK 462
Cdd:TIGR02168 319 EELEAQLEELESK-LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 463 MTEEQQSLKNKIKQMTADLE-------------TYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTTDYEAL 529
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRErlqqeieellkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888387 530 KTQLQD-NETHAQLTNLERKWQHLEQNNFVMKEFIATKSQESDYQPVIKNVMKQIAEYNKTIMDAL 594
Cdd:TIGR02168 478 DAAERElAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAL 543
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-505 |
4.24e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 225 EKQVKYIEMKTT-----NEKLLQELDTLQQQLDSLNIKKESLETEIAHSQVKQEAVllyEKlyELESHRDQMIAEDksmg 299
Cdd:COG1196 210 EKAERYRELKEElkeleAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL---EA--ELEELRLELEELE---- 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 300 spmEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQgemnqkyKELKKREENMDAFIETFEETK 379
Cdd:COG1196 281 ---LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-------EELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 380 NQELERKAQIETSIITLLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELL 459
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1046888387 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 |
6.19e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 238 EKLLQELDTLQQQLDSLNIKKESLETEiaHSQVKQEAVLLYEklyELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQ 317
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKE--LEELEEELEQLRK---ELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 318 EIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETkNQELERKAQIETSIITLL 397
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-NEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 398 EHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNKIKQM 477
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 478 TADLEtysdlaalkssaeEKKKKLHQERTVLSTHRNAFKKIMEKLTTDYEAL---------KTQLQDNETHAQLTNLERK 548
Cdd:TIGR02168 914 RRELE-------------ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTleeaealenKIEDDEEEARRRLKRLENK 980
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1046888387 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 |
6.98e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 6.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 238 EKLLQELDTLQQQLDSLNIKKESLETEIA------------HSQVKQEAVLLYEKLYELESHRDQMIAEDKSMgspMEER 305
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAeleaeleelrleLEELELELEEAQAEEYELLAELARLEQDIARL---EERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 306 ERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELER 385
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 386 KAQIEtSIITLLEHCSRNINRMKQISSITNQELKMMQDDLsfkSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTE 465
Cdd:COG1196 392 LRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEAL---AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260
....*....|....*....|....*
gi 1046888387 466 EQQSLKNKIKQMTADLETYSDLAAL 490
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAAR 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
101-388 |
2.79e-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: 53.92 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 101 LRSKISELTTEINKLQKEIEMYNQEnsvYLSYEKRAETLAVEIKDFQGQladynmlvDKLNTNTEMEEVMNDYNMLKAQN 180
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKR---LEEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 181 DRETQSMDviftERQAKEKQIRSVEEEVEQEKQAADGIIKnmspEKQVKYIEMKTTNEKLLQELDTLQQQLDSLNikKES 260
Cdd:TIGR02169 311 AEKERELE----DAEERLAKLEAEIDKLLAEIEELEREIE----EERKRRDKLTEEYAELKEELEDLRAELEEVD--KEF 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 261 LETEIAHSQVKQEAVLLYEKLYELESHRDqmiaedksmgspmeereRLLKQVKEDNQEIASMERQLTDIKEKINQFSEEI 340
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELD-----------------RLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1046888387 341 RQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETkNQELERKAQ 388
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV-EKELSKLQR 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
239-390 |
4.09e-07 |
|
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: 51.46 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 239 KLLQELDTLQQQLDSLNIKKESLETEIAhsQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKeDNQE 318
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELA--ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888387 319 IASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFE----ETKNQELERKAQIE 390
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDeelaELEAELEELEAERE 166
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-409 |
9.74e-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: 51.98 E-value: 9.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 101 LRSKISELTTEINKLQKEIEMYNQENSvylSYEKRAETLAVEIKDFQGQLADYNMLVDKLNTNTEMEEVMNdynmlkAQN 180
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELE---ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI------AQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 181 DRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAADGIIKNMSPEKQvkyiEMKTTNEKLLQELDTLQQQLDSLNIKKES 260
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK----ALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 261 LETEIAhsQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEE----RERLLKQVKEDNQEIASMERQLTDIKEKINQF 336
Cdd:TIGR02168 829 LERRIA--ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEleseLEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046888387 337 SEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIETSIITLLEHCSRNINRMKQ 409
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
283-385 |
2.25e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 283 ELESHRDQMIAEDKSMGspMEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELK 362
Cdd:PRK12704 50 EAEAIKKEALLEAKEEI--HKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100
....*....|....*....|...
gi 1046888387 363 KREENmdafIETFEETKNQELER 385
Cdd:PRK12704 128 KKEEE----LEELIEEQLQELER 146
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
283-489 |
5.18e-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: 48.99 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 283 ELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELK 362
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 363 K------REENMDAFIETFEETKNQELERKAQIETSIITLLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQ 436
Cdd:COG4942 108 EllralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEER 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046888387 437 TTARNLTSDSQRLQLDLQKMELLESK----MTEEQQSLKNKIKQMTADLETYSDLAA 489
Cdd:COG4942 188 AALEALKAERQKLLARLEKELAELAAelaeLQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-366 |
5.57e-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: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 101 LRSKISELTTEINKLQKEIEMYNQENSvylSYEKRAETLAVEIKDFQGQLADYNMlvDKLNTNTEMEEVMNDYNMLKAQN 180
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVS---ELEEEIEELQKELYALANEISRLEQ--QKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 181 DRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAADgiiknmspEKQVKYIEMKTTNEKLLQELDT-------LQQQLDS 253
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELE--------ELEAELEELESRLEELEEQLETlrskvaqLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 254 LNIKKESLETEIAHSQV-----KQEAVLLYEKLYELESHRDQMIAEDKSMG--SPMEERERLLKQVKEDNQEIASMERQL 326
Cdd:TIGR02168 398 LNNEIERLEARLERLEDrrerlQQEIEELLKKLEEAELKELQAELEELEEEleELQEELERLEEALEELREELEEAEQAL 477
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1046888387 327 TDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREE 366
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
238-384 |
6.32e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 238 EKLLQELDTLQQQLDSLNIKKESLETEIAHSQVKQEAvllYEKLyeleshrDQMIAEDKSMGSPMEERERL---LKQVKE 314
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREA---LQRL-------AEYSWDEIDVASAEREIAELeaeLERLDA 682
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 315 DNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELE 384
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
104-526 |
7.10e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 104 KISELTTEINKLQKEIEMYNQENSVYLSYEKRAETLAVEIKDFQGQLADYNMLVDKLNTNTEMEEVMNDYNMLKAQNDRE 183
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 184 TQSMDviftERQAKEKQIRSVEEEVEQEKQAADGIIKNMSPEKQVKYIEMKTTNEKLLQELDTLQQQLDSLNIKKESLET 263
Cdd:COG4717 152 EERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 264 EIAHSQVKQEAVLLYEKLYELESHR-----------------------------------DQMIAEDKSMGSPMEERERL 308
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLliaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 309 LKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQgEMNQKYKELKKREEnmdafIETFEETKNQELER-KA 387
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQ-----LEELEQEIAALLAEaGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 388 QIETSIITLLEHCSRNINRMKQISSITNQElkmmqdDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQ 467
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQL------EELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888387 468 QSLKNKIKQMTADlETYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTTDY 526
Cdd:COG4717 456 AELEAELEQLEED-GELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
238-550 |
8.29e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 238 EKLLQELDTLQQQLDSLNIKKESLETEIAHSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQ 317
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 318 EIASMERQLTDIKEK--------INQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQI 389
Cdd:COG4717 171 ELAELQEELEELLEQlslateeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 390 ETSIITLL------------------------------------------EHCSRNINRMKQISSITNQELKMMQDDLSF 427
Cdd:COG4717 251 LLLIAAALlallglggsllsliltiagvlflvlgllallflllarekaslGKEAEELQALPALEELEEEELEELLAALGL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 428 KST--------------EMQKSQTTARNLTSDSQRLQLDLQKMELLES-------------KMTEEQQSLKNKIKQMTAD 480
Cdd:COG4717 331 PPDlspeellelldrieELQELLREAEELEEELQLEELEQEIAALLAEagvedeeelraalEQAEEYQELKEELEELEEQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 481 LE-------------TYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTTDYEALKTQLQDNETHAQLTNLER 547
Cdd:COG4717 411 LEellgeleellealDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAE 490
|
...
gi 1046888387 548 KWQ 550
Cdd:COG4717 491 EWA 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
77-482 |
1.23e-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: 48.58 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 77 LSGMKTGMKGPQRQILDKSYYLGLLRSKISELTTEINKLQKEIEMYNQENSVYLSYEKRAETLAVEIKDFQGQLADYNML 156
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 157 VDKLNTNTEmeevmnDYNMLKAQNDRETQSMDViftERQAKEKQIRSVEEEveqekqaadgiiknmspekqvkyiemktt 236
Cdd:pfam15921 564 IEILRQQIE------NMTQLVGQHGRTAGAMQV---EKAQLEKEINDRRLE----------------------------- 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 237 neklLQELDTLQQQLDSlniKKESLETEIahSQVKQEAVllyeKLYELESHRDQMIAEDKsmgspmEERERLLKQVKEDN 316
Cdd:pfam15921 606 ----LQEFKILKDKKDA---KIRELEARV--SDLELEKV----KLVNAGSERLRAVKDIK------QERDQLLNEVKTSR 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 317 QEIASMERQLTDIKEKINQFSEEIR----QLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIET- 391
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMEtttnKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDAl 746
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 392 -SIITLLEHCSRNINRMKQissITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMT------ 464
Cdd:pfam15921 747 qSKIQFLEEAMTNANKEKH---FLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASlqfaec 823
|
410 420
....*....|....*....|....
gi 1046888387 465 ------EEQQSLKNKIkQMTADLE 482
Cdd:pfam15921 824 qdiiqrQEQESVRLKL-QHTLDVK 846
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
103-590 |
1.94e-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: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 103 SKISELTTEINKLQKEIEMYNQE----NSVYLSYEKRAETLAVEIKDFQGQLADYNmlvDKLNTNTEM-EEVMNDYNMLK 177
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKElknlDKNLNKDEEKINNSNNKIKILEQQIKDLN---DKLKKNKDKiNKLNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 178 AQNDRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAadgiIKNMspEKQVKYIEMKttNEKLLQELDTLQQQLDSLNIK 257
Cdd:TIGR04523 110 SEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE----IKKK--EKELEKLNNK--YNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 258 KESLETEIahSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQEIASMERQLTDIKEKINQFS 337
Cdd:TIGR04523 182 KLNIQKNI--DKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 338 EEIRQLDMDLEEHQGEM---NQKYKELKKREENMDAFIETFEETKNQEL--ERKAQIE------TSIITLLEHCSRNINR 406
Cdd:TIGR04523 260 DEQNKIKKQLSEKQKELeqnNKKIKELEKQLNQLKSEISDLNNQKEQDWnkELKSELKnqekklEEIQNQISQNNKIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 407 MKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMEL----LESKMTEEQQSLKNKIKQMTADLE 482
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESqindLESKIQNQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 483 TYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTTDYEALKTQLQD--NETHAQLTNLERKWQHLEQNNfvmK 560
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVlsRSINKIKQNLEQKQKELKSKE---K 496
|
490 500 510
....*....|....*....|....*....|
gi 1046888387 561 EFIATKSQESDYQPVIKNVMKQIAEYNKTI 590
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKI 526
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
165-391 |
2.61e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 165 EMEEVMNDYNMLKAQNDRETQSMDVIFTERQAKEKQIR---SVEEEVEQEKQAADGIIKNMspEKQVKYIEMKTTNEK-- 239
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGeieKEIEQLEQEEEKLKERLEEL--EEDLSSLEQEIENVKse 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 240 ---LLQELDTLQQQLDSLNIKKESLETEIAHSQVKQ----------EAVLLYEKLYELES-----HRDQMIAEDKSMGsp 301
Cdd:TIGR02169 760 lkeLEARIEELEEDLHKLEEALNDLEARLSHSRIPEiqaelskleeEVSRIEARLREIEQklnrlTLEKEYLEKEIQE-- 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 302 MEERERLLK-QVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKN 380
Cdd:TIGR02169 838 LQEQRIDLKeQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
250
....*....|.
gi 1046888387 381 QELERKAQIET 391
Cdd:TIGR02169 918 RLSELKAKLEA 928
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
302-490 |
3.03e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 302 MEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLD----------MDLEEHQGEMNQKYKELKKREENMDAF 371
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELReeleklekevKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 372 IETFEETKNQELERKAQIETsiitlLEHCSRNINRMKQiSSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQL 451
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEE-----LEEKVKELKELKE-KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190
....*....|....*....|....*....|....*....
gi 1046888387 452 DLQKMELLESKMTEEQQSLKNKIKQMTADLETYSDLAAL 490
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
88-473 |
6.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 88 QRQILDKSYYLGLLRSKISELTTEINKLQKEIEMYNQEnsvYLSYEKRAETLAVEIKDFQGQLADYNMLVDKL-NTNTEM 166
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKE---VKELEELKEEIEELEKELESLEGSKRKLEEKIrELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 167 EEVMNDYNMLKAQNDRetqsmdviFTERQAKEKQIRSVEEEVEQEKQAADGIIKNMSpekqvKYIEMKTTNEKLLQELDT 246
Cdd:PRK03918 269 EELKKEIEELEEKVKE--------LKELKEKAEEYIKLSEFYEEYLDELREIEKRLS-----RLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 247 LQQQLDSLNIKKESLETEIAhsqVKQEAVLLYEKLYELESHRDQMIAEDKsmGSPMEERERLLKQVKEDNQEIasmERQL 326
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLE---ELEERHELYEEAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEI---EEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 327 TDIKEKINQFSEEIRQLDMDL------------------EEHQGEMNQKY-KELKKREENMDAFIETFEETKNQ--ELER 385
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIeelkkakgkcpvcgreltEEHRKELLEEYtAELKRIEKELKEIEEKERKLRKElrELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 386 KAQIETSIITLLEhcsrninRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTE 465
Cdd:PRK03918 488 VLKKESELIKLKE-------LAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
....*...
gi 1046888387 466 EQQSLKNK 473
Cdd:PRK03918 561 LEKKLDEL 568
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
229-483 |
1.35e-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: 44.96 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 229 KYIEMKTTNEKLLQELdtLQQQLDSLNIKKESLETEIAHSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSpMEERERL 308
Cdd:TIGR00618 598 DLTEKLSEAEDMLACE--QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSI-RVLPKEL 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 309 LKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQldmdLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQ 388
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRE----LETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMH 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 389 IETSIITLLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSD-SQRLQLDLQKMELLESKMTEEQ 467
Cdd:TIGR00618 751 QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEiGQEIPSDEDILNLQCETLVQEE 830
|
250
....*....|....*.
gi 1046888387 468 QSLKNKIKQMTADLET 483
Cdd:TIGR00618 831 EQFLSRLEEKSATLGE 846
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
242-427 |
1.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 242 QELDTLQQQLDSLNIKKESLETEIAhsQVKQEAVLLYEKLYELESHRDQmiaedksmgSPMEERERLlkqvkedNQEIAS 321
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELE--RLEARLDALREELDELEAQIRG---------NGGDRLEQL-------EREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 322 MERQLTDIKEKINQFSEEIRQLDMDLEEHQgemnqkyKELKKREENMDAFIETFEETKNQELERKAQIETSIITL---LE 398
Cdd:COG4913 350 LERELEERERRRARLEALLAALGLPLPASA-------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLrreLR 422
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1046888387 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 ... |
238-553 |
1.38e-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: 45.06 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 238 EKLLQELDTLQQQLDSLNIKKESLETEIAHSQVKQEAVLLYEKLyeleshrdQMIAEDKSMGSPMEERERLLKQVKEDNQ 317
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAL--------LKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 318 EIASMERQLTDIKEKINQFSEEIRQLDMDLEE--------HQGEMNQ---KYKELKKREENMDAFIETFEETKNQELERK 386
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikdlGEEEQLRvkeKIGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 387 AQIETSIITLL---EHCSRNINRMK-QISSITN--QELKMMQDDLSFKSTEMQKSQTTARNLTSDSQR----LQLDLQKM 456
Cdd:TIGR02169 325 AKLEAEIDKLLaeiEELEREIEEERkRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREklekLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 457 ELLESKMTEEQQSLKNKIKQMTADLETY-SDLAALKSSAEEKKKKLHQERTVLSThrnaFKKIMEKLTTDYEALKTQLQD 535
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIeAKINELEEEKEDKALEIKKQEWKLEQ----LAADLSKYEQELYDLKEEYDR 480
|
330
....*....|....*...
gi 1046888387 536 NEThaQLTNLERKWQHLE 553
Cdd:TIGR02169 481 VEK--ELSKLQRELAEAE 496
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
231-389 |
1.42e-04 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.86 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 231 IEMKTTNEKLLQELDTLQQQLDSLNIKKESlETEIAHSQVKQEAvllyeklyELESHRDQMIAEDKSmgSPMEERERLLK 310
Cdd:PRK00106 22 ISIKMKSAKEAAELTLLNAEQEAVNLRGKA-ERDAEHIKKTAKR--------ESKALKKELLLEAKE--EARKYREEIEQ 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046888387 311 QVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENmdafIETFEETKNQELERKAQI 389
Cdd:PRK00106 91 EFKSERQELKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQ----VEKLEEQKKAELERVAAL 165
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-554 |
1.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 225 EKQVKYIEMKTTNEKLLQELDTLQQQLDSLNIKKESLETEIAHSQVKQEAvlLYEKLYELESHRDQMIAEDKSMGSPMEE 304
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE--LEELEAELAELQEELEELLEQLSLATEE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 305 R-ERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQEL 383
Cdd:COG4717 193 ElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 384 ERKAQIETSIITLLEHCSRNINRMKQ--------------ISSITNQELKMMQDDLSFKST--------------EMQKS 435
Cdd:COG4717 273 LTIAGVLFLVLGLLALLFLLLAREKAslgkeaeelqalpaLEELEEEELEELLAALGLPPDlspeellelldrieELQEL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 436 QTTARNLTSDSQRLQLDLQKMELLES-------------KMTEEQQSLKNKIKQMTADLETYSDlAALKSSAEEKKKKLH 502
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEagvedeeelraalEQAEEYQELKEELEELEEQLEELLG-ELEELLEALDEEELE 431
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1046888387 503 QERTVLSTHRNAFKKIMEKLTTDYEALKTQLQDNETHAQLTNLERKWQHLEQ 554
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKA 483
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
101-475 |
2.57e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 101 LRSKISELTTEINKLQKEIEMYNQENSvylSYEKRAETLAVEIKDFQGQLADYNMLVDKLNTN-----TEMEEVMNDYNM 175
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQ---SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQikklqQEKELLEKEIER 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 176 LKAQNDRETQSMDVIFTERQAKEKQIRSVEEEVEqekqaadgIIKNMSPEKQVKYIEMKTTNEKLLQELDTLQQQLDSLN 255
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE--------SLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 256 IKKESLETEIahSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEE------RERLLKQVKEDNQEIA-------SM 322
Cdd:TIGR04523 503 EEKKELEEKV--KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKddfelkKENLEKEIDEKNKEIEelkqtqkSL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 323 ERQLTDIKEKINQFSEEIRQLDMDLEEH---QGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIETSIITLLEH 399
Cdd:TIGR04523 581 KKKQEEKQELIDQKEKEKKDLIKEIEEKekkISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046888387 400 CSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKsQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNKIK 475
Cdd:TIGR04523 661 WPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKK-YITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIK 735
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
98-353 |
3.11e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 98 LGLLRSKISELTTEINKLQKEIEMYNQEnsvYLSYEKRAETLAVEIKDFQGQLADYnmLVDKLNTNTEMEEVMNDYNMLK 177
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAE---EYELLAELARLEQDIARLEERRREL--EERLEELEEELAELEEELEELE 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 178 AQNDRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAADGIIKNMSpEKQVKYIEMKTTNEKLLQELDTLQQQLDSLNIK 257
Cdd:COG1196 337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE-ELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 258 KESLETEI-AHSQVKQEAVLLYEKLYELESHRDQMIAEDKsmgspmEERERLLKQVKEDNQEIASMERQLTDIKEKINQF 336
Cdd:COG1196 416 LERLEEELeELEEALAELEEEEEEEEEALEEAAEEEAELE------EEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250
....*....|....*..
gi 1046888387 337 SEEIRQLDMDLEEHQGE 353
Cdd:COG1196 490 AARLLLLLEAEADYEGF 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
103-349 |
3.64e-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: 43.21 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 103 SKISELTTEINKLQKEIEmynQENSVYLSYEKRAETLAVEIKDFQGQLADYNMLVDKLNTntEMEEVMNDYNMLKAQNDR 182
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ--ELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 183 ETQSMDvifTERQAKEKQIRSVEEEVEQEKQAAdgIIKNMSPEKQVKYIE-MKTTNEKLLQELDTLQQQLDSLNIKKESL 261
Cdd:COG4942 95 LRAELE---AQKEELAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 262 ETEIAhsqvkqeavllyeklyELESHRDQMIAEDKSMGSPMEERERLLKQVkedNQEIASMERQLTDIKEKINQFSEEIR 341
Cdd:COG4942 170 EAERA----------------ELEALLAELEEERAALEALKAERQKLLARL---EKELAELAAELAELQQEAEELEALIA 230
|
....*...
gi 1046888387 342 QLDMDLEE 349
Cdd:COG4942 231 RLEAEAAA 238
|
|
| TTC8_N |
cd21341 |
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 ... |
7-63 |
3.75e-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: 41.13 E-value: 3.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046888387 7 SAAPRPISRGGIGLTG--RP-PSGIRPPSGTVRVATAMPPATARPGS----RGGPLGTGGVLSS 63
Cdd:cd21341 66 SQAMRPTTSSGRPITGfvRPgTQSGRPGTSRQALRTPRRAGTARPVTsasgRFVRLGTASMLSG 129
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
289-489 |
3.83e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 289 DQMIAEDKSMGSPMEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKReenm 368
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 369 dafietfeetkNQELERKAQIETSIITLLEhcSRN----INRMKQISSITNQELKMMQDDlsfkSTEMQKSQTTARNLTS 444
Cdd:COG3883 92 -----------ARALYRSGGSVSYLDVLLG--SESfsdfLDRLSALSKIADADADLLEEL----KADKAELEAKKAELEA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1046888387 445 DSQRLQLDLQKMELLESKMTEEQQSLKNKIKQMTADLETYSDLAA 489
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
290-470 |
7.91e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 7.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 290 QMIAE-DKSMGSPMEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKReenM 368
Cdd:PRK11637 54 QDIAAkEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQ---L 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 369 DAFIETFEET------KNQELERKAQIETSIITLlehcsrNINRMKQISsitnqELKMMQDDLSFKSTEMQKSQTTARNL 442
Cdd:PRK11637 131 DAAFRQGEHTglqlilSGEESQRGERILAYFGYL------NQARQETIA-----ELKQTREELAAQKAELEEKQSQQKTL 199
|
170 180 190
....*....|....*....|....*....|....*....
gi 1046888387 443 TSDSQRLQldlQKMEL-----------LESKMTEEQQSL 470
Cdd:PRK11637 200 LYEQQAQQ---QKLEQarnerkktltgLESSLQKDQQQL 235
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
242-362 |
1.02e-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: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 242 QELDTLQQQLDSLNIKKESLeteiahsqVKQEAVLLYEKLYELESHRDQMIaedksmgspmEERERLLKQVKEDNQEIAs 321
Cdd:COG0542 411 EELDELERRLEQLEIEKEAL--------KKEQDEASFERLAELRDELAELE----------EELEALKARWEAEKELIE- 471
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1046888387 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 |
1.51e-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: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 316 NQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEM---NQKYKELKKREENMDAFIETFEETKNQELERKAQIETS 392
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLaalERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 393 IITLLEHCSRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKN 472
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 473 KIKQMTadletysdlaalkssaeekkkklhQERTVLSTHRNAFKKIMEKLTTDYEALKTQLQDNETHAQltNLERKWQHL 552
Cdd:COG4942 179 LLAELE------------------------EERAALEALKAERQKLLARLEKELAELAAELAELQQEAE--ELEALIARL 232
|
..
gi 1046888387 553 EQ 554
Cdd:COG4942 233 EA 234
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
232-391 |
1.80e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 232 EMKTTNEKLLQELDTLQQQLDSLNIKKESLETEiaHSQVKQEAVLLYEKLYELESHRDQMIAEdKSMGSPmeERERLLKQ 311
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETERE--REELAEEVRDLRERLEELEEERDDLLAE-AGLDDA--DAEAVEAR 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 312 VKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIET 391
Cdd:PRK02224 316 REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
244-596 |
1.83e-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: 41.26 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 244 LDTLQQQLDSLNIKKESLETeiahsqvkqeavLLYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQEIASME 323
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEA------------LLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 324 RQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELE-RKAQIETSIITLlehcsr 402
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHlRNVQTECEALKL------ 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 403 NINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNKIkqmtADLE 482
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV----SDLE 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 483 TYS-DLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTTDYEALKTQLQDNETHAQLTNLERKWQ------HLEQN 555
Cdd:pfam15921 632 LEKvKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQlksaqsELEQT 711
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1046888387 556 NFVMKefiATKSQESDYQPVIKNVMKQIAEYNKTImDALHS 596
Cdd:pfam15921 712 RNTLK---SMEGSDGHAMKVAMGMQKQITAKRGQI-DALQS 748
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
102-590 |
1.91e-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: 41.16 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 102 RSKISELTTEINKLQKEIEmynqENsvylsyEKRAETLAVEIKDFQGQLADYNmlVDKLNTNTEMEEVMNDYNMLKAQND 181
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKK----EN------KKNIDKFLTEIKKKEKELEKLN--NKYNDLKKQKEELENELNLLEKEKL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 182 RETQSMDVIFTERQAKEKQIRSVEEEveqekqaadgIIKNMSPEKQVKyiEMKTTNEKLLQELDTLQQQLDSLNIKKESL 261
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKKK----------IQKNKSLESQIS--ELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 262 ETEIAHSQVKQEAVL--LYEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKED-----NQEIASMERQLTDIK---- 330
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDwnkelKSELKNQEKKLEEIQnqis 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 331 ---EKINQFSEEIRQLDMDL-------EEHQGEMNQKYKELKKREENMDAFIETFEETKNQ--ELERK--------AQIE 390
Cdd:TIGR04523 332 qnnKIISQLNEQISQLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQinDLESKiqnqeklnQQKD 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 391 TSIITL---LEHCSRNINRMKQISSITNQELKMMQDDLSFK---------STEMQKSQTTARNLTSDSQRLQLDLQKMEL 458
Cdd:TIGR04523 412 EQIKKLqqeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKeliiknldnTRESLETQLKVLSRSINKIKQNLEQKQKEL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 459 LE-----SKMTEEQQSLKNKIKQMTadletySDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKIMEKLTtdYEALKTQL 533
Cdd:TIGR04523 492 KSkekelKKLNEEKKELEEKVKDLT------KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEI 563
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1046888387 534 QDNEThaQLTNLERKWQHLEQNNFVMKEFIATKSQEsdyqpvIKNVMKQIAEYNKTI 590
Cdd:TIGR04523 564 DEKNK--EIEELKQTQKSLKKKQEEKQELIDQKEKE------KKDLIKEIEEKEKKI 612
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
302-483 |
2.13e-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: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 302 MEERERLLKQVKEDNQEIA----SMERQLTDIKEKINQFSEEIRQLDMDLEEhqgeMNQKYKELKKREENMDAFIETFEE 377
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKrdreQWERQRRELESRVAELKEELRQSREKHEE----LEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 378 TKNQELERKAQIETSIITLLEHC---SRNINRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQldlq 454
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVlerETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR---- 198
|
170 180
....*....|....*....|....*....
gi 1046888387 455 kmELLESKMTEEQQsLKNKIKQMTADLET 483
Cdd:pfam07888 199 --NSLAQRDTQVLQ-LQDTITTLTQKLTT 224
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
225-340 |
2.56e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 225 EKQVKYIEMKTTNEKLLQELDTLQQQLDSLNIKKESLETEIAHSQVKQEAVLlyEKLYELESHRDQMIAE-DKSMGSPME 303
Cdd:PRK12704 76 ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE--KKEEELEELIEEQLQElERISGLTAE 153
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1046888387 304 E-RERLLKQVKED-NQEIASMERQL-TDIKEKINQFSEEI 340
Cdd:PRK12704 154 EaKEILLEKVEEEaRHEAAVLIKEIeEEAKEEADKKAKEI 193
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
243-477 |
2.74e-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: 40.87 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 243 ELDTLQQQLDSLNIKKESLET--EIAHSQVKQEAVLLYEKLYELESHRDQMIAEDKSMGSPMEER-ERLLKQVKEDNQEi 319
Cdd:pfam15921 279 EITGLTEKASSARSQANSIQSqlEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKiEELEKQLVLANSE- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 320 asmerqLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELK-KREEN-------------MDAFIETFEEtKNQELER 385
Cdd:pfam15921 358 ------LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSlEKEQNkrlwdrdtgnsitIDHLRRELDD-RNMEVQR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 386 kaqIETSIITLLEHCSRNINR-----------MKQISSITNQ------ELKMMQDDLSFKSTEMQKSQTTARNLTSDsqr 448
Cdd:pfam15921 431 ---LEALLKAMKSECQGQMERqmaaiqgknesLEKVSSLTAQlestkeMLRKVVEELTAKKMTLESSERTVSDLTAS--- 504
|
250 260
....*....|....*....|....*....
gi 1046888387 449 LQLDLQKMELLESKMTEEQQSLKNKIKQM 477
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQEL 533
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
223-381 |
3.01e-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: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 223 SPEKQVKYIEMKTTNEKLLQeLDTLQQQLDSLNIKKESLETEiaHSQVKQEAVLLYEKLYELESHRDQMIAE-DKSMGSP 301
Cdd:pfam04849 146 SCSTPLRRNESFSSLHGCVQ-LDALQEKLRGLEEENLKLRSE--ASHLKTETDTYEEKEQQLMSDCVEQLSEaNQQMAEL 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 302 MEERERLLKQVKEDNQEIASMERQLTDIKEKINQFSEEIRQLDMDL---EEHQGEMNQKYKELKKR-EENMDAFIETFEE 377
Cdd:pfam04849 223 SEELARKMEENLRQQEEITSLLAQIVDLQHKCKELGIENEELQQHLqasKEAQRQLTSELQELQDRyAECLGMLHEAQEE 302
|
....
gi 1046888387 378 TKNQ 381
Cdd:pfam04849 303 LKEL 306
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
236-412 |
3.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 236 TNEKLLQELDTLQQQLDSLNIKKESLETEI-AHSQVKQEAVLLYEKLYELESHRDQMiaedksmgSPMEERERLLKQVKE 314
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQeELEELEEELEELEAELEELREELEKL--------EKLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 315 DNQEIASMERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQELERKAQIETSII 394
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170
....*....|....*...
gi 1046888387 395 TLLEHCSRNINRMKQISS 412
Cdd:COG4717 217 EAQEELEELEEELEQLEN 234
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
238-537 |
3.95e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 238 EKLLQELDTLQQQLDSLNIKKESLETEIAhsqVKQEAVLLYEKLYELESHRDQMIAEDKsmGSPMEERERLLKQVKEDNQ 317
Cdd:PRK03918 327 EERIKELEEKEERLEELKKKLKELEKRLE---ELEERHELYEEAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 318 EIasmERQLTDIKEKINQFSEEIRQLDMDL------------------EEHQGEMNQKY-KELKKREENMDAFIETFEET 378
Cdd:PRK03918 402 EI---EEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgreltEEHRKELLEEYtAELKRIEKELKEIEEKERKL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 379 KNQ--ELERKAQIETSIITLLEhcsrninRMKQISSITNQELKMMQDDLSFKSTEMQKSQTTARNLTSDSQRLQLDLQKM 456
Cdd:PRK03918 479 RKElrELEKVLKKESELIKLKE-------LAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 457 ELLESKMTEeqqsLKNKIKQmtadletysdlaalkssaeekkkkLHQERTvlsthrNAFKKIMEKLTTDYEALKTQLQDN 536
Cdd:PRK03918 552 EELKKKLAE----LEKKLDE------------------------LEEELA------ELLKELEELGFESVEELEERLKEL 597
|
.
gi 1046888387 537 E 537
Cdd:PRK03918 598 E 598
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
157-551 |
4.01e-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: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 157 VDKLNTNTEMEEVMNDYNMLKAQNDRETQSMDVIFTERQAKEKQIRSVEEEVEQEKQAADGIIKNMSPEKQVKYIEMKTT 236
Cdd:COG5185 204 VNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNEN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 237 NEKLLQELDTLQQQLDSlNIKKESLETEIAHSQVKQEAVLLYEKLYELESHRDQMIAEDKSmgSPMEERERLLKQVKEDN 316
Cdd:COG5185 284 ANNLIKQFENTKEKIAE-YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTA--EIEQGQESLTENLEAIK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 317 QEIASM--ERQLTDIKEKINQFSEEIRQLDMDLEEHQGEMNQKYKE-LKKREENMDAFIETFEETKNQELERKAQIETSI 393
Cdd:COG5185 361 EEIENIvgEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEiLATLEDTLKAADRQIEELQRQIEQATSSNEEVS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 394 ITLLEHCSRNINRMKQISSITNQELKMMQDDLsfKSTEMQKSQTTARNLTSDSQRLQLDLQKMELLESKMTEEQQSLKNK 473
Cdd:COG5185 441 KLLNELISELNKVMREADEESQSRLEEAYDEI--NRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSK 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046888387 474 IKQMTADLETYSDLAalkssAEEKKKKLHQERTVLSTHRNAFKKIMEKLTTDYEALKTQLQDNETHAQLTNLERKWQH 551
Cdd:COG5185 519 LDQVAESLKDFMRAR-----GYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQAREDPIP 591
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
304-538 |
5.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.61 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 304 ERERLLK-QVKEDNQEIASMERQLTDIKEKINQFseeirqldmdlEEHQGEMNQKYKELKKREENMdafietFEETKNQE 382
Cdd:PHA02562 167 EMDKLNKdKIRELNQQIQTLDMKIDHIQQQIKTY-----------NKNIEEQRKKNGENIARKQNK------YDELVEEA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 383 LERKAQIETSIITLLEHCSRNINRMKQISSITNQELKM-MQDDLSFKSTEMQKSQTTARNLTsdsQRLQLDLQKMELLES 461
Cdd:PHA02562 230 KTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkSKIEQFQKVIKMYEKGGVCPTCT---QQISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 462 KMTEEQQSLKNKIKQMTADLETYSDLAALKSSAEEKKKKLHQERTVLSTHRNAFKKI---MEKLT---TDYEALKTQLQD 535
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVkaaIEELQaefVDNAEELAKLQD 386
|
...
gi 1046888387 536 NET 538
Cdd:PHA02562 387 ELD 389
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
280-421 |
5.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 280 KLYELESHRDQMIAEDKSMGSpmEERERLLKQVKEDNQEIAS-MERqltDIKEKINqfseEIRQLDMDLEEHQGEMNQKY 358
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAE--AIKKEALLEAKEEIHKLRNeFEK---ELRERRN----ELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046888387 359 KELKKREENMDAFIETFEETKNQELERKAQIETSIITLLEhcsrninRMKQISSITNQELKMM 421
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ-------ELERISGLTAEEAKEI 158
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
303-419 |
7.30e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.31 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 303 EERERLLKQVKEDNQEIasMERQLTDIKEKINQFSEEIRQldmDLEEHQGEMNQKYKELKKREENMDAFIETFEETKNQE 382
Cdd:PRK12705 33 KEAERILQEAQKEAEEK--LEAALLEAKELLLRERNQQRQ---EARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110
....*....|....*....|....*....|....*..
gi 1046888387 383 LERKAQIETSIITLLEHCSRNINRMKQISSITNQELK 419
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRVAGLTPEQAR 144
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
238-345 |
9.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 38.84 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046888387 238 EKLLQELDTLQQQLDSLNIKKESLEtEIAHSQVKQEAVLLyEKLYELESHRDQMIAEDKSMGSPMEERERLLKQVKEDNQ 317
Cdd:PHA02562 302 TKIKDKLKELQHSLEKLDTAIDELE-EIMDEFNEQSKKLL-ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
90 100
....*....|....*....|....*...
gi 1046888387 318 EIASMERQLTDIKEKINQFSEEIRQLDM 345
Cdd:PHA02562 380 ELAKLQDELDKIVKTKSELVKEKYHRGI 407
|
|
| |
