|
Name |
Accession |
Description |
Interval |
E-value |
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
418-722 |
1.28e-151 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 443.05 E-value: 1.28e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 418 SLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDM 497
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKLIASLKEGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 498 EAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTL 577
Cdd:pfam09787 81 EAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 578 SNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHSASSGPNSGSAINMSGVDSGEGTRLRNVPVLF 657
Cdd:pfam09787 161 SSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLRNVPGLF 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7305095 658 NDTETNLAGMYGKVRKAASSIDQFSIRLGIFLRRYPIARVFVIIYMALLHLWVMIVLLTYSPEMH 722
Cdd:pfam09787 241 SESDSDRAGMYGKVRKAASVIDKFSIRLGIFLRRYPIARLFVIIYMGLLHLWVMIVLLTYTPEMH 305
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
232-518 |
2.68e-15 |
|
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: 80.10 E-value: 2.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 232 LRNEVQSLnQEMASLLQRSKETQEELNKARVR--VEKWNVDNSKSDRITRELRA---QVDDLTEAVAAKDSQLAVLKVRL 306
Cdd:TIGR02168 198 LERQLKSL-ERQAEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEaeeELEELTAELQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 307 QEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQT---LQERLHEADATLKREQESYKQMQSEFA--------- 374
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQleeLEAQLEELESKLDELAEELAELEEKLEelkeelesl 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 375 -ARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEGSSF 453
Cdd:TIGR02168 357 eAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7305095 454 EGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEaQQVSEAESAREQLQDLQDQ 518
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE-RELAQLQARLDSLERLQEN 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
217-568 |
7.63e-15 |
|
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: 78.95 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 217 SRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEkwnvdnSKSDRItRELRAQVDDLTEAVAAKD 296
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE------ELSRQI-SALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 297 SQLAVLKVRLQEADQVLSSRTEALEALRSEKSRimqdHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAAR 376
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLEEAEEELAE----AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 377 LNKMEVDRQNLAEAVTLAERkYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKegssfEGL 456
Cdd:TIGR02168 823 RERLESLERRIAATERRLED-LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR-----SEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 457 ESSTASSMELEELRHEKEMQKEEIQKLMGQMH---------------QLRSELQDMEAQQVSEAESAREQLQDLQDQIAK 521
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLElrleglevridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 7305095 522 QRTSKQEL-------ETELERMKQEFRYME---EDLHRTKNTLQSRIKDREEEIQKL 568
Cdd:TIGR02168 977 LENKIKELgpvnlaaIEEYEELKERYDFLTaqkEDLTEAKETLEEAIEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
226-536 |
7.66e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 7.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 226 RLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDnsksdriTRELRAQVDDLTEAVAAKDSQLAVLKVR 305
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE-------LEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 306 LQEADQVLSSRTEALEALRSEKSRIMQDHKEgsslQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEVDRQ 385
Cdd:COG1196 297 LARLEQDIARLEERRRELEERLEELEEELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 386 NLAEAVTLAERKYSEEKkkvdELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKegssfeglesstassmE 465
Cdd:COG1196 373 ELAEAEEELEELAEELL----EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA----------------E 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7305095 466 LEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERM 536
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
248-606 |
1.95e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 77.28 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 248 QRSKETQEELNKARVRVEKwnvdnskSDRITRELRAQVDDL-TEAVAAKDSQlaVLKVRLQEAD-QVLSSRTEALEALRS 325
Cdd:COG1196 172 ERKEEAERKLEATEENLER-------LEDILGELERQLEPLeRQAEKAERYR--ELKEELKELEaELLLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 326 EKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEvdrqNLAEAVTLAERKYSEEKKKV 405
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA----RLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 406 DELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEgssfeglesstassmeLEELRHEKEMQKEEIQKLMG 485
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----------------AEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 486 QMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEfrymEEDLHRTKNTLQSRIKDREEEI 565
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE----EEEEEEALEEAAEEEAELEEEE 458
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 7305095 566 QKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLESL 606
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
308-626 |
3.18e-14 |
|
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: 76.63 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 308 EADQVLSSRTEALEALRSEKSRIMQDHKEGSSlQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEVDRQNL 387
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEK-ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 388 AEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEgssfeglesstaSSMELE 467
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE------------LRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 468 ELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQqvseAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDL 547
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 548 HRTKN---TLQSRIKDREEEIQKLRNQLTNKTLSNSS----QSELESRLHQLTETLIQK-QTMLESLSTEKNSLVFQLER 619
Cdd:TIGR02168 890 ALLRSeleELSEELRELESKRSELRRELEELREKLAQlelrLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEE 969
|
....*..
gi 7305095 620 LEQQVHS 626
Cdd:TIGR02168 970 ARRRLKR 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
248-622 |
6.65e-14 |
|
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: 75.86 E-value: 6.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 248 QRSKETQEELNKAR---VRVEKwnvdnsksdrITRELRAQVDDL-TEAVAA----------KDSQLAVLKVRLQEADqvl 313
Cdd:TIGR02168 172 ERRKETERKLERTRenlDRLED----------ILNELERQLKSLeRQAEKAerykelkaelRELELALLVLRLEELR--- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 314 ssrtEALEALRSEKSRIMQDHKEGSSLQnQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEVDrqnlaeavtl 393
Cdd:TIGR02168 239 ----EELEELQEELKEAEEELEELTAEL-QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ---------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 394 aERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEgssfeglesstassmELEELRHEK 473
Cdd:TIGR02168 304 -KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEA---------------ELEELEAEL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 474 EMQKEEIQKLMGQMHQLRSELQDMEAQQVS---EAESAREQLQDLQDQIAKQRTSKQELETELERM-KQEFRYMEEDLHR 549
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASlnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEE 447
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7305095 550 TKNTLQSRIKDREEEIQKLRNQLTNKTlsnSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQ 622
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAE---QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
279-592 |
1.33e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 279 RELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRImqdhkegsslqNQALQTLQERLHEADAT 358
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-----------ELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 359 LKREQ---ESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELvdykQKATR 435
Cdd:COG1196 297 LARLEqdiARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL----LEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 436 ILQSKEKLINSLKEgssfeglesstassmELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDL 515
Cdd:COG1196 373 ELAEAEEELEELAE---------------ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305095 516 QDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQL 592
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
220-523 |
1.14e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 220 QELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEkwnvdnsksdritrELRAQVDDLTEAVAAKDSQL 299
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE--------------ELEEELAELEEELEELEEEL 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 300 AVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEfAARLNK 379
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL-LERLER 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 380 MEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLESS 459
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7305095 460 TASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQR 523
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-622 |
1.40e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 346 QTLQERLHEADATLK-REQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQ 424
Cdd:COG1196 216 RELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 425 ELVDYKQKATRILQSKEKLINSLKEgssfeglesstaSSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSE 504
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEE------------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 505 AESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSE 584
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
|
250 260 270
....*....|....*....|....*....|....*...
gi 7305095 585 LESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQ 622
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
226-627 |
4.59e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 226 RLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVE--KWNVDNSKSDRITReLRAQVDDLTEAVAAKDSQLAVLK 303
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDelEAQIRGNGGDRLEQ-LEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 304 VRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEAD---ATLKREQESYKQMQS--------- 371
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRrelRELEAEIASLERRKSniparllal 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 372 --EFAARLNKMEVDRQNLAEAVTLAE------------------------RKYSEEKKKVDELQQQVKLHrasLESAKQE 425
Cdd:COG4913 446 rdALAEALGLDEAELPFVGELIEVRPeeerwrgaiervlggfaltllvppEHYAAALRWVNRLHLRGRLV---YERVRTG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 426 LVDYKQKATRILQSKEKLinSLKEGSSFEGLESSTASSMEL------EEL-RHEKEMQKEeiqklmGQMHQLRS--ELQD 496
Cdd:COG4913 523 LPDPERPRLDPDSLAGKL--DFKPHPFRAWLEAELGRRFDYvcvdspEELrRHPRAITRA------GQVKGNGTrhEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 497 meAQQVSEA----ESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEE--DLHRTKNTLQSRIKD---REEEIQK 567
Cdd:COG4913 595 --RRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYSWDEIDvasAEREIAE 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 568 LRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHSA 627
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
246-634 |
4.75e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.98 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 246 LLQRSKETQEELNKARvrvEKWNVDNSKSDRITRELRAQVD---DLTEAVAAKDSQLAVLK--VRLQEAdqvLSSRTEAL 320
Cdd:COG3096 283 LSERALELRRELFGAR---RQLAEEQYRLVEMARELEELSAresDLEQDYQAASDHLNLVQtaLRQQEK---IERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 321 EALrSEKSRImqdhkegsslQNQALQTLQERLHEADATLKREQESYKQMQSEFAarlnkmevDRQNLAEAVTLAERKYSE 400
Cdd:COG3096 357 EEL-TERLEE----------QEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA--------DYQQALDVQQTRAIQYQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 401 EKKKVDELQQQVKLHRASLESAKQELVDYKQKA----TRILQSKEKLINSLKEGSSFE-----------GLESSTASSME 465
Cdd:COG3096 418 AVQALEKARALCGLPDLTPENAEDYLAAFRAKEqqatEEVLELEQKLSVADAARRQFEkayelvckiagEVERSQAWQTA 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 466 LEELRhekemQKEEIQKLMGQMHQLRSELQDMEaQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEE 545
Cdd:COG3096 498 RELLR-----RYRSQQALAQRLQQLRAQLAELE-QRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 546 DLhRTKNTLQSRIKDREEEIQKLRNQLTNK------------TLSNSSQSELESRlHQLTETLiqkQTMLE---SLSTEK 610
Cdd:COG3096 572 QA-AEAVEQRSELRQQLEQLRARIKELAARapawlaaqdaleRLREQSGEALADS-QEVTAAM---QQLLErerEATVER 646
|
410 420
....*....|....*....|....*.
gi 7305095 611 NSLVFQLERLEQQVH--SASSGPNSG 634
Cdd:COG3096 647 DELAARKQALESQIErlSQPGGAEDP 672
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
232-586 |
9.18e-12 |
|
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: 68.94 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 232 LRNEVQSLNQEMASLLqRSKETQEELNKAR--VRVEKWNvdnsKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEA 309
Cdd:TIGR02169 196 KRQQLERLRREREKAE-RYQALLKEKREYEgyELLKEKE----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 310 DQVLSSRTEALEALRSEKSRimqdhkegsslqnqALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEVDRQNLAE 389
Cdd:TIGR02169 271 EQLLEELNKKIKDLGEEEQL--------------RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 390 AVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQEL--VDYKQKATRILQSKEKlinslkegssfeglesstassMELE 467
Cdd:TIGR02169 337 EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELeeVDKEFAETRDELKDYR---------------------EKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 468 ELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQqvseaesareqLQDLQDQIAkqrtskqELETELERMKQEFRYMEEDL 547
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAA-----------IAGIEAKIN-------ELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 7305095 548 HRTK---NTLQSRIKDREEEIQKLRNQLTnktlsnSSQSELE 586
Cdd:TIGR02169 458 EQLAadlSKYEQELYDLKEEYDRVEKELS------KLQRELA 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-631 |
2.76e-11 |
|
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: 67.40 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 345 LQTLQERLHEAD---ATLKREQESYKQMQSEFAARLN---KMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRAS 418
Cdd:TIGR02169 676 LQRLRERLEGLKrelSSLQSELRRIENRLDELSQELSdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 419 LESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDME 498
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 499 AQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRymeedlhrtknTLQSRIKDREEEIQKLRNQLtnktls 578
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR-----------DLESRLGDLKKERDELEAQL------ 898
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 7305095 579 nssqSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHSASSGP 631
Cdd:TIGR02169 899 ----RELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
220-623 |
1.07e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 220 QELSNLRLENQLLRNEVQSLNQemasLLQRSKETQEELNKARVRVEKWNvdnSKSDRITRELRAQvdDLTEAVAAKDSQL 299
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELR---EELEKLEKLLQLL--PLYQELEALEAEL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 300 AVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNK 379
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 380 MEVDRQNLAEAVTLAERKysEEKKKVDELQQQVKLH--RASLESAKQELVDYKQKATRILQskekLINSLKEGSSFEGLE 457
Cdd:COG4717 222 LEELEEELEQLENELEAA--ALEERLKEARLLLLIAaaLLALLGLGGSLLSLILTIAGVLF----LVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 458 SSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSElQDMEAQQVSEAESAREQLQDLQDQIAKQRT--SKQELETELER 535
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLP-PDLSPEELLELLDRIEELQELLREAEELEEelQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 536 MKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKT------LSNSSQSELESRLHQLTETLIQKQTMLESLSTE 609
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLgeleelLEALDEEELEEELEELEEELEELEEELEELREE 454
|
410
....*....|....
gi 7305095 610 KNSLVFQLERLEQQ 623
Cdd:COG4717 455 LAELEAELEQLEED 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
206-623 |
3.47e-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: 63.54 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 206 EEHSSTPSDGSSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVE-----KWNVDNSKSDRITRE 280
Cdd:TIGR02168 351 EELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLErledrRERLQQEIEELLKKL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 281 LRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNqALQTLQERLHEADATLK 360
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSEGVK 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 361 REQESYKQMQSEFAARLNKMEVDRQ-NLAEAVTLAER------KYSEEKKKVDELQQQVKLHRAS--------------- 418
Cdd:TIGR02168 510 ALLKNQSGLSGILGVLSELISVDEGyEAAIEAALGGRlqavvvENLNAAKKAIAFLKQNELGRVTflpldsikgteiqgn 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 419 -LESAKQ---------ELVDYKQKATRI-------------LQSKEKLINSLKEGSSFEGLE--------------SSTA 461
Cdd:TIGR02168 590 dREILKNiegflgvakDLVKFDPKLRKAlsyllggvlvvddLDNALELAKKLRPGYRIVTLDgdlvrpggvitggsAKTN 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 462 SSM-----ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQ--------------------QVSEAESAREQLQDLQ 516
Cdd:TIGR02168 670 SSIlerrrEIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleelsrqisalrkDLARLEAEVEQLEERI 749
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 517 DQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLtnktlsnssqSELESRLHQLTETL 596
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----------DELRAELTLLNEEA 819
|
490 500
....*....|....*....|....*..
gi 7305095 597 IQKQTMLESLSTEKNSLVFQLERLEQQ 623
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
397-624 |
5.77e-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: 62.73 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 397 KYSEEKKKVDELQQQVKlhraSLESAKQELVDYKQKATRILQSKEKLINSLKEgssfegleSSTASSMELEELRHEKEMQ 476
Cdd:TIGR04523 212 KNKSLESQISELKKQNN----QLKDNIEKKQQEINEKTTEISNTQTQLNQLKD--------EQNKIKKQLSEKQKELEQN 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 477 KEEIQKLMGQMHQLRSELQDMEAQQV--------SEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFrymeEDLH 548
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLNNQKEqdwnkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL----TNSE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 549 RTKNTLQSRIKDREEEIQKLRNQ----LTNKTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQV 624
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKEnqsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-685 |
1.33e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 377 LNKMEVDRQNLAEAVTLAErkysEEKKKVDELQQQVK-----------LHRASLESAKQELVDYKQKATRILQSKEKLIN 445
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILN----ELERQLKSLERQAEkaerykelkaeLRELELALLVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 446 SLKEGSSfeGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTS 525
Cdd:TIGR02168 254 ELEELTA--ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 526 KQELETELERMKQEFrymeedlhrtkNTLQSRIKDREEEIQKLRNQLTN-KTLSNSSQSELE---SRLHQLTETLIQKQT 601
Cdd:TIGR02168 332 LDELAEELAELEEKL-----------EELKEELESLEAELEELEAELEElESRLEELEEQLEtlrSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 602 MLESLSTEKNSLVFQLERLEQQVHSASSGPNSGSAINMSGVDSGEGTRLRNVPVLFNDTETNLAGMYGKVRKAASSIDQF 681
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
....
gi 7305095 682 SIRL 685
Cdd:TIGR02168 481 EREL 484
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
218-613 |
1.82e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.21 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 218 RSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEEL-----NKARVRVEKWNVDnsksDRITR---------ELRA 283
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIeryeeQREQARETRDEAD----EVLEEheerreeleTLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 284 QVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRimqdhkegSSLQNQALQTLQERLHEADATLKREQ 363
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL--------DDADAEAVEARREELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 364 ESYKQMQSEFaarlnkmEVDRQNLAEAVTLAERKYSEEKKKVDELQqqvklhrASLESAKQELVDYKQKATRIlqskEKL 443
Cdd:PRK02224 331 EECRVAAQAH-------NEEAESLREDADDLEERAEELREEAAELE-------SELEEAREAVEDRREEIEEL----EEE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 444 INSLKEGSSFEGLESSTASSmELEELRHEKEMQKEEIQKLMGQMHQLRSELQdmEAQQVSEAESAREQLQDLQDQ----- 518
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAED-FLEELREERDELREREAELEATLRTARERVE--EAEALLEAGKCPECGQPVEGSphvet 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 519 IAKQRTSKQELETELERMKQEFRYMEEDLHRTKNtlqsrIKDREEEIQKLRNQLTNktlsnssqseLESRLHQLTETLIQ 598
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAED-----LVEAEDRIERLEERRED----------LEELIAERRETIEE 534
|
410
....*....|....*
gi 7305095 599 KQTMLESLSTEKNSL 613
Cdd:PRK02224 535 KRERAEELRERAAEL 549
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
217-629 |
1.83e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 217 SRSQELSNLRLENQLLRNEVQSLNQEMASL---LQRSKETQEELNKARVRVEKwnvdnSKSDRITRELRAQVDDLTEAVA 293
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLedrRERLQQEIEELLKKLEEAEL-----KELQAELEELEEELEELQEELE 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 294 AKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEAD-----ATLKREQESYKQ 368
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGilgvlSELISVDEGYEA 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 369 -MQSEFAARLNKMEVDRQNLAEA------------VTLAERKYSEEKKKVDELQQQVKLHRASLESAKqELVDYKQKATR 435
Cdd:TIGR02168 538 aIEAALGGRLQAVVVENLNAAKKaiaflkqnelgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAK-DLVKFDPKLRK 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 436 I-------------LQSKEKLINSLKEGSSFEGLE--------------SSTASSM-----ELEELRHEKEMQKEEIQKL 483
Cdd:TIGR02168 617 AlsyllggvlvvddLDNALELAKKLRPGYRIVTLDgdlvrpggvitggsAKTNSSIlerrrEIEELEEKIEELEEKIAEL 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 484 MGQMHQLRSELQDMEAQ--------------------QVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYM 543
Cdd:TIGR02168 697 EKALAELRKELEELEEEleqlrkeleelsrqisalrkDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 544 EEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKtlsNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 623
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDEL---RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
....*.
gi 7305095 624 VHSASS 629
Cdd:TIGR02168 854 IESLAA 859
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
216-624 |
1.84e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.19 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 216 SSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNvdNSKSDRITRELRAQVDDlteavaaK 295
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN--NQKEQDWNKELKSELKN-------Q 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 296 DSQLAVLKVRLQEADQVLSSRTEALEALRSEKSrimqdhkeGSSLQNQALQTLQERLHEADATLKREQESYKQmqsefaa 375
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELT--------NSESENSEKQRELEEKQNEIEKLKKENQSYKQ------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 376 RLNKMEVDRQNLaeavtlaERKYSEEKKKVDELQQQVKlhraSLESAKQELVDYKQ--KATRILQSKEklINSLKEgssf 453
Cdd:TIGR04523 385 EIKNLESQINDL-------ESKIQNQEKLNQQKDEQIK----KLQQEKELLEKEIErlKETIIKNNSE--IKDLTN---- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 454 egleSSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDME---AQQVSEAESAREQLQDLQDQIAkqrtskqele 530
Cdd:TIGR04523 448 ----QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQkelKSKEKELKKLNEEKKELEEKVK---------- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 531 tELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLS---NSSQSELEsRLHQLTETLI----QKQTML 603
Cdd:TIGR04523 514 -DLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEkeiDEKNKEIE-ELKQTQKSLKkkqeEKQELI 591
|
410 420
....*....|....*....|.
gi 7305095 604 ESLSTEKNSLVFQLERLEQQV 624
Cdd:TIGR04523 592 DQKEKEKKDLIKEIEEKEKKI 612
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
222-618 |
1.98e-09 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 60.99 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 222 LSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRV-EKWNVDNSKSDRITR------ELRAQVDDLTEAVAA 294
Cdd:pfam10174 312 LETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLeEKESFLNKKTKQLQDlteeksTLAGEIRDLKDMLDV 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 295 KDSQLAVLKVRLQEADQVLSSRTEALEALRseksRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFA 374
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLK----ERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 375 ARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQqvklHRASL-ESAKQELVDYKQKATRILQSKE---KLINSLKEG 450
Cdd:pfam10174 468 EELESLKKENKDLKEKVSALQPELTEKESSLIDLKE----HASSLaSSGLKKDSKLKSLEIAVEQKKEecsKLENQLKKA 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 451 SSFEglESSTASSMELEELRH-EKEMQ--KEEIQKLMGQMHQLRSELQDMEA------QQVSEAES-AREQLQDLQDQIA 520
Cdd:pfam10174 544 HNAE--EAVRTNPEINDRIRLlEQEVAryKEESGKAQAEVERLLGILREVENekndkdKKIAELESlTLRQMKEQNKKVA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 521 KQRTSKQELETELERMKQEFRYMEEDLHRtkNTLQSRIKDREEEIQKLRNQL--TNKTLSNSSQSELESRLH-------- 590
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLLEEARRREDNLAD--NSQQLQLEELMGALEKTRQELdaTKARLSSTQQSLAEKDGHltnlraer 699
|
410 420 430
....*....|....*....|....*....|
gi 7305095 591 --QLTETLIQKQTMLESLSTEKNSLVFQLE 618
Cdd:pfam10174 700 rkQLEEILEMKQEALLAAISEKDANIALLE 729
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
219-632 |
2.64e-09 |
|
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: 60.90 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 219 SQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEK-WNVDNSKSDRITrELRAQVDDLTEAVaakds 297
Cdd:pfam15921 355 NSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRlWDRDTGNSITID-HLRRELDDRNMEV----- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 298 qlavlkvrlqeadqvlsSRTEAL-EALRSEKSRIMQDHKEGSSLQNQALqtlqERLHEADATLKREQESYKQMQSEFAAR 376
Cdd:pfam15921 429 -----------------QRLEALlKAMKSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 377 ---LNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRI------LQSKEKLINSL 447
Cdd:pfam15921 488 kmtLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECealklqMAEKDKVIEIL 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 448 KEG----SSFEGLESSTASSMELEELRHEKEM--QKEEIQKLM-------GQMHQLRSELQDMEAQQVSEAESAREQLQD 514
Cdd:pfam15921 568 RQQienmTQLVGQHGRTAGAMQVEKAQLEKEIndRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERLRA 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 515 LQD----------QIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSS--- 581
Cdd:pfam15921 648 VKDikqerdqllnEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamk 727
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 582 -----QSELESRLHQLTETLIQKQTMLESLST---EKNSLVFQLERLEQQVHSASSGPN 632
Cdd:pfam15921 728 vamgmQKQITAKRGQIDALQSKIQFLEEAMTNankEKHFLKEEKNKLSQELSTVATEKN 786
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
189-641 |
2.96e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.44 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 189 EVHKEPSEESTAPSATSEEHSSTPSDGSSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWN 268
Cdd:PRK02224 325 ELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 269 VDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVL--------------SSRTEALEALRSEKSRimqdh 334
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgqpvegSPHVETIEEDRERVEE----- 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 335 kegsslqnqaLQTLQERLHEADATLKREQESYKQMQsEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKL 414
Cdd:PRK02224 480 ----------LEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 415 HRASLESAKQELVDYKQKATRILQSKEKLINSLKE-GSSFEGLESSTASSMELEELRHEKEMQKEEiqklmgqmhqlRSE 493
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAElKERIESLERIRTLLAAIADAEDEIERLREK-----------REA 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 494 LQDMEAQQVSEAESAREQLQDLQ-----DQIAKQRTSKQELETELERMKQEFRYMEEDlhrtKNTLQSRIKDREEEIQKL 568
Cdd:PRK02224 618 LAELNDERRERLAEKRERKRELEaefdeARIEEAREDKERAEEYLEQVEEKLDELREE----RDDLQAEIGAVENELEEL 693
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7305095 569 RNQLTNKTLSNSSQSELESrLHQLTETLiqkQTMLESLSTE-KNSLVFQLERLEQQVHSASSGPNSGSAINMSG 641
Cdd:PRK02224 694 EELRERREALENRVEALEA-LYDEAEEL---ESMYGDLRAElRQRNVETLERMLNETFDLVYQNDAYSHIELDG 763
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
354-572 |
6.11e-09 |
|
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: 58.62 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 354 EADATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKA 433
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 434 TRILQSKEKLINSLKEGSSFEGLESsTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQvSEAESAREQLQ 513
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAL-LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR-AELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 514 DLQDQIAKQRTskqeletELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQL 572
Cdd:COG4942 178 ALLAELEEERA-------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
219-569 |
8.63e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 219 SQELSNLRLENQLLRNEVQSLN---------QEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLT 289
Cdd:COG4717 101 EEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 290 EAV----AAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSslQNQALQTLQERLHEADATLK----- 360
Cdd:COG4717 181 ELLeqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE--NELEAAALEERLKEARLLLLiaaal 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 361 -------REQESYKQMQSEFAA-----------RLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESA 422
Cdd:COG4717 259 lallglgGSLLSLILTIAGVLFlvlgllallflLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 423 KQELVDYKQKATRILQSKEKLINSLKEGSSFEGLES--STASSMELEELRhEKEMQKEEIQKLMGQMHQLRSELQDM--- 497
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELlge 417
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 498 --EAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEED-----LHRTKNTLQSRIKDREEEIQKLR 569
Cdd:COG4717 418 leELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgelaeLLQELEELKAELRELAEEWAALK 496
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
221-565 |
9.25e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQ---EELNKARVR--VEKWNVDNSKSDRITRELRAQVDDLTEAVAAK 295
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKkaiEELKKAKGKcpVCGRELTEEHRKELLEEYTAELKRIEKELKEI 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 296 DSQLAVLKVRLQEADQVLSSRTE------ALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADA---TLKREQESY 366
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESEliklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGeikSLKKELEKL 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 367 KQMQSEFAARLNKMEVDRQNLAEAVT-LAERKYSEEKKKVDELQQQVKLHRASLEsakqeLVDYKQKATRILQSKEKLIN 445
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKeLEELGFESVEELEERLKELEPFYNEYLE-----LKDAEKELEREEKELKKLEE 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 446 SLKEgsSFEGLESSTAS----SMELEELrhEKEMQKEEIQKLMGQMHQLRSELQDMEAQqVSEAESAREQ----LQDLQD 517
Cdd:PRK03918 627 ELDK--AFEELAETEKRleelRKELEEL--EKKYSEEEYEELREEYLELSRELAGLRAE-LEELEKRREEikktLEKLKE 701
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 7305095 518 QIAKQRTSKQELEtELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEI 565
Cdd:PRK03918 702 ELEEREKAKKELE-KLEKALERVEELREKVKKYKALLKERALSKVGEI 748
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
341-581 |
1.06e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 341 QNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNkmevDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLE 420
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 421 SAKQELVDYKQKATRILQSKEKL--INSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDME 498
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLgrQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 499 AQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEfrymEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLS 578
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 7305095 579 NSS 581
Cdd:COG4942 250 ALK 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
216-592 |
1.17e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 216 SSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEkwnvdnsksdritrELRAQVDDLTEavaak 295
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE--------------ELEEKVKELKE----- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 296 dsqlavlkvrLQEADQVLSSRTEALEALRSEKSRImqdHKEGSSLQNQaLQTLQERLHEADaTLKREQESYKQMQSEFAA 375
Cdd:PRK03918 288 ----------LKEKAEEYIKLSEFYEEYLDELREI---EKRLSRLEEE-INGIEERIKELE-EKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 376 RLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEgsSFEG 455
Cdd:PRK03918 353 RLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK--AIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 456 LESSTAS----SMELEElRHEKEMQKE----------EIQKLMGQMHQLRSELQDMEAQQVSEAESAReqLQDLQDQI-- 519
Cdd:PRK03918 431 LKKAKGKcpvcGRELTE-EHRKELLEEytaelkriekELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAEQLke 507
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7305095 520 AKQRTSKQELEtELERMKQEFRYMEEDLhrtkNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQL 592
Cdd:PRK03918 508 LEEKLKKYNLE-ELEKKAEEYEKLKEKL----IKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEL 575
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
213-621 |
2.56e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 213 SDGSSRSQELSNLRLENQLLRNEVQSLnQEMASLLQRSKETQEELNKARVRVEKWNVDnsksdritrELRAQVDDLTEAV 292
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKEELERLKKRLTGLTPE---------KLEKELEELEKAK 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 293 AAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSR-------IMQDHKEgsslqnqalqtlqERLHEADATLKREQES 365
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEHRK-------------ELLEEYTAELKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 366 YKqmqsEFAARLNKMEVDRQNLaEAVTLAERKYSEEKKKVDELQQ-QVKLHRASLESAKQELVDYKQKATRILQSKEKLI 444
Cdd:PRK03918 468 LK----EIEEKERKLRKELREL-EKVLKKESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 445 NSLKEGSSFEGLESstassmELEELRHEKEMQKEEIQKLMGQMHQLRSElqdmeaqQVSEAESAREQLQDLQDQIAKQRT 524
Cdd:PRK03918 543 SLKKELEKLEELKK------KLAELEKKLDELEEELAELLKELEELGFE-------SVEELEERLKELEPFYNEYLELKD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 525 SKQELETELERMKQEFRYME---EDLHRTKNTLQsRIKDREEEIQKLRNQ-----LTNKTLSNSSQ-SELESRLHQLTET 595
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDkafEELAETEKRLE-ELRKELEELEKKYSEeeyeeLREEYLELSRElAGLRAELEELEKR 688
|
410 420
....*....|....*....|....*.
gi 7305095 596 LIQKQTMLESLSTEKNSLVFQLERLE 621
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKKELE 714
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
251-623 |
2.76e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 251 KETQEELNKARVRVEKWNVDNSKSDRITR--ELRAQVDDLTEAvAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEK- 327
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEEDKKKADELKKaaAAKKKADEAKKK-AEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEa 1462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 328 SRIMQDHKEGSSLQNQAlqtlqERLHEADATLKREQESYKQmqsefAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDE 407
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKA-----EEAKKADEAKKKAEEAKKK-----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 408 LQQQVKLHRASLESAKQELvdYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEIQKLMGQM 487
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADEL--KKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 488 HQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELE----RMKQEFRYMEEDlhrtkntlqsriKDREE 563
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenkiKAAEEAKKAEED------------KKKAE 1678
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 564 EIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 623
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
220-541 |
3.82e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 220 QELSNLRLENQLLRNEVQSLNQEMASLLQR-SKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQ 298
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 299 LAVLKV--RLQEADQVLSSRTeALEALRSEKSRIMQDHKE--------------GSSLQNQALQTLQERLHEADATLKRE 362
Cdd:COG4717 236 LEAAALeeRLKEARLLLLIAA-ALLALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 363 QESYKQMQSEFAARLNKMEVDRQNLAEAVTLAErKYSEEKKKVDELQQQVKLH-----------------RASLESAKQE 425
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEeleqeiaallaeagvedEEELRAALEQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 426 LVDYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQ-VSE 504
Cdd:COG4717 394 AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGeLAE 473
|
330 340 350
....*....|....*....|....*....|....*..
gi 7305095 505 AESAREQLQDLQDQIAKQRTSKQELETELERMKQEFR 541
Cdd:COG4717 474 LLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
219-619 |
4.58e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 219 SQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVR---VEKWNVDNSKSDRITRELRAQVDDLTEAVAAK 295
Cdd:TIGR04523 158 NNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLlsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 296 DSQLAVLKVRLQEAD----QVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQaLQTLQERLHEADAtlKREQESYKQMQS 371
Cdd:TIGR04523 238 QQEINEKTTEISNTQtqlnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ-LNQLKSEISDLNN--QKEQDWNKELKS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 372 EFAARLNKMEVdrqnlaeavtlAERKYSEEKKKVDELQQQVklhrASLESAKQELVDYKQKATRILQSKEKLINSLKEGS 451
Cdd:TIGR04523 315 ELKNQEKKLEE-----------IQNQISQNNKIISQLNEQI----SQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 452 SfEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQ---VSEAESAREQLQDLQDQIAKQRTSKQE 528
Cdd:TIGR04523 380 Q-SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIerlKETIIKNNSEIKDLTNQDSVKELIIKN 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 529 LETELERMKQEFRYMEEDLHRTKNTL---QSRIKDREEEIQKLRNQltnKTLSNSSQSELESRLHQLTEtliqKQTMLES 605
Cdd:TIGR04523 459 LDNTRESLETQLKVLSRSINKIKQNLeqkQKELKSKEKELKKLNEE---KKELEEKVKDLTKKISSLKE----KIEKLES 531
|
410
....*....|....
gi 7305095 606 LSTEKNSLVFQLER 619
Cdd:TIGR04523 532 EKKEKESKISDLED 545
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
233-613 |
4.87e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 56.40 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 233 RNEVQSLNQEMASLLQRSkeTQEELNKAR---------VRVEKWNvdnSKSDRITRELRAQVDDLTEAVAAKDSQLAVLK 303
Cdd:pfam06160 9 YKEIDELEERKNELMNLP--VQEELSKVKklnltgetqEKFEEWR---KKWDDIVTKSLPDIEELLFEAEELNDKYRFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 304 VR--LQEADQVLSSRTEALEALRSEKSRIMQDHKEgsslQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKME 381
Cdd:pfam06160 84 AKkaLDEIEELLDDIEEDIKQILEELDELLESEEK----NREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 382 vdrQNLAEAVTLAER-KYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQkatrILQSKeklINSLKEGssfegLESST 460
Cdd:pfam06160 160 ---EEFSQFEELTESgDYLEAREVLEKLEEETDALEELMEDIPPLYEELKT----ELPDQ---LEELKEG-----YREME 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 461 ASSMELEELRHEKEMQ--KEEIQKLMGQMHQLrsELQDMEaQQVSEAESAREQLQD------------------LQDQIA 520
Cdd:pfam06160 225 EEGYALEHLNVDKEIQqlEEQLEENLALLENL--ELDEAE-EALEEIEERIDQLYDllekevdakkyveknlpeIEDYLE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 521 KQRTSKQELETELERMKQEFRYMEEDLHRTKNtLQSRIKDREEEIQKLRNQLTNKTlsnSSQSELESRLHQLTETLIQKQ 600
Cdd:pfam06160 302 HAEEQNKELKEELERVQQSYTLNENELERVRG-LEKQLEELEKRYDEIVERLEEKE---VAYSELQEELEEILEQLEEIE 377
|
410
....*....|...
gi 7305095 601 TMLESLSTEKNSL 613
Cdd:pfam06160 378 EEQEEFKESLQSL 390
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
214-630 |
4.98e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.77 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 214 DGSSRSQELSNLrlenQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDnsKSDRITRELRAQVD--DLTEA 291
Cdd:pfam12128 338 DIETAAADQEQL----PSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNR--DIAGIKDKLAKIREarDRQLA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 292 VAAKDSQLAVLKVRLQEADQVLSSRTEAL---EALRSEKSRIMQDHKEGSSLQNQALQtlQERLHEADATLKREQESYKQ 368
Cdd:pfam12128 412 VAEDDLQALESELREQLEAGKLEFNEEEYrlkSRLGELKLRLNQATATPELLLQLENF--DERIERAREEQEAANAEVER 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 369 MQSEfaarLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASL-ESAKQELVDYKQKATRILQSKEKLINSL 447
Cdd:pfam12128 490 LQSE----LRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlHFLRKEAPDWEQSIGKVISPELLHRTDL 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 448 ---KEGSSFEGLESSTASSMELEELRHEKEMQKEEiqklmgqmhQLRSELQDMEaqqvSEAESAREQLQDLQDQIAKQRT 524
Cdd:pfam12128 566 dpeVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE---------ELRERLDKAE----EALQSAREKQAAAEEQLVQANG 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 525 SKQELETELERMKQEFRYMEEDLHRTKNTLQS-----------RIKDREEEIQKLRNQLtnKTLSNSSQSELESRLHQLT 593
Cdd:pfam12128 633 ELEKASREETFARTALKNARLDLRRLFDEKQSekdkknkalaeRKDSANERLNSLEAQL--KQLDKKHQAWLEEQKEQKR 710
|
410 420 430
....*....|....*....|....*....|....*..
gi 7305095 594 ETLIQKQTMLESLSTEKNSlvfQLERLEQQVHSASSG 630
Cdd:pfam12128 711 EARTEKQAYWQVVEGALDA---QLALLKAAIAARRSG 744
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
220-568 |
5.88e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 220 QELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKW--NVDNSKSDRITRELRAQVDDLTEAVAAKDS 297
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVkaALLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 298 QL-AVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERL---HEADATLKREQESYKQMQSEF 373
Cdd:COG1196 543 ALaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGaavDLVASDLREADARYYVLGDTL 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 374 AARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDyKQKATRILQSKEKLINSLKEGSSF 453
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEA-EAELEELAERLAEEELELEEALLA 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 454 EGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESARE--QLQDLQDQIAKQRTSKQELET 531
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppDLEELERELERLEREIEALGP 781
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 7305095 532 -------ELERMKQEFRYMEE---DLHRTKNTLQSRIKDREEEIQKL 568
Cdd:COG1196 782 vnllaieEYEELEERYDFLSEqreDLEEARETLEEAIEEIDRETRER 828
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
220-433 |
8.53e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 220 QELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKwnvDNSKSDRITRELRAQVDDLTEAVAakdsql 299
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE---LEKEIAELRAELEAQKEELAELLR------ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 300 AVLKVRLQEADQVLSSRTEALEALRSekSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNK 379
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 7305095 380 MEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKA 433
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
232-568 |
1.90e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 232 LRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQ------------- 298
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaekqrrdlge 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 299 -LAVLKVRLQE------ADQVLSSR-----TEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEAdatlKREQESY 366
Cdd:pfam01576 300 eLEALKTELEDtldttaAQQELRSKreqevTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQA----KRNKANL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 367 KQMQSEFAARLNKMEVDRQNLAEAVTLAERKyseeKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINS 446
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHK----RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 447 LKEGSSFEGLESSTASSM--ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRT 524
Cdd:pfam01576 452 AEGKNIKLSKDVSSLESQlqDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 7305095 525 SKQELETELERMKQEFRYMEEDLhrtkNTLQSRIKDREEEIQKL 568
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQREL----EALTQQLEEKAAAYDKL 571
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
230-606 |
3.01e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 53.70 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 230 QLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKwnvdnsksdrITRELRAQVDDLTEAVAAKDSQLAVLKVRLQ-- 307
Cdd:pfam06160 96 DDIEEDIKQILEELDELLESEEKNREEVEELKDKYRE----------LRKTLLANRFSYGPAIDELEKQLAEIEEEFSqf 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 308 ----------EADQVLSSRTEALEALRSEKSRIMQDHKEgssLQNqalqTLQERLHEADATLKR-EQESYKQMQSEFAAR 376
Cdd:pfam06160 166 eeltesgdylEAREVLEKLEEETDALEELMEDIPPLYEE---LKT----ELPDQLEELKEGYREmEEEGYALEHLNVDKE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 377 LNKMEVDRQNLAEA-----VTLAERKYSEEKKKVDELQQQV---KLHRASLESAKQELVDYKQKATRILQSKEKLINSLK 448
Cdd:pfam06160 239 IQQLEEQLEENLALlenleLDEAEEALEEIEERIDQLYDLLekeVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 449 EgsSFEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDmeaqqvsEAESAREQLQDLQDQIAKQRTSKQE 528
Cdd:pfam06160 319 Q--SYTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQE-------ELEEILEQLEEIEEEQEEFKESLQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 529 LETELERMKQEFRYMEEDLHRTK------------NTLQSRIKDREEEIQKLRNQLTNKTL--------SNSSQSELEsR 588
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREIKrlveksnlpglpESYLDYFFDVSDEIEDLADELNEVPLnmdevnrlLDEAQDDVD-T 468
|
410
....*....|....*...
gi 7305095 589 LHQLTETLIQKQTMLESL 606
Cdd:pfam06160 469 LYEKTEELIDNATLAEQL 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
206-428 |
3.04e-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: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 206 EEHSSTPSDGSSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQV 285
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 286 DDLTEAVAAKDSQLAVLKVRLQEadqvlssrteaLEALRSEKSRIMqdhkegsSLQNQALQTLQERLHEADATLKREQES 365
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEE-----------LEAQIEKKRKRL-------SELKAKLEALEEELSEIEDPKGEDEEI 946
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7305095 366 YKQMQSE--FAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQvklhRASLESAKQELVD 428
Cdd:TIGR02169 947 PEEELSLedVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK----RAKLEEERKAILE 1007
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
397-629 |
3.79e-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: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 397 KYSEEKKKVDELQQQVKLHRaslesaKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLESStASSMELEELRHE-KEM 475
Cdd:TIGR02169 212 RYQALLKEKREYEGYELLKE------KEALERQKEAIERQLASLEEELEKLTEEISELEKRLE-EIEQLLEELNKKiKDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 476 QKEEIQKLMGQMHQLRSE---LQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEfrymeedlhrtKN 552
Cdd:TIGR02169 285 GEEEQLRVKEKIGELEAEiasLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR-----------RD 353
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305095 553 TLQSRIKDREEEIQKLRNQLtnktlsnssqSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHSASS 629
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAEL----------EEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
347-551 |
4.16e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 347 TLQERLHE--ADATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAvTLAERKYSEEKKKVDELQQQVKLHRASLESAKQ 424
Cdd:COG4717 38 TLLAFIRAmlLERLEKEADELFKPQGRKPELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 425 EL--VDYKQKATRILQSKEKLINSLKEGSsfEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQV 502
Cdd:COG4717 117 ELekLEKLLQLLPLYQELEALEAELAELP--ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 7305095 503 SEAesaREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTK 551
Cdd:COG4717 195 QDL---AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
465-629 |
4.70e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQvSEAESAREQLQDLQdQIAKQRTSKQELETELERMKQEFRYME 544
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAEL-EELREELEKLEKLL-QLLPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 545 EDLHRTKNtLQSRIKDREEEIQKLRNQLTnkTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQV 624
Cdd:COG4717 153 ERLEELRE-LEEELEELEAELAELQEELE--ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
....*
gi 7305095 625 HSASS 629
Cdd:COG4717 230 EQLEN 234
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-517 |
6.67e-07 |
|
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: 52.81 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 182 NSSDSVPEVHKEPSEESTAPSATSEEHSSTPSDGSSRSQELSNLRLENQLLRN---EVQSLNQEMA-------------- 244
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtECEALKLQMAekdkvieilrqqie 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 245 --------------SLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDL----TEAVAAKDSQLAVLKVRL 306
Cdd:pfam15921 573 nmtqlvgqhgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLelekVKLVNAGSERLRAVKDIK 652
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 307 QEADQVL----SSRTEaLEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEfaarlnkmev 382
Cdd:pfam15921 653 QERDQLLnevkTSRNE-LNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGS---------- 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 383 DRQNLAEAVTLaERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQskeKLINSLKEGSSFEGlesstas 462
Cdd:pfam15921 722 DGHAMKVAMGM-QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ---ELSTVATEKNKMAG------- 790
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 7305095 463 smELEELRHEKEMQKEEIQKLmgQMHQLRSELQDMEAQ---QVSEAESAREQLQDLQD 517
Cdd:pfam15921 791 --ELEVLRSQERRLKEKVANM--EVALDKASLQFAECQdiiQRQEQESVRLKLQHTLD 844
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
216-568 |
7.48e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 216 SSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKwnvDNSKSDRITRELRAQVDDLTEAVAAK 295
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE---LEEEEEEEEEALEEAAEEEAELEEEE 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 296 DSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRI-----MQDHKEGSS------------------------------- 339
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLlllleAEADYEGFLegvkaalllaglrglagavavligveaayea 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 340 -LQNQALQTLQERLHEADATLKREQESYKQMQSEFAARL--NKMEVDR---QNLAEAVTLAERKYSEEKKKVDELQQQVK 413
Cdd:COG1196 539 aLEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLplDKIRARAalaAALARGAIGAAVDLVASDLREADARYYVL 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 414 LHRASLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSE 493
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEA 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 494 LQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTK------NTLQSRIKDREEEIQK 567
Cdd:COG1196 699 LLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELpeppdlEELERELERLEREIEA 778
|
.
gi 7305095 568 L 568
Cdd:COG1196 779 L 779
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
397-582 |
9.94e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.94 E-value: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 397 KYSEEKKK-----VDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEELRH 471
Cdd:PHA02562 202 KNIEEQRKkngenIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMY 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 472 EK-----------EMQKEEIQKLMGQMHQLrselqdmeAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEF 540
Cdd:PHA02562 282 EKggvcptctqqiSEGPDRITKIKDKLKEL--------QHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSL 353
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 7305095 541 RYMEEDLHRTK---NTLQSRIKDREEEIQKLRNQL--TNKTLSNSSQ 582
Cdd:PHA02562 354 ITLVDKAKKVKaaiEELQAEFVDNAEELAKLQDELdkIVKTKSELVK 400
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
465-623 |
1.02e-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: 51.69 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEaQQVSEAE----SAREQLQDLQDQIAKQRTSKQELETELERMKQEF 540
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALE-RRIAALArrirALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 541 RYMEEDLHRTKNT---------------------LQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQK 599
Cdd:COG4942 107 AELLRALYRLGRQpplalllspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180
....*....|....*....|....
gi 7305095 600 QTMLESLSTEKNSLVFQLERLEQQ 623
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAE 210
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
374-641 |
1.37e-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: 51.30 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 374 AARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKatriLQSKEKLINSLKEgssf 453
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE----LAALEAELAELEK---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 454 eglesstassmELEELRHEKEMQKEEIQKLMGQMHQLRSELQDM---EAQQVSEAESAREQLQDLQDQIAKQRTSKQELE 530
Cdd:COG4942 91 -----------EIAELRAELEAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 531 TELERMKQEfrymeedLHRTKNTLQSRIKDREEEIQKLRNQltnktlsnssQSELESRLHQLTETLIQKQTMLESLSTEK 610
Cdd:COG4942 160 AELAALRAE-------LEAERAELEALLAELEEERAALEAL----------KAERQKLLARLEKELAELAAELAELQQEA 222
|
250 260 270
....*....|....*....|....*....|.
gi 7305095 611 NSLVFQLERLEQQVHSASSGPNSGSAINMSG 641
Cdd:COG4942 223 EELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
219-623 |
1.37e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 219 SQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVE-KWNVDNSKSDRITRELRAQVDDlteavaaKDS 297
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEIND-------KEK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 298 QLAVLKVRLQEADQVLSSRTEALEALRSEKSRImqdhKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARL 377
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDLTFLLEESRDKANQL----EEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 378 NKMEVDRQNLAEaVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSlkegssfeGLE 457
Cdd:pfam05483 317 EDLQIATKTICQ-LTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITM--------ELQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 458 SSTASSMELEELRHEKEMQKEEIQKLMG----------QMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQ 527
Cdd:pfam05483 388 KKSSELEEMTKFKNNKEVELEELKKILAedeklldekkQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 528 ELETELERMKQEF---RYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLe 604
Cdd:pfam05483 468 HYLKEVEDLKTELekeKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNL- 546
|
410
....*....|....*....
gi 7305095 605 slsteKNSLVFQLERLEQQ 623
Cdd:pfam05483 547 -----RDELESVREEFIQK 560
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
230-610 |
1.39e-06 |
|
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: 51.43 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 230 QLLRNEVQSLNQEMASLLQRSKETQEELNKARvrvEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEA 309
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEK---ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 310 DQVLSSRTEALEALRSEKS----RIMQDHKEGSSLQNQA------LQTLQERLHEADATLKREQESYKQMQSEfaarLNK 379
Cdd:pfam07888 107 SASSEELSEEKDALLAQRAaheaRIRELEEDIKTLTQRVlereteLERMKERAKKAGAQRKEEEAERKQLQAK----LQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 380 MEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKegsSFEGLESS 459
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASER---KVEGLGEE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 460 TASSMELEElRHEKEMQKEEIQ--KLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMK 537
Cdd:pfam07888 260 LSSMAAQRD-RTQAELHQARLQaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER 338
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7305095 538 QEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLtnkTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEK 610
Cdd:pfam07888 339 MEREKLEVELGREKDCNRVQLSESRRELQELKASL---RVAQKEKEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
343-565 |
1.54e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 343 QALQTLQERLhEADATLKREQESYKQMQSEfAARLNKME--VDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLE 420
Cdd:COG4913 242 EALEDAREQI-ELLEPIRELAERYAAARER-LAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 421 SAKQELVDYKQkatRILQSKEKLINSLKEgssfeglesstassmELEELRHEKEMQKEEIQKLMGQMHQL-------RSE 493
Cdd:COG4913 320 ALREELDELEA---QIRGNGGDRLEQLER---------------EIERLERELEERERRRARLEALLAALglplpasAEE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 494 LQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYME-------EDLHRTKNTLQSRIKDREEEI 565
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLErrksnipARLLALRDALAEALGLDEAEL 460
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
221-619 |
2.29e-06 |
|
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: 51.17 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLA 300
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 301 VLKvrlQEADQVLSSRTealealrseKSRIMQDHKEGSSLQNQALQTLQ--ERLHEADATLKREQESykqmqsefaARLN 378
Cdd:TIGR04523 299 DLN---NQKEQDWNKEL---------KSELKNQEKKLEEIQNQISQNNKiiSQLNEQISQLKKELTN---------SESE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 379 KMEVDRQnLAEAVTLAERKYSEEKKKVDELQQqvklhrasLESAKQELVDYKQKATRILQSKEKLINSLKegSSFEGLES 458
Cdd:TIGR04523 358 NSEKQRE-LEEKQNEIEKLKKENQSYKQEIKN--------LESQINDLESKIQNQEKLNQQKDEQIKKLQ--QEKELLEK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 459 stassmELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEaqqvSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQ 538
Cdd:TIGR04523 427 ------EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD----NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 539 EFrymeedlhrtkNTLQSRIKDREEEIQKLrnqltnktlsNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLE 618
Cdd:TIGR04523 497 EL-----------KKLNEEKKELEEKVKDL----------TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
.
gi 7305095 619 R 619
Cdd:TIGR04523 556 K 556
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
374-541 |
2.36e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 374 AARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRAsLESAKQELVDYKQKATRIlQSKEKLINSLKEGSS- 452
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSWDEIDVASAEREI-AELEAELERLDASSDd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 453 FEGLESstassmELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQ----------------------------QVSE 504
Cdd:COG4913 687 LAALEE------QLEELEAELEELEEELDELKGEIGRLEKELEQAEEEldelqdrleaaedlarlelralleerfaAALG 760
|
170 180 190
....*....|....*....|....*....|....*..
gi 7305095 505 AESAREQLQDLQDQIAKQRTSKQELETELERMKQEFR 541
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
375-539 |
2.87e-06 |
|
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: 49.15 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 375 ARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELvdyKQKATRILQSKEKL--INSLKEgss 452
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI---EEVEARIKKYEEQLgnVRNNKE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 453 FEGLESstassmELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETE 532
Cdd:COG1579 91 YEALQK------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
....*..
gi 7305095 533 LERMKQE 539
Cdd:COG1579 165 REELAAK 171
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
218-625 |
2.90e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.60 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 218 RSQELSNLRLENQLlrNEVQSLNqeMASllqrskETQEELnkarvrvEKWNvdnSKSDRITRELRAQVDDLTEAVAAKDS 297
Cdd:PRK04778 37 RKQELENLPVNDEL--EKVKKLN--LTG------QSEEKF-------EEWR---QKWDEIVTNSLPDIEEQLFEAEELND 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 298 QLAVLKVR--LQEADQVLSSRTEALEALRSEKSRIMQDHKEGSslqnQALQTLQERLHEADATLKREQESYKQMQSEFAA 375
Cdd:PRK04778 97 KFRFRKAKheINEIESLLDLIEEDIEQILEELQELLESEEKNR----EEVEQLKDLYRELRKSLLANRFSFGPALDELEK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 376 RLNKMEvdrQNLAEAVTLAERKYSEEKKKVdelqqqvklhrasLESAKQELVDYKQKATRILQSKEKLINSLKEgssfeg 455
Cdd:PRK04778 173 QLENLE---EEFSQFVELTESGDYVEAREI-------------LDQLEEELAALEQIMEEIPELLKELQTELPD------ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 456 lesstassmELEELRH-EKEMQKE----EIQKLMGQMHQLRSELQDMEAQQVS-EAESAREQLQDLQDQI---------- 519
Cdd:PRK04778 231 ---------QLQELKAgYRELVEEgyhlDHLDIEKEIQDLKEQIDENLALLEElDLDEAEEKNEEIQERIdqlydilere 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 520 ------------------AKQRTSKQELETELERMKQEFRYMEEDLHRTKNtLQSRIKDREEEIQKLRNQLTNKTLSNSS 581
Cdd:PRK04778 302 vkarkyveknsdtlpdflEHAKEQNKELKEEIDRVKQSYTLNESELESVRQ-LEKQLESLEKQYDEITERIAEQEIAYSE 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 7305095 582 -QSELESRLHQLTEtlIQKQ-----TMLESLSTEKNSLVFQLERLEQQVH 625
Cdd:PRK04778 381 lQEELEEILKQLEE--IEKEqeklsEMLQGLRKDELEAREKLERYRNKLH 428
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
220-411 |
2.93e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 220 QELSNLRLENQLLrnevqSLNQEMASLLQRSKETQEELNKARVRVEKwnvDNSKSDRITRELRAQVDDLTE-----AVAA 294
Cdd:COG3206 196 AALEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAE---AEARLAALRAQLGSGPDALPEllqspVIQQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 295 KDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMqsefA 374
Cdd:COG3206 268 LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR----L 343
|
170 180 190
....*....|....*....|....*....|....*..
gi 7305095 375 ARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQ 411
Cdd:COG3206 344 AELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
312-613 |
3.01e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 312 VLSSRTEALEALRSEKSRimqdhKEGSSLqNQALQTLQERLHEADATLKREQEsykqmQSEFAarlnkmevdRQNLAEAV 391
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEE-----KEEKDL-HERLNGLESELAELDEEIERYEE-----QREQA---------RETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 392 TLAERkYSEEKKKVDELQQQVKLHRASL---ESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSmELEE 468
Cdd:PRK02224 241 EVLEE-HEERREELETLEAEIEDLRETIaetEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEA-RREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 469 LRHEKEMQKEEIQklmgqmhQLRSELQDMEaqqvSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRymeedlh 548
Cdd:PRK02224 319 LEDRDEELRDRLE-------ECRVAAQAHN----EEAESLREDADDLEERAEELREEAAELESELEEAREAVE------- 380
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 549 rtknTLQSRIKDREEEIQKLRNQLTNktlSNSSQSELESRLHQLTET---LIQKQTMLE-SLSTEKNSL 613
Cdd:PRK02224 381 ----DRREEIEELEEEIEELRERFGD---APVDLGNAEDFLEELREErdeLREREAELEaTLRTARERV 442
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
277-527 |
3.45e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 277 ITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQvlssrteALEALRsEKSRIMqDHKEGSSLQNQALQTLQERLHEAD 356
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEA-------ALEEFR-QKNGLV-DLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 357 ATLKREQESYKQMQSEFAARLNKMEVDRQN-----LAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELvdyKQ 431
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSpviqqLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 432 KATRILQSKEKLINSLKEgssfeglesstassmELEELRHEKEMQKEEIQklmgQMHQLRSELQDMEAqqvsEAESAREQ 511
Cdd:COG3206 310 EAQRILASLEAELEALQA---------------REASLQAQLAQLEARLA----ELPELEAELRRLER----EVEVAREL 366
|
250
....*....|....*.
gi 7305095 512 LQDLQDQIAKQRTSKQ 527
Cdd:COG3206 367 YESLLQRLEEARLAEA 382
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
227-574 |
4.36e-06 |
|
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: 50.02 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 227 LENQL--LRNEVQSLNQEMASLLqrSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKV 304
Cdd:TIGR04523 286 LEKQLnqLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 305 RLQEADQVL-------SSRTEALEALRSEKSRI---MQDHKEGSSLQNQALQTLQ----------ERLHEADATLKREQE 364
Cdd:TIGR04523 364 ELEEKQNEIeklkkenQSYKQEIKNLESQINDLeskIQNQEKLNQQKDEQIKKLQqekellekeiERLKETIIKNNSEIK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 365 SYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAK-------QELVDYKQKATRIL 437
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNeekkeleEKVKDLTKKISSLK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 438 QSKEKLINSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQD 517
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 518 QIAKQRTSKQELETELERMKQEFRYMEE---DLHRTKNTLQSRIKDREEEIQKLRNQLTN 574
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSiikNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-629 |
4.45e-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: 50.44 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 219 SQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQ 298
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 299 LAVLKVRLQEADQVLSSRTEALEALRSEKSRI-MQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARL 377
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 378 NKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLH----------------RASLESAKQELVDYKqkATRILQSKE 441
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgilgvlselisvdegyEAAIEAALGGRLQAV--VVENLNAAK 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 442 KLINSLKEGSSFEG--LESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDM---------------EAQQVSE 504
Cdd:TIGR02168 560 KAIAFLKQNELGRVtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvddldNALELAK 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 505 AESAREQLQDLQDQI-----------AKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLT 573
Cdd:TIGR02168 640 KLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRK 719
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 7305095 574 NKTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHSASS 629
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
279-626 |
8.69e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.91 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 279 RELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNqalqTLQERLHEADAT 358
Cdd:pfam19220 23 RSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELE----ELVARLAKLEAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 359 LKREQESYKQMQSEFAARLNKME-VDRQNLAEAvtlAERKYSEEkkKVDELQQQVKLHRASLESAKQELVDYKQKATRIL 437
Cdd:pfam19220 99 LREAEAAKEELRIELRDKTAQAEaLERQLAAET---EQNRALEE--ENKALREEAQAAEKALQRAEGELATARERLALLE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 438 QSKEKLiNSLKEGSSFEgLESSTASSMELEELRhekEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAE-------SARE 510
Cdd:pfam19220 174 QENRRL-QALSEEQAAE-LAELTRRLAELETQL---DATRARLRALEGQLAAEQAERERAEAQLEEAVEahraeraSLRM 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 511 QLQDLQDQIAKQRTSKQELETELERMKQEFRYME---EDLHRTKNTLQSRIKDREEEIQKLRNQLTNktlSNSSQSELES 587
Cdd:pfam19220 249 KLEALTARAAATEQLLAEARNQLRDRDEAIRAAErrlKEASIERDTLERRLAGLEADLERRTQQFQE---MQRARAELEE 325
|
330 340 350
....*....|....*....|....*....|....*....
gi 7305095 588 RLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHS 626
Cdd:pfam19220 326 RAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEV 364
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
306-623 |
9.88e-06 |
|
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: 49.20 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 306 LQEADQVLSSRTEaLEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEvdRQ 385
Cdd:TIGR00618 183 LMEFAKKKSLHGK-AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK--KQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 386 NLAEAVTLAERKYSEEKKKVDELQQQVKL--HRASLESAKQELVDYKQKATRILQSKEKLINSLKegSSFEGLESSTASS 463
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRarKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRA--KLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 464 MELEELRH-EKEMQKEEIqkLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETE------LERM 536
Cdd:TIGR00618 338 SSIEEQRRlLQTLHSQEI--HIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILqreqatIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 537 KQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQ 616
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLAR 495
|
....*..
gi 7305095 617 LERLEQQ 623
Cdd:TIGR00618 496 LLELQEE 502
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
178-422 |
1.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 178 SPGVNSSDSVPEVHKEPSEESTAPSATSEEHSSTPSDGSSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEEL 257
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 258 NKARVRVEKwnvdnsKSDRITRELRA-----QVDDLTEAVAAKDSQLAVlkVRLQEADQVLSSRTEALEALRSEKSRIMQ 332
Cdd:COG4942 93 AELRAELEA------QKEELAELLRAlyrlgRQPPLALLLSPEDFLDAV--RRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 333 dhkegsslQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQV 412
Cdd:COG4942 165 --------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|
gi 7305095 413 KLHRASLESA 422
Cdd:COG4942 237 AAAAERTPAA 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
219-629 |
1.08e-05 |
|
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: 49.20 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 219 SQELSNLRLENQLLRNEVQSLNQEMASLLQR---------SKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLT 289
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKraahvkqqsSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 290 EAVAAKDSQLAVLKVRLQEADQVLSSRTE--ALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYK 367
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQReqATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 368 QMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDY------KQKATRILQSKE 441
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgplTRRMQRGEQTYA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 442 KLINSLK--EGSSFEGLESSTASSMELEELRHEKEMQ-------KEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQL 512
Cdd:TIGR00618 539 QLETSEEdvYHQLTSERKQRASLKEQMQEIQQSFSILtqcdnrsKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 513 QDLQDQIAKQRTSKqeletELERMKQEFRYMEEDLHRTKNTL---QSRIKDREEEIQKLRNQLTNKTLSNSSQSELESrL 589
Cdd:TIGR00618 619 RKLQPEQDLQDVRL-----HLQQCSQELALKLTALHALQLTLtqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQ-L 692
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 7305095 590 HQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHSASS 629
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGS 732
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
205-467 |
1.30e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 205 SEEHSSTPSDGSSRSQELSNLRLENQLLRNEVQSLNQEMASLlqrsKETQEELnkarVRVEKwnvDNSKSDRITRELRAQ 284
Cdd:PLN02939 211 LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEV----AETEERV----FKLEK---ERSLLDASLRELESK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 285 VDDLTEAVaakdSQLAVLKVrlqeadQVLSSRTEALEALrseksrimqdhkegsslqnqaLQTLQERLHEADATLKREQe 364
Cdd:PLN02939 280 FIVAQEDV----SKLSPLQY------DCWWEKVENLQDL---------------------LDRATNQVEKAALVLDQNQ- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 365 sykqmqsEFAARLNKMEvdrQNLAEAVTlaerkYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLI 444
Cdd:PLN02939 328 -------DLRDKVDKLE---ASLKEANV-----SKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTL 392
|
250 260
....*....|....*....|...
gi 7305095 445 NSLKEGSSFEGLESStASSMELE 467
Cdd:PLN02939 393 SKLKEESKKRSLEHP-ADDMPSE 414
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
235-629 |
1.58e-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: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 235 EVQSLNQEMASLLQRSKETQEEL-NKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVL 313
Cdd:pfam15921 121 EMQMERDAMADIRRRESQSQEDLrNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEAS 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 314 SSR--------TEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHeadaTLKREQES-----YKQMQSEFAARLNKM 380
Cdd:pfam15921 201 GKKiyehdsmsTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLE----ALKSESQNkiellLQQHQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 381 EVDRQNLAEAVTLAERKYSEEKKKVDELQQQVK-------LHRASLESAKQELVDYKQKATRILQSKeklinslkegssF 453
Cdd:pfam15921 277 EVEITGLTEKASSARSQANSIQSQLEIIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYEDK------------I 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 454 EGLESSTA-SSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEaesaREQLQDLQDQIAKQRTSKQELETE 532
Cdd:pfam15921 345 EELEKQLVlANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE----KEQNKRLWDRDTGNSITIDHLRRE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 533 LERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKlRNQLTNKTLSNSSQSE-LESRLHQLTETLIQKQTMLESLSTEKN 611
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQG-KNESLEKVSSLTAQLEsTKEMLRKVVEELTAKKMTLESSERTVS 499
|
410
....*....|....*...
gi 7305095 612 SLVFQLERLEQQVHSASS 629
Cdd:pfam15921 500 DLTASLQEKERAIEATNA 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
403-571 |
1.76e-05 |
|
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: 46.84 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 403 KKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLinslkegssfeglesstasSMELEELRHEKEMQKEEIQK 482
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-------------------EKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 483 LMGQMHQLRS--ELQDMEaqqvSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKD 560
Cdd:COG1579 78 YEEQLGNVRNnkEYEALQ----KEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|.
gi 7305095 561 REEEIQKLRNQ 571
Cdd:COG1579 154 LEAELEELEAE 164
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
395-600 |
2.00e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 395 ERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKatrilqskEKLIN-SLKEGSSFEGLESSTASSMELEELRHEK 473
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK--------NGLVDlSEEAKLLLQQLSELESQLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 474 EMQKEEIQKLMGQMH-------------QLRSELQDMEAQQVSEAE----------SAREQLQDLQDQIAKQ-RTSKQEL 529
Cdd:COG3206 239 EARLAALRAQLGSGPdalpellqspviqQLRAQLAELEAELAELSArytpnhpdviALRAQIAALRAQLQQEaQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7305095 530 ETELERMKQEFRYMEEDLHRTKNTLQsRIKDREEEIQKLRNQLTNKtlsnssQSELESRLHQLTETLIQKQ 600
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLA-ELPELEAELRRLEREVEVA------RELYESLLQRLEEARLAEA 382
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
237-447 |
2.27e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 237 QSLNQEMASLLQRSKETQEELNKARVRVEKW--NVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLS 314
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAeaALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 315 SRTEALEALRSEKSRIMQDhKEGSSLQNQaLQTLQERLHEADATLKREQESYKQMQSEFAARLNKMevdRQNLAEAVTLA 394
Cdd:COG3206 244 ALRAQLGSGPDALPELLQS-PVIQQLRAQ-LAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASL 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 7305095 395 ERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQkATRILQSKEKLINSL 447
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVARELYESL 370
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
463-631 |
2.32e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.70 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 463 SMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIA--------------KQRTSKQE 528
Cdd:PHA02562 187 DMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLnlvmdiedpsaalnKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 529 LETELERMKQEFRYMEEdlHRTKNTLQSRIKDREEEIQKLRNQLTNKTLS----NSSQSELESRLHQLTETLIQKQTMLE 604
Cdd:PHA02562 267 IKSKIEQFQKVIKMYEK--GGVCPTCTQQISEGPDRITKIKDKLKELQHSleklDTAIDELEEIMDEFNEQSKKLLELKN 344
|
170 180 190
....*....|....*....|....*....|
gi 7305095 605 SLSTEKNSL---VFQLERLEQQVHSASSGP 631
Cdd:PHA02562 345 KISTNKQSLitlVDKAKKVKAAIEELQAEF 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
345-621 |
2.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 345 LQTLQERLHEADATLKRE---QESYKQMQSEFAA---RLNKMEVDRQNLAEAVTLAERKYsEEKKKVDELQQQVKLHRAS 418
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTeniEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEV-KELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 419 LESAKQEL-VDYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQdm 497
Cdd:PRK03918 250 LEGSKRKLeEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE-- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 498 eaQQVSEAESAREQLQDLQDQiakqrtsKQELETELERMKQEFRYMEEdlhrtkntlqsrIKDREEEIQKLRNQLTNKTL 577
Cdd:PRK03918 328 --ERIKELEEKEERLEELKKK-------LKELEKRLEELEERHELYEE------------AKAKKEELERLKKRLTGLTP 386
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 7305095 578 S--NSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLE 621
Cdd:PRK03918 387 EklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
402-606 |
2.67e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 402 KKKVDELQQQvklhRASLESAKQELVDYKQKATRILQSKEKLINSLkegssfEGLESSTASSMELEELRhekemqkEEIQ 481
Cdd:COG4913 609 RAKLAALEAE----LAELEEELAEAEERLEALEAELDALQERREAL------QRLAEYSWDEIDVASAE-------REIA 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 482 KLMGQMHQLRSELQDMEAQQvSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSrikDR 561
Cdd:COG4913 672 ELEAELERLDASSDDLAALE-EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL---EL 747
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 7305095 562 EEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLESL 606
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
290-591 |
3.22e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.48 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 290 EAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQA----------LQTLQERLHEADATL 359
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAeemrarlaarKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 360 KREQESYKQMQSEfaarlnkmevdRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQS 439
Cdd:pfam01576 85 EEEEERSQQLQNE-----------KKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 440 KEKLINSLKEGSSFEGLESSTASSmeLEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQI 519
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEEEKAKS--LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 520 AKQRTS----KQELETELERMKQE-----------------FRYMEEDLHRTK---NTLQSRIKDREEEIQKLRNQLTNK 575
Cdd:pfam01576 232 AELRAQlakkEEELQAALARLEEEtaqknnalkkireleaqISELQEDLESERaarNKAEKQRRDLGEELEALKTELEDT 311
|
330
....*....|....*.
gi 7305095 576 TLSNSSQSELESRLHQ 591
Cdd:pfam01576 312 LDTTAAQQELRSKREQ 327
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
311-650 |
3.59e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 311 QVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEVDRQNLAEA 390
Cdd:pfam02463 198 QELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 391 -----VTLAERKYSEEKKKVDELQqqvklhRASLESAKQELVDYKQKATRILQSKEKLINSLKegssfeglESSTASSME 465
Cdd:pfam02463 278 ekekkLQEEELKLLAKEEEELKSE------LLKLERRKVDDEEKLKESEKEKKKAEKELKKEK--------EEIEELEKE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 466 LEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEfrymEE 545
Cdd:pfam02463 344 LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQL----ED 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 546 DLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLhQLTETLIQKQTMLESLSTEKNSLVFQLER-LEQQV 624
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD-ELELKKSEDLLKETQLVKLQEQLELLLSRqKLEER 498
|
330 340
....*....|....*....|....*.
gi 7305095 625 HSASSGPNSGSAINMSGVDSGEGTRL 650
Cdd:pfam02463 499 SQKESKARSGLKVLLALIKDGVGGRI 524
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
217-576 |
3.63e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.41 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 217 SRSQELSNLRLENQLLRNEVQSLNQEMASL--LQRSKETQ-EELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVA 293
Cdd:pfam05483 367 TEQQRLEKNEDQLKIITMELQKKSSELEEMtkFKNNKEVElEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 294 AKDSQLAVLKVRLQEADQVLSSRTEALEALRSE------KSRIMQDHKEGSSLQNQAL---------------------- 345
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTElekeklKNIELTAHCDKLLLENKELtqeasdmtlelkkhqediinck 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 346 ----------QTLQERLHEADATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLH 415
Cdd:pfam05483 527 kqeermlkqiENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 416 RASLESAKQELVDYKQKAT---RILQSKEKLINSLK-----EGSSFEGLESSTASSMELEELRHEKEMQK-EEIQKLMGQ 486
Cdd:pfam05483 607 NKNIEELHQENKALKKKGSaenKQLNAYEIKVNKLElelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEvEKAKAIADE 686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 487 MHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRY-MEEDLHRTKNTLQSRIKDRE--- 562
Cdd:pfam05483 687 AVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAaLEIELSNIKAELLSLKKQLEiek 766
|
410
....*....|....
gi 7305095 563 EEIQKLRNQLTNKT 576
Cdd:pfam05483 767 EEKEKLKMEAKENT 780
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
237-515 |
3.64e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 237 QSLNQEMASLLQRSKETQEELNKARvrvekwnvdNSKSDRITRE--LRAQVDDLTEA--VAAKDSQLAVLKVRLQEADQV 312
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELR---------ADEAERARELdlLRFQLEELEAAalQPGEEEELEEERRRLSNAEKL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 313 LSSRTEALEALRSEksrimqdhkEGSSLQ--NQALQTLqERLHEADATLK----REQESYKQMQ---SEFAARLNKMEVD 383
Cdd:COG0497 225 REALQEALEALSGG---------EGGALDllGQALRAL-ERLAEYDPSLAelaeRLESALIELEeaaSELRRYLDSLEFD 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 384 RQNLAEavtLAERkyseekkkVDELQQQVKLHRASLEsakqELVDYKQKAtrilqsKEKLinslkegssfEGLESSTAss 463
Cdd:COG0497 295 PERLEE---VEER--------LALLRRLARKYGVTVE----ELLAYAEEL------RAEL----------AELENSDE-- 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 7305095 464 mELEELRHEKEMQKEEIQKLMGQMHQLRSELqdmeAQQVSEAesAREQLQDL 515
Cdd:COG0497 342 -RLEELEAELAEAEAELLEAAEKLSAARKKA----AKKLEKA--VTAELADL 386
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
504-607 |
3.94e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 504 EAES-AREQLQDLQDQIAKQRtskQELETELERMKQEFRYMEEDLHRTKNTL---QSRIKDREEEIQKLRNQLTNKtlsn 579
Cdd:PRK12704 50 EAEAiKKEALLEAKEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEENLdrkLELLEKREEELEKKEKELEQK---- 122
|
90 100
....*....|....*....|....*...
gi 7305095 580 ssQSELESRLHQLTETLIQKQTMLESLS 607
Cdd:PRK12704 123 --QQELEKKEEELEELIEEQLQELERIS 148
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
400-624 |
4.76e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 400 EEKKKVDELQQQvklhraslesAKQELVDYKQKATRILQSKEKLInslkegssfEGLESSTASSMELEELRHEKEMQKEE 479
Cdd:pfam01576 12 EELQKVKERQQK----------AESELKELEKKHQQLCEEKNALQ---------EQLQAETELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 480 IQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEED----------LHR 549
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDillledqnskLSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 550 TKNTLQSRIKD------REEEIQKLRNQLTNKtlSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 623
Cdd:pfam01576 153 ERKLLEERISEftsnlaEEEEKAKSLSKLKNK--HEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
.
gi 7305095 624 V 624
Cdd:pfam01576 231 I 231
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
235-632 |
4.85e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 46.64 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 235 EVQSLNQEMASLLQRSKETQEELN-KARVRVEKWNVDNSKSDRITRELraqvDDLTEAVAAKDSQLAVLKVRLQEADQVL 313
Cdd:pfam05483 251 EKENKMKDLTFLLEESRDKANQLEeKTKLQDENLKELIEKKDHLTKEL----EDIKMSLQRSMSTQKALEEDLQIATKTI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 314 SSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEvdrqnlaEAVTL 393
Cdd:pfam05483 327 CQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELE-------EMTKF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 394 AERKYSE--EKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLkEGSSFEGLESSTASSMELEELRH 471
Cdd:pfam05483 400 KNNKEVEleELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL-EIQLTAIKTSEEHYLKEVEDLKT 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 472 EKEMQKEEIQKLMGQMHQLRSELQDMeaqqVSEAESAREQLQDLQDQIAKQRtsKQEletelERMKQEFRYMEEDLHRTK 551
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKEL----TQEASDMTLELKKHQEDIINCK--KQE-----ERMLKQIENLEEKEMNLR 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 552 NTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHSASSGP 631
Cdd:pfam05483 548 DELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAE 627
|
.
gi 7305095 632 N 632
Cdd:pfam05483 628 N 628
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
231-442 |
5.03e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 231 LLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEAD 310
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 311 QVLSSRTEALEALRSEKSRIM-----------------QDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEF 373
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 374 AARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEK 442
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
228-598 |
6.15e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 228 ENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRIT------RELRAQVDDLT-------EAVAA 294
Cdd:PRK11281 67 QTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTLdqlqnaqNDLAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 295 KDSQLAVLK--------------VRLQEADQVLSSRTEALEALRSekSRIMQDHKEGSSLQnqALQTLQERLHEADATLk 360
Cdd:PRK11281 147 YNSQLVSLQtqperaqaalyansQRLQQIRNLLKGGKVGGKALRP--SQRVLLQAEQALLN--AQNDLQRKSLEGNTQL- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 361 reQESYKQMQSEFAARLNKMEVDRQNLAEAVTlaERKYSEEKKKVDELQQQVKLHRASLES-AKQELVDYKQKATRILQS 439
Cdd:PRK11281 222 --QDLLQKQRDYLTARIQRLEHQLQLLQEAIN--SKRLTLSEKTVQEAQSQDEAARIQANPlVAQELEINLQLSQRLLKA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 440 KEKLiNSLKEGS--SFEGLESSTASSMELEE----LRHE--------KEMQK----EEIQKLMGQMHQLRSELQDMEAQq 501
Cdd:PRK11281 298 TEKL-NTLTQQNlrVKNWLDRLTQSERNIKEqisvLKGSlllsrilyQQQQAlpsaDLIEGLADRIADLRLEQFEINQQ- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 502 vseaesaREQLQDLQDQIAK-QRTSKQELETELermkqefrymeedlhrtKNTLQSRIKDREEEIQKLRNQLTNK-TLSN 579
Cdd:PRK11281 376 -------RDALFQPDAYIDKlEAGHKSEVTDEV-----------------RDALLQLLDERRELLDQLNKQLNNQlNLAI 431
|
410 420
....*....|....*....|..
gi 7305095 580 S---SQSELESRLHQLTETLIQ 598
Cdd:PRK11281 432 NlqlNQQQLLSVSDSLQSTLTQ 453
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
457-627 |
6.70e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 457 ESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQvseaESAREQLQDLQDQIAKQRTSKQELETELERM 536
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKR----DELNAQVKELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 537 KQEfrymeedlhrtKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLiqkQTmlESLSTEK-NSLVF 615
Cdd:COG1340 77 KEE-----------RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ---QT--EVLSPEEeKELVE 140
|
170
....*....|..
gi 7305095 616 QLERLEQQVHSA 627
Cdd:COG1340 141 KIKELEKELEKA 152
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
301-532 |
6.74e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 301 VLKVRLQEADQVLSSRTEALEALRsEKSRIMQDH-KEGSSLQNQALQTLQERLHEadatLKREQESYKQMQSEFAARLNK 379
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQ-QQIKTYNKNiEEQRKKNGENIARKQNKYDE----LVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 380 MEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHR---------ASLESAKQELVDYKQKATRILQSKEKLINSLKEG 450
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 451 SsfEGLESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAesarEQLQDLQDQIAKQRTSKQELE 530
Cdd:PHA02562 326 E--EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNA----EELAKLQDELDKIVKTKSELV 399
|
..
gi 7305095 531 TE 532
Cdd:PHA02562 400 KE 401
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
242-571 |
8.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 242 EMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITR-ELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVlssrTEAL 320
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADEL----KKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 321 EALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEVDRQNlAEAVtlaeRKYSE 400
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-AEEL----KKAEE 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 401 EKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKlinslkegssfeglesstaSSMELEELRHEKEMQKEEI 480
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE-------------------DKKKAEEAKKAEEDEKKAA 1691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 481 QKLMGQMHQLR--SELQDMEAQQVSEAESAREqlqdlQDQIAKQRTSKQELETELERMKQEFRYMEEDlhrTKNTLQSRI 558
Cdd:PTZ00121 1692 EALKKEAEEAKkaEELKKKEAEEKKKAEELKK-----AEEENKIKAEEAKKEAEEDKKKAEEAKKDEE---EKKKIAHLK 1763
|
330
....*....|...
gi 7305095 559 KDREEEIQKLRNQ 571
Cdd:PTZ00121 1764 KEEEKKAEEIRKE 1776
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
239-622 |
8.66e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 239 LNQEMASLLQRSKETQEELNKARVRVEKWNVdnSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVlssrte 318
Cdd:PRK10246 255 LQQEASRRQQALQQALAAEEKAQPQLAALSL--AQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMAL------ 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 319 alealrseKSRIMQDHKEGSSLQNQALQTLQERLHEAD----------------ATLKREQESYKQMQSEFAA---RLNK 379
Cdd:PRK10246 327 --------RARIRHHAAKQSAELQAQQQSLNTWLAEHDrfrqwnnelagwraqfSQQTSDREQLRQWQQQLTHaeqKLNA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 380 MEVDRQNL-AEAVTLAERKYSEEK-----------------KKVDELQQQVKLHRASLESAKQELV----DYKQKATRIL 437
Cdd:PRK10246 399 LPAITLTLtADEVAAALAQHAEQRplrqrlvalhgqivpqqKRLAQLQVAIQNVTQEQTQRNAALNemrqRYKEKTQQLA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 438 QSK-----EKLINSLKE--------------GSS-------FEGLESsTASSMELEELRHEKEMQKEEIQKLMGQMHQLR 491
Cdd:PRK10246 479 DVKticeqEARIKDLEAqraqlqagqpcplcGSTshpaveaYQALEP-GVNQSRLDALEKEVKKLGEEGAALRGQLDALT 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 492 SELQ--DMEAQQVSEAESA-REQLQDLQDQIAKQRTSKQELETELErmKQEFRYMEEDLHRTKNTLQSRIKDREEEI--- 565
Cdd:PRK10246 558 KQLQrdESEAQSLRQEEQAlTQQWQAVCASLNITLQPQDDIQPWLD--AQEEHERQLRLLSQRHELQGQIAAHNQQIiqy 635
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7305095 566 --------QKLRNQLTNKTLSNSSQSELESRLH---QLTETLIQKQTMLESLSTEKNSLVFQLERLEQ 622
Cdd:PRK10246 636 qqqieqrqQQLLTALAGYALTLPQEDEEASWLAtrqQEAQSWQQRQNELTALQNRIQQLTPLLETLPQ 703
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
229-497 |
9.67e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 9.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 229 NQLLRNEVQSLNQEMASLlqrskETQEELNKARVRVEKWNVDNS--KSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRL 306
Cdd:PHA02562 169 DKLNKDKIRELNQQIQTL-----DMKIDHIQQQIKTYNKNIEEQrkKNGENIARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 307 QEADQVLSSRTEALEALRSEKSRImqdhkegsSLQNQALQTLQERLHEADatlkrEQESYKQMQSEFAARLNKMEVDRQN 386
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKI--------KSKIEQFQKVIKMYEKGG-----VCPTCTQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 387 LAEAVTLAERKYSEEKKKVDEL-QQQVKLH--RASLESAKQELVDYKQKATRIlqskEKLInslkegssfEGLESSTAS- 462
Cdd:PHA02562 311 LQHSLEKLDTAIDELEEIMDEFnEQSKKLLelKNKISTNKQSLITLVDKAKKV----KAAI---------EELQAEFVDn 377
|
250 260 270
....*....|....*....|....*....|....*
gi 7305095 463 SMELEELRHEKEMQKEEIQKLMGQMHQlRSELQDM 497
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSELVKEKYH-RGIVTDL 411
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
217-624 |
1.23e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 217 SRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKArvrvekwnvdnskSDRITRELRAQVDDLTEAVaakd 296
Cdd:PRK01156 346 SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERM-------------SAFISEILKIQEIDPDAIK---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 297 SQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHK--EGSSLQNQALQTLqerlheADATLKREQESYKQMQSEFA 374
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlNGQSVCPVCGTTL------GEEKSNHIINHYNEKKSRLE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 375 ARLNKMEVDRQNLAEA-VTLAERKYSEEKKKVDELQ---QQVKLHRASLESAKQELVDYKQKATRILQSKEKlINSLKEG 450
Cdd:PRK01156 483 EKIREIEIEVKDIDEKiVDLKKRKEYLESEEINKSIneyNKIESARADLEDIKIKINELKDKHDKYEEIKNR-YKSLKLE 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 451 SSFEGLES-----STASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQrts 525
Cdd:PRK01156 562 DLDSKRTSwlnalAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEI--- 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 526 kqeletelermkqefrymeEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLES 605
Cdd:PRK01156 639 -------------------QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR 699
|
410
....*....|....*....
gi 7305095 606 LSTEKNSLVFQLERLEQQV 624
Cdd:PRK01156 700 LESTIEILRTRINELSDRI 718
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
421-584 |
1.25e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 421 SAKQELVDYKQKATRILQSKEKlinslkegssfeglesstassmELEELRHEKEMQ-KEEIqklmgqmHQLRSELQDmea 499
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKK----------------------EAEAIKKEALLEaKEEI-------HKLRNEFEK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 500 qqvsEAESAREQLQDLQDQIA-KQRTSKQELEtELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNktLS 578
Cdd:PRK12704 76 ----ELRERRNELQKLEKRLLqKEENLDRKLE-LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER--IS 148
|
....*.
gi 7305095 579 NSSQSE 584
Cdd:PRK12704 149 GLTAEE 154
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
210-574 |
1.25e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 210 STPSDGSSRSQELSNLRLENQLLRNEVQSlnqeMASLLQRSKETQEELNKARVRVEKWNVDNSKsDRITR------ELRA 283
Cdd:PLN02939 54 IAPKQRSSNSKLQSNTDENGQLENTSLRT----VMELPQKSTSSDDDHNRASMQRDEAIAAIDN-EQQTNskdgeqLSDF 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 284 QVDDLTEAVaaKDSQLAVLkvRLQEAdqvlssRTEALEALrsekSRIMqdhKEGSSLQnQALQTLQERLHEADATLKREQ 363
Cdd:PLN02939 129 QLEDLVGMI--QNAEKNIL--LLNQA------RLQALEDL----EKIL---TEKEALQ-GKINILEMRLSETDARIKLAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 364 esykQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQ-SKEK 442
Cdd:PLN02939 191 ----QEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKlEKER 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 443 linSLKEgSSFEGLESSTASSME----LEELRHEKEMQK-EEIQKLMgqmhqlrselqDMEAQQVSEAESAREQLQDLQD 517
Cdd:PLN02939 267 ---SLLD-ASLRELESKFIVAQEdvskLSPLQYDCWWEKvENLQDLL-----------DRATNQVEKAALVLDQNQDLRD 331
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7305095 518 QIAKQRTSKQELET------ELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTN 574
Cdd:PLN02939 332 KVDKLEASLKEANVskfssyKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSK 394
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
221-580 |
1.51e-04 |
|
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: 44.89 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 221 ELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQ---EELNKARVRVEKWNVDNSKsdRItRELRAQVDDLTEAVAAKDS 297
Cdd:pfam07888 74 QRRELESRVAELKEELRQSREKHEELEEKYKELSassEELSEEKDALLAQRAAHEA--RI-RELEEDIKTLTQRVLERET 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 298 QLAVLKvrlQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLqNQALQTLQERLHEADATLKREQESYKQMQSEFAARL 377
Cdd:pfam07888 151 ELERMK---ERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSL-SKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 378 NKMEVDRQNLAEAVTLAERKYSEEKKKV---DEL--------QQQVKLHRASLESAKQELvdykQKATRILQSKEKLINS 446
Cdd:pfam07888 227 RKEAENEALLEELRSLQERLNASERKVEglgEELssmaaqrdRTQAELHQARLQAAQLTL----QLADASLALREGRARW 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 447 LKEGSSFEglesstaSSMELEELRHEKemQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSK 526
Cdd:pfam07888 303 AQERETLQ-------QSAEADKDRIEK--LSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 7305095 527 QELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNS 580
Cdd:pfam07888 374 RVAQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSEAALTSTERPDSPLSDS 427
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
310-625 |
1.64e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 44.71 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 310 DQVLSSRTEALEALRSEKSRIMQDHKEGSslqNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKMEVDRQNLAE 389
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEAEF---NQKRAKFKELYLAKEEDLKRQNAVLQEAQVELDALQNQLALARAEMEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 390 AVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELV-DYKQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEE 468
Cdd:pfam03528 80 IKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKETVrEYEVQFHRRLEQERAQWNQYRESAEREIADLRRRLSEGQEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 469 LRHEKEMQK--EEIQKLMGQMHQLRSELQDMEAQQVSEAESARE----QLQDLQDQIAKQRTSKQELETELERMKQEFRY 542
Cdd:pfam03528 160 ENLEDEMKKaqEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKEleasKMKELNHYLEAEKSCRTDLEMYVAVLNTQKSV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 543 MEEDLHRTKNTLQSRIKDREEEIQKlRNQLTNkTLSNSSQSELESRlhqltETLIQKQTMLES-LSTEKNSLVFQLERLE 621
Cdd:pfam03528 240 LQEDAEKLRKELHEVCHLLEQERQQ-HNQLKH-TWQKANDQFLESQ-----RLLMRDMQRMESvLTSEQLRQVEEIKKKD 312
|
....
gi 7305095 622 QQVH 625
Cdd:pfam03528 313 QEEH 316
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
465-572 |
1.80e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEA------QQVSEAESAREqLQDLQDQIAKQRTSKQELETE------ 532
Cdd:COG1579 39 ELAALEARLEAAKTELEDLEKEIKRLELEIEEVEArikkyeEQLGNVRNNKE-YEALQKEIESLKRRISDLEDEilelme 117
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 7305095 533 -LERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQL 572
Cdd:COG1579 118 rIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
505-622 |
1.86e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 505 AESAREQLQDLQDQ---IAKQRTSKQELETELERMKQEFRYMEE--DLHRTKNTLQSRIKDREEEIQKLRNQL---TNKT 576
Cdd:PRK11281 38 EADVQAQLDALNKQkllEAEDKLVQQDLEQTLALLDKIDRQKEEteQLKQQLAQAPAKLRQAQAELEALKDDNdeeTRET 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 7305095 577 LSNSSQSELESRlhqLTETLIQKQTMLESLSTEKNSLVFQLERLEQ 622
Cdd:PRK11281 118 LSTLSLRQLESR---LAQTLDQLQNAQNDLAEYNSQLVSLQTQPER 160
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
275-628 |
1.97e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 275 DRITRElRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTE---ALEALRSEKSRIMQDHKEGSSLQNQALQTLQER 351
Cdd:TIGR00606 224 DQITSK-EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKldnEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 352 LHEADATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRAS-LESAKQELVDYK 430
Cdd:TIGR00606 303 LNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLiQSLATRLELDGF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 431 QKATRILQSKEKLINSLKEGSSFEG----------LESSTASSMELEELRHEK-------EMQKEEIQKLMGQMHQLRSE 493
Cdd:TIGR00606 383 ERGPFSERQIKNFHTLVIERQEDEAktaaqlcadlQSKERLKQEQADEIRDEKkglgrtiELKKEILEKKQEELKFVIKE 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 494 LQDMEAQ-----------QVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIK--- 559
Cdd:TIGR00606 463 LQQLEGSsdrileldqelRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMltk 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 560 ---DREEEIQKLRNQLTNKTLSNS----SQSELESRLH-------QLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVH 625
Cdd:TIGR00606 543 dkmDKDEQIRKIKSRHSDELTSLLgyfpNKKQLEDWLHskskeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLS 622
|
...
gi 7305095 626 SAS 628
Cdd:TIGR00606 623 SYE 625
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
348-627 |
2.01e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 348 LQERLHEADATLKREQESYKQ----------MQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRA 417
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSlsklknkheaMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 418 SLESAKQELVD----------YKQKATRILQSKEKLINSLKE-------------------GSSFEGL----ESSTASSM 464
Cdd:pfam01576 237 QLAKKEEELQAalarleeetaQKNNALKKIRELEAQISELQEdleseraarnkaekqrrdlGEELEALktelEDTLDTTA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 ELEELRHEKEMQKEEIQKLM---GQMHQlrSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFR 541
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALeeeTRSHE--AQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 542 ymeeDLHRTKNTLQSRIKDREEEIQKLRNQLTNktlSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLE 621
Cdd:pfam01576 395 ----TLQQAKQDSEHKRKKLEGQLQELQARLSE---SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLE 467
|
....*.
gi 7305095 622 QQVHSA 627
Cdd:pfam01576 468 SQLQDT 473
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
280-566 |
2.05e-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: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 280 ELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRtEALEALRSEKSRIMQDHKEGSSLQNQalqtlQERLHEADATL 359
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVASAEREIAELEAE-----LERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 360 KREQESYKQMQSEfaarlnkmevdRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYkqkatrilqs 439
Cdd:COG4913 688 AALEEQLEELEAE-----------LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE---------- 746
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 440 KEKLINSLKEGSSFEGLESSTASSMElEELRHEKEMQKEEIQKLMGQMHQLRSElQDMEAQQVSEAESAREQLQDLQDQI 519
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLE-ERIDALRARLNRAEEELERAMRAFNRE-WPAETADLDADLESLPEYLALLDRL 824
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 7305095 520 AkqrtskqelETELERMKQEFR-YMEEDLHRTKNTLQSRIKDREEEIQ 566
Cdd:COG4913 825 E---------EDGLPEYEERFKeLLNENSIEFVADLLSKLRRAIREIK 863
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
218-622 |
2.09e-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: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 218 RSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKAR------VRVEKWNVDNSKSDRITRELRAQVDDLTE- 290
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARkaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKl 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 291 ----AVAAKDSQLAVLKVRL------------QEADQVLSSRTEALEALRSEKS-RIMQDHKEGSSLQNQALQTLQERLH 353
Cdd:TIGR00618 327 lmkrAAHVKQQSSIEEQRRLlqtlhsqeihirDAHEVATSIREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQ 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 354 EADATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVdYKQKA 433
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQ-IHLQE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 434 TRILQSKEKLINSLKEGSS-FEGLESSTASSME-----------LEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQq 501
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCpLCGSCIHPNPARQdidnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQ- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 502 vseAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRymEEDLHRTKNTLQSRIKDREEEIQkLRNQLTNKTLSNSS 581
Cdd:TIGR00618 565 ---MQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPE-QDLQDVRLHLQQCS 638
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 7305095 582 QSE--LESRLHQLTETLIQKQTMLESLSTEknslVFQLERLEQ 622
Cdd:TIGR00618 639 QELalKLTALHALQLTLTQERVREHALSIR----VLPKELLAS 677
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
279-427 |
2.24e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 279 RELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSlqNQALQTLQERLheadAT 358
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--NKEYEALQKEI----ES 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 359 LKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELV 427
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
382-582 |
2.86e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 382 VDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHraslesAKQELVDYKQKATRILQSKEKLINSL------KEgssfEG 455
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLE------AKEEIHKLRNEFEKELRERRNELQKLekrllqKE----EN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 456 LESSTASsmeLEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSE--------AESAREQLqdlqdqiakqrtskq 527
Cdd:PRK12704 98 LDRKLEL---LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEIL--------------- 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 7305095 528 eleteLERMKQEfrymeedlhrTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQ 582
Cdd:PRK12704 160 -----LEKVEEE----------ARHEAAVLIKEIEEEAKEEADKKAKEILAQAIQ 199
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
500-616 |
2.95e-04 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 41.41 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 500 QQVSEAESAREQLQDLQdqiakqrtskQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLtnKTLSN 579
Cdd:pfam03938 12 EESPEGKAAQAQLEKKF----------KKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQEL--QQLQQ 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 7305095 580 SSQSELESRLHQLTETLIQK-QTMLESLSTEKN-SLVFQ 616
Cdd:pfam03938 80 KAQQELQKKQQELLQPIQDKiNKAIKEVAKEKGyDLVLD 118
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
437-620 |
3.00e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.47 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 437 LQSKE-------KLINSLKEG--SSFEGLESstassmELEELRHEKEMQKEEIQKLM----GQMHQLRSELQ---DMEAQ 500
Cdd:smart00787 128 LEAKKmwyewrmKLLEGLKEGldENLEGLKE------DYKLLMKELELLNSIKPKLRdrkdALEEELRQLKQledELEDC 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 501 QVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFrymeEDLHRTKNTLQSRIKdreeEIQKLRNQltNKTLSNS 580
Cdd:smart00787 202 DPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKI----EDLTNKKSELNTEIA----EAEKKLEQ--CRGFTFK 271
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 7305095 581 SQSELESRLHQLtetliQKQTMLESLSTEKNSLVFQLERL 620
Cdd:smart00787 272 EIEKLKEQLKLL-----QSLTGWKITKLSGNTLSMTYDRE 306
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
465-606 |
3.33e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQqvseaesareqLQDLQDQIAKQRTSKQELETELERMKQEFRymE 544
Cdd:COG2433 393 EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE-----------VEELEAELEEKDERIERLERELSEARSEER--R 459
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7305095 545 EDLHRTKntlqsrIKDREEEIQKLRNQLtnktlsnssqSELESRLHQLTETLIQKQTMLESL 606
Cdd:COG2433 460 EIRKDRE------ISRLDREIERLEREL----------EEERERIEELKRKLERLKELWKLE 505
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
255-567 |
4.24e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 255 EELNKAR-VRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQD 333
Cdd:PTZ00121 1227 EAVKKAEeAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 334 HK---EGSSLQNQALQTLQERLHEADATLKREQESYKQmqSEFAARLNKMEVDRQNLAE-AVTLAERKYSEEKKKVDELQ 409
Cdd:PTZ00121 1307 AKkkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA--AEAAKAEAEAAADEAEAAEeKAEAAEKKKEEAKKKADAAK 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 410 QQVKLHRASlESAKQELVDYKQKATRILQSK------EKLINSLKEGSSFEGLESSTASSMELEELRHEKEMQKEEIQKL 483
Cdd:PTZ00121 1385 KKAEEKKKA-DEAKKKAEEDKKKADELKKAAaakkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAK 1463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 484 MGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREE 563
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAE 1543
|
....
gi 7305095 564 EIQK 567
Cdd:PTZ00121 1544 EKKK 1547
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
242-620 |
4.56e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.89 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 242 EMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRlQEADQVLSSRTEALE 321
Cdd:PRK10929 45 EIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALE-QEILQVSSQLLEKSR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 322 ALRSEKSRIMQDHKEGSSLQNQ------ALQTLQERLHEADATLK-REQESYKQMQSEFAAR---LNKMEV------DRQ 385
Cdd:PRK10929 124 QAQQEQDRAREISDSLSQLPQQqtearrQLNEIERRLQTLGTPNTpLAQAQLTALQAESAALkalVDELELaqlsanNRQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 386 NLAeavtlaeRKYSE-EKKKVDELQQQVKLHRASLESAKQelvdykQKATRILQSKEKlinsLKEGSsfEGLESSTASSM 464
Cdd:PRK10929 204 ELA-------RLRSElAKKRSQQLDAYLQALRNQLNSQRQ------REAERALESTEL----LAEQS--GDLPKSIVAQF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 EL-EELRHEKEMQKEEIQKLMGQMHQLRSELqdmeaQQVSEAESA-REQLQ----------DLQDQIAK--QRTSKQELE 530
Cdd:PRK10929 265 KInRELSQALNQQAQRMDLIASQQRQAASQT-----LQVRQALNTlREQSQwlgvsnalgeALRAQVARlpEMPKPQQLD 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 531 TELERMK-QEFRYmeedlhrtkntlqsrikdrEEEIQKLRNQLTNKTLSNSSQSELESRLhqLTETLIQKQTMLESLSTE 609
Cdd:PRK10929 340 TEMAQLRvQRLRY-------------------EDLLNKQPQLRQIRQADGQPLTAEQNRI--LDAQLRTQRELLNSLLSG 398
|
410
....*....|.
gi 7305095 610 KNSLVFQLERL 620
Cdd:PRK10929 399 GDTLILELTKL 409
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
219-629 |
4.74e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 219 SQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQ 298
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQL 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 299 LAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGsslQNQALqTLQERLHEADATLKREQESYKQMQSEFAARLN 378
Cdd:pfam01576 596 VSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK---ETRAL-SLARALEEALEAKEELERTNKQLRAEMEDLVS 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 379 KMEVDRQNLAEAvtlaERKYSEEKKKVDELQQQVKlhraSLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLES 458
Cdd:pfam01576 672 SKDDVGKNVHEL----ERSKRALEQQVEEMKTQLE----ELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEK 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 459 STASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQqVSEAESARE-----------QLQDLQDQIAKQRTSKQ 527
Cdd:pfam01576 744 RRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQ-IDAANKGREeavkqlkklqaQMKDLQRELEEARASRD 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 528 EL-------ETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQ 600
Cdd:pfam01576 823 EIlaqskesEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQ 902
|
410 420
....*....|....*....|....*....
gi 7305095 601 TMLESLSTEKNSLVFQLERLEQQVHSASS 629
Cdd:pfam01576 903 SNTELLNDRLRKSTLQVEQLTTELAAERS 931
|
|
| pepcterm_ChnLen |
TIGR03007 |
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this ... |
408-625 |
5.53e-04 |
|
polysaccharide chain length determinant protein, PEP-CTERM locus subfamily; Members of this protein family belong to the family of polysaccharide chain length determinant proteins (pfam02706). All are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria, and are found near the epsH homolog that is the putative exosortase gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 274386 [Multi-domain] Cd Length: 498 Bit Score: 43.12 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 408 LQQQVKLHRASLESAKQELVDYKQKATRILqskeklinSLKEGSSFEglesstassmELEELRHEKEMQKEEIQKLMGQM 487
Cdd:TIGR03007 166 IDEQIKTYEKKLEAAENRLKAFKQENGGIL--------PDQEGDYYS----------EISEAQEELEAARLELNEAIAQR 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 488 HQLRSELQDMEAQQVSEAESAreqLQDLQDQIakqrtskQELETELERMKqeFRYMEE--DLHRTKNTLQSRIKDREEEI 565
Cdd:TIGR03007 228 DALKRQLGGEEPVLLAGSSVA---NSELDGRI-------EALEKQLDALR--LRYTDKhpDVIATKREIAQLEEQKEEEG 295
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 566 QKLRNQLTNKTLSNSSQSELESRLHQLTETliqkqtmLESLSTEKNSLVFQLERLEQQVH 625
Cdd:TIGR03007 296 SAKNGGPERGEIANPVYQQLQIELAEAEAE-------IASLEARVAELTARIERLESLLR 348
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
260-391 |
5.84e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 260 ARVRVEKwnvdNSKSDRItRELRAQVDDL-TEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALR----SEKSRI--MQ 332
Cdd:COG0542 400 ARVRMEI----DSKPEEL-DELERRLEQLeIEKEALKKEQDEASFERLAELRDELAELEEELEALKarweAEKELIeeIQ 474
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 333 DHKEGSSLQNQALQTLQERLHEADATLKREqesykqmqsefaARLNKMEVDRQNLAEAV 391
Cdd:COG0542 475 ELKEELEQRYGKIPELEKELAELEEELAEL------------APLLREEVTEEDIAEVV 521
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
400-600 |
6.79e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 400 EEKKKVDELQQQVKLHRASLESAKQElvdyKQKATRILQSKEKLINSLKEGSS---------FEGLESSTASSMELEELR 470
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQE----KEEKAREVERRRKLEEAEKARQAemdrqaaiyAEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 471 HE---KEMQKEEIQKLMGQMHQLRS-ELQDMEAQQVSEA-----ESAREQL---QDLQDQIAKQRTSKQELETELERMKQ 538
Cdd:pfam17380 355 QEerkRELERIRQEEIAMEISRMRElERLQMERQQKNERvrqelEAARKVKileEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7305095 539 -EFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTN---KTLSNSSQSELESRLHQLTETLIQKQ 600
Cdd:pfam17380 435 rEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEErkrKKLELEKEKRDRKRAEEQRRKILEKE 500
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
460-603 |
7.05e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 7.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 460 TASSMeleeLRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQvseAESAREQLQDLQDQIAkqrtskqELETELERMKQe 539
Cdd:COG0542 397 EAAAR----VRMEIDSKPEELDELERRLEQLEIEKEALKKEQ---DEASFERLAELRDELA-------ELEEELEALKA- 461
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7305095 540 fRYMEEdlhrtkntlqsriKDREEEIQKLRNQLTNKtlsNSSQSELESRLHQLTETLIQKQTML 603
Cdd:COG0542 462 -RWEAE-------------KELIEEIQELKEELEQR---YGKIPELEKELAELEEELAELAPLL 508
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
454-563 |
8.46e-04 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 40.36 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 454 EGLESSTASSME-LEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQV---SEAESAREQLQDLQDQIAKQRTSKQEL 529
Cdd:pfam10473 27 ENLERELEMSEEnQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVtlrSEKENLTKELQKKQERVSELESLNSSL 106
|
90 100 110
....*....|....*....|....*....|....
gi 7305095 530 ETELERMKQEFRYMEEDLHRTKNTLQSRIKDREE 563
Cdd:pfam10473 107 ENLLEEKEQEKVQMKEESKTAVEMLQTQLKELNE 140
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
489-623 |
8.83e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 40.69 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 489 QLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRtskQELETelermkqefrymeedLHRTKNTLQSRIKDREEEIQKL 568
Cdd:pfam08614 29 EPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLR---EELAE---------------LYRSRGELAQRLVDLNEELQEL 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 569 RNQLTNKTLSNSSQ----SELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 623
Cdd:pfam08614 91 EKKLREDERRLAALeaerAQLEEKLKDREEELREKRKLNQDLQDELVALQLQLNMAEEK 149
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
240-572 |
1.02e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 240 NQEMASLLQRSKETQEELNKARVRVEkwnvdnSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEA 319
Cdd:TIGR00606 676 NQSCCPVCQRVFQTEAELQEFISDLQ------SKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPEL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 320 LEALRSeKSRIMQDHKEGSSLQNQALQTLQERLHEAD------ATLKREQESYKQMQSEFAARLNKMevDRQNLAEAVTL 393
Cdd:TIGR00606 750 RNKLQK-VNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKL--QGSDLDRTVQQ 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 394 AERKYSEEKKKVDELQQQVKLHRaslesakqELVDYKQKATRILQSKeklINSLKegssfeglesstASSMELEELRHEK 473
Cdd:TIGR00606 827 VNQEKQEKQHELDTVVSKIELNR--------KLIQDQQEQIQHLKSK---TNELK------------SEKLQIGTNLQRR 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 474 EMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFR----YMEEDLHR 549
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKnihgYMKDIENK 963
|
330 340
....*....|....*....|...
gi 7305095 550 TKNTLQSRIKDREEEIQKLRNQL 572
Cdd:TIGR00606 964 IQDGKDDYLKQKETELNTVNAQL 986
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
218-602 |
1.08e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 218 RSQELSNLRLENQLLRNEVQSLNQEMASLlQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVA--AK 295
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRL-KNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAqqAA 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 296 DSQLAVLKVRLQEADQVLSSRTEALEALRSEksriMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQsEFAA 375
Cdd:TIGR00606 814 KLQGSDLDRTVQQVNQEKQEKQHELDTVVSK----IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ-QFEE 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 376 RLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQ----VKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEGS 451
Cdd:TIGR00606 889 QLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEkeelISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 452 SFEGLESSTASSMELEELrHEKEMQKEEIQKLMGQM-------HQLRSELQD-----MEAQQVSEAESAREQL--QDLQD 517
Cdd:TIGR00606 969 DDYLKQKETELNTVNAQL-EECEKHQEKINEDMRLMrqdidtqKIQERWLQDnltlrKRENELKEVEEELKQHlkEMGQM 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 518 QIAKQRTSKQELETELERMKQEF--------RYMEEDLHRTKNTLQSRIKDREEeiqKLRNQLTNKTLSNSSQSELESRL 589
Cdd:TIGR00606 1048 QVLQMKQEHQKLEENIDLIKRNHvlalgrqkGYEKEIKHFKKELREPQFRDAEE---KYREMMIVMRTTELVNKDLDIYY 1124
|
410
....*....|...
gi 7305095 590 HQLTETLIQKQTM 602
Cdd:TIGR00606 1125 KTLDQAIMKFHSM 1137
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
500-616 |
1.15e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 500 QQVSEAESAREQLQDLQDQiakqrtskqeLETELERMKQEFRYMEEDLHRTKNTL-QSRIKDREEEIQKLRNQLTNKtlS 578
Cdd:smart00935 11 QESPAGKAAQKQLEKEFKK----------RQAELEKLEKELQKLKEKLQKDAATLsEAAREKKEKELQKKVQEFQRK--Q 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 7305095 579 NSSQSELESRLHQLTETLIQK-QTMLESLSTEKN-SLVFQ 616
Cdd:smart00935 79 QKLQQDLQKRQQEELQKILDKiNKAIKEVAKKKGyDLVLD 118
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
213-623 |
1.27e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 213 SDGSSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNvdnskSDRITRELRAQVDDLTEAV 292
Cdd:TIGR00606 312 RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARD-----SLIQSLATRLELDGFERGP 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 293 AAKdsqlavlkvrlQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSE 372
Cdd:TIGR00606 387 FSE-----------RQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 373 FAARLNKMevdrQNLAEAVTLAERKYSEEKKKVDELQQQVKlhRASLESAKQELVDYKQKATRILQSKEKLINSLKEgss 452
Cdd:TIGR00606 456 LKFVIKEL----QQLEGSSDRILELDQELRKAERELSKAEK--NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ--- 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 453 fegLESSTASSMELEELRHEKEMQKEEIQK--------LMGQMHQL--RSELQDMEAQQVSEAESAREQLQDLQDQIAKQ 522
Cdd:TIGR00606 527 ---LNHHTTTRTQMEMLTKDKMDKDEQIRKiksrhsdeLTSLLGYFpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 523 RTSKQELETELERMKQEFRYMEEDLHR--TKNTLQSRIKDREEEIQKLRNQL--------------TNKTLSNSSQSELE 586
Cdd:TIGR00606 604 EQNKNHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRamlagatavysqfiTQLTDENQSCCPVC 683
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 7305095 587 SRLHQ----LTETLIQKQTMLESLSTEKNSLVFQLERLEQQ 623
Cdd:TIGR00606 684 QRVFQteaeLQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
255-581 |
1.32e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 255 EELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEA--LRSEKSRIMQ 332
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeeLKKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 333 DHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAAR-LNKMEVDRQNLAEAVTLAE----------RKYSEE 401
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeAKKAEEDEKKAAEALKKEAeeakkaeelkKKEAEE 1714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 402 KKKVDELQQQVKLHRASLESAKQELVDYKQKA--TRILQSKEKLINSLKEGSSFEGLESSTASSMELEE-LRHEKEMQKE 478
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRM 1794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 479 EIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYM-------EEDLHRTK 551
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNEngedgnkEADFNKEK 1874
|
330 340 350
....*....|....*....|....*....|..
gi 7305095 552 NTLQSRIKDREE--EIQKLRNQLTNKTLSNSS 581
Cdd:PTZ00121 1875 DLKEDDEEEIEEadEIEKIDKDDIEREIPNNN 1906
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
241-590 |
1.38e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.25 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 241 QEMASLLQRSKETQEELNKARvrvekwnvdnsksdRITRELRAQVDDLTEAVAAKD---SQLAVLkvrlqeADQVLSSRT 317
Cdd:COG3096 836 AELAALRQRRSELERELAQHR--------------AQEQQLRQQLDQLKEQLQLLNkllPQANLL------ADETLADRL 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 318 EALEALRSEksriMQDHKEGSSLQNQALQTLQERLheadATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERK 397
Cdd:COG3096 896 EELREELDA----AQEAQAFIQQHGKALAQLEPLV----AVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRR 967
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 398 ----YSEEKKKVDELQQQVKLHRASLESAKQELvdykqkatriLQSKEKLINSLKEGSSFEGLESSTASSmeleeLRHEK 473
Cdd:COG3096 968 phfsYEDAVGLLGENSDLNEKLRARLEQAEEAR----------REAREQLRQAQAQYSQYNQVLASLKSS-----RDAKQ 1032
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 474 EMQKEeiqklmgqmhqLRSELQDMEAQQVSEAES-AREQLQDLQDQIAKQRTSKQELETELERMKQEfryMEEdlhrtkn 552
Cdd:COG3096 1033 QTLQE-----------LEQELEELGVQADAEAEErARIRRDELHEELSQNRSRRSQLEKQLTRCEAE---MDS------- 1091
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 7305095 553 tLQSRIKDREEEIQKLRNQLTN------KTLSNSSQSELESRLH 590
Cdd:COG3096 1092 -LQKRLRKAERDYKQEREQVVQakagwcAVLRLARDNDVERRLH 1134
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
307-442 |
1.44e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 307 QEADQVLSSRTEALEALRSEK--------SRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLN 378
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEAlleakeeiHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7305095 379 KMEVDRQNLAEAVTLAERKYSEEkkkVDELQQQVKLhraSLESAKQELVD-----YKQKATRILQSKEK 442
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQ---LQELERISGL---TAEEAKEILLEkveeeARHEAAVLIKEIEE 180
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
216-609 |
1.60e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 216 SSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKarvRVEKWnvDNSKSDRITRELRAQVD---DLTEAV 292
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRK---EAPDW--EQSIGKVISPELLHRTDldpEVWDGS 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 293 AAKDSQLAVLKVRLQEADQVLS-SRTEALEALRSEKSRIMQDHKEGSSLQNQALQTLQERLHEADATLKREQESYKQmqs 371
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVPEWaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKN--- 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 372 efaARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQ---QVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLK 448
Cdd:pfam12128 651 ---ARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSleaQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGAL 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 449 EGSsfEGLESSTASSMELEELRHEKEMQKE----------EIQKLMGQMHQLRSELQDMEAQQVSEAESAR--------- 509
Cdd:pfam12128 728 DAQ--LALLKAAIAARRSGAKAELKALETWykrdlaslgvDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetw 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 510 -EQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLR------NQLTNKTLSNSSQ 582
Cdd:pfam12128 806 lQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRcemsklATLKEDANSEQAQ 885
|
410 420
....*....|....*....|....*..
gi 7305095 583 SELESRLHQLTETLIQKQTMLESLSTE 609
Cdd:pfam12128 886 GSIGERLAQLEDLKLKRDYLSESVKKY 912
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
465-624 |
1.95e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQvSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYME 544
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELK-EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 545 EDLHRTKntlqsRIKDREEEIQKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQV 624
Cdd:PRK03918 280 EKVKELK-----ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL 354
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
219-529 |
2.09e-03 |
|
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: 41.49 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 219 SQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQV--------DDLTE 290
Cdd:TIGR00618 583 KEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHalqltltqERVRE 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 291 AVAAKDSQLAVLKVRLQEADQVLSSRTEAL-----------EALRSEKSRIMQDHKEGSSLQNqALQTLQERLHEADATL 359
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQSEKEQLtywkemlaqcqTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDAL 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 360 kreQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQS 439
Cdd:TIGR00618 742 ---NQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 440 KE-KLINSLKEGSSFEG-LESSTASSMELEELRHEKE---MQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQD 514
Cdd:TIGR00618 819 LNlQCETLVQEEEQFLSrLEEKSATLGEITHQLLKYEecsKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLH 898
|
330
....*....|....*
gi 7305095 515 LQDQIAKQRTSKQEL 529
Cdd:TIGR00618 899 EITLYANVRLANQSE 913
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
394-613 |
2.36e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 394 AERKYSEEKKKVDELQQQVKLhraslESAKQELVDYKQKATRILQSKEKLINSLKEGSSFegleSSTASSMELEELrhek 473
Cdd:COG5022 857 AKKRFSLLKKETIYLQSAQRV-----ELAERQLQELKIDVKSISSLKLVNLELESEIIEL----KKSLSSDLIENL---- 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 474 EMQKEEIQKLMGQMHQLRSELQ-DMEAQQVSEaesareqLQDLQDQIAKQRTSKQELETELERMKQEFRymeedlhrtkn 552
Cdd:COG5022 924 EFKTELIARLKKLLNNIDLEEGpSIEYVKLPE-------LNKLHEVESKLKETSEEYEDLLKKSTILVR----------- 985
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7305095 553 tlqsRIKDREEEI----QKLRNQLTNKTLSNSSQSELESRLHQLTEtLIQKQTMLESLSTEKNSL 613
Cdd:COG5022 986 ----EGNKANSELknfkKELAELSKQYGALQESTKQLKELPVEVAE-LQSASKIISSESTELSIL 1045
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
220-401 |
2.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 220 QELSNLRLENQLLRNEVQSLNQEMASLLQRS----------------KETQEELnkARVRVEKWNVDNSKSDriTRELRA 283
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERRealqrlaeyswdeidvASAEREI--AELEAELERLDASSDD--LAALEE 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 284 QVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGSSLQnqalqtLQERLHEADAtlkreQ 363
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL------LEERFAAALG-----D 761
|
170 180 190
....*....|....*....|....*....|....*...
gi 7305095 364 ESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEE 401
Cdd:COG4913 762 AVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
493-624 |
2.44e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 493 ELQDMEaqqvSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFrymeEDLHRTKNTLQSRIKDREEEIQKLRNQL 572
Cdd:COG1579 11 DLQELD----SELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL----EDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7305095 573 ----TNKTLSN---------SSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQV 624
Cdd:COG1579 83 gnvrNNKEYEAlqkeieslkRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
385-622 |
2.73e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 385 QNLAEAVTLAERKySEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRIL-QSKEKLinSLKEgssfegLESSTAS- 462
Cdd:PRK11281 63 QDLEQTLALLDKI-DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETrETLSTL--SLRQ------LESRLAQt 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 463 SMELEELRHE----------KEMQKEEIQKLMG----QMHQLRSELQDMEAQQVSEAESAREQLQDLQDQI-AKQRTSKQ 527
Cdd:PRK11281 134 LDQLQNAQNDlaeynsqlvsLQTQPERAQAALYansqRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLnAQNDLQRK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 528 ELE--TELERMKQEFR-YMEED---LHRTKNTLQSRIKDR-----EEEIQKLRN-QLTNKTLSNS-SQSELESRlHQLTE 594
Cdd:PRK11281 214 SLEgnTQLQDLLQKQRdYLTARiqrLEHQLQLLQEAINSKrltlsEKTVQEAQSqDEAARIQANPlVAQELEIN-LQLSQ 292
|
250 260 270
....*....|....*....|....*....|..
gi 7305095 595 TLIQKQTMLESLSTE----KNslvfQLERLEQ 622
Cdd:PRK11281 293 RLLKATEKLNTLTQQnlrvKN----WLDRLTQ 320
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
293-605 |
3.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 293 AAKDSQLAVLKVRLQEadqvLSSRTEALEALRSEKSRIMQDHKE--GSSLQ-------NQALQTLQERLHEADATLKREQ 363
Cdd:PRK04863 782 AAREKRIEQLRAEREE----LAERYATLSFDVQKLQRLHQAFSRfiGSHLAvafeadpEAELRQLNRRRVELERALADHE 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 364 ESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEkkkVDELQQQvklhRASLESAKQELVDYKQKATRIlqskEKL 443
Cdd:PRK04863 858 SQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLADR---VEEIREQ----LDEAEEAKRFVQQHGNALAQL----EPI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 444 INSLKEG-SSFEGLEsstASSMELEELRHEKEMQK---------------EEIQKLMGQMHQLRSELQDMEAQQVSEAES 507
Cdd:PRK04863 927 VSVLQSDpEQFEQLK---QDYQQAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTR 1003
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 508 AREQLQDLQDQIAK----------QRTSKQELETELERMKQEFRY-----MEEDLHRTKNTLQSRIKDREEEIQKLRNQL 572
Cdd:PRK04863 1004 AREQLRQAQAQLAQynqvlaslksSYDAKRQMLQELKQELQDLGVpadsgAEERARARRDELHARLSANRSRRNQLEKQL 1083
|
330 340 350
....*....|....*....|....*....|...
gi 7305095 573 tnkTLSNSSQSELESRLHQLTETLIQKQTMLES 605
Cdd:PRK04863 1084 ---TFCEAEMDNLTKKLRKLERDYHEMREQVVN 1113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
499-598 |
3.29e-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: 40.52 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 499 AQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLhrtkNTLQSRIKDREEEIQKLRNQLTNKtls 578
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAEL--- 88
|
90 100
....*....|....*....|
gi 7305095 579 NSSQSELESRLHQLTETLIQ 598
Cdd:COG4942 89 EKEIAELRAELEAQKEELAE 108
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
339-569 |
3.35e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 339 SLQNQALQTLQERLHEADATLKREQESYKQMQSEFAArlnkMEVDRQNLAEAVTLAERKYSEE--KKKVDELQQQVKLHR 416
Cdd:pfam15905 90 GEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS----LEKQLLELTRVNELLKAKFSEDgtQKKMSSLSMELMKLR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 417 ASLESAKQELVDYKQKATRILQSKEK-LINSLKEGSSFEGLESSTASSMELEELRHEKEMQK-EEIQKLMGQMHQLRSEL 494
Cdd:pfam15905 166 NKLEAKMKEVMAKQEGMEGKLQVTQKnLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYiTELSCVSEQVEKYKLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 495 QDME---AQQVSEAESAREQLQD----LQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQK 567
Cdd:pfam15905 246 AQLEellKEKNDEIESLKQSLEEkeqeLSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQK 325
|
..
gi 7305095 568 LR 569
Cdd:pfam15905 326 LQ 327
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
340-575 |
3.40e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.83 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 340 LQNQALQTLQERLHEADATLKREQESYKQMQSEFAARLNKME---VDRQNLAEavTLAERKYSE-EKKKVDELQQQVKLH 415
Cdd:pfam05622 187 TYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKErliIERDTLRE--TNEELRCAQlQQAELSQADALLSPS 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 416 RASLESAKQELV--DYKQKATRiLQSKEKLINSLKEGSSFEGLESSTA----SSMELEELRHEKEMQKEEIQKLMGQMHQ 489
Cdd:pfam05622 265 SDPGDNLAAEIMpaEIREKLIR-LQHENKMLRLGQEGSYRERLTELQQlledANRRKNELETQNRLANQRILELQQQVEE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 490 LRSELQD--------------MEAQQV------SEAESAREQLQDLQDQIAKQRTSK-QELETELERMKQEFRYMEEDLH 548
Cdd:pfam05622 344 LQKALQEqgskaedssllkqkLEEHLEklheaqSELQKKKEQIEELEPKQDSNLAQKiDELQEALRKKDEDMKAMEERYK 423
|
250 260 270
....*....|....*....|....*....|....*
gi 7305095 549 RTKNTLQSRIKDRE--------EEIQKLRNQLTNK 575
Cdd:pfam05622 424 KYVEKAKSVIKTLDpkqnpaspPEIQALKNQLLEK 458
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
204-626 |
3.43e-03 |
|
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: 40.72 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 204 TSEEHSSTPSDGSSRSQELSNLRLENQllrnevQSLNQEMASLLQRSKETQEELNKARVRVEkwnVDNSKSDRITRELRA 283
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQ------QELQQRYAELCAAAITCTAQCEKLEKIHL---QESAQSLKEREQQLQ 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 284 QVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSE--------------KSRIMQDHKEGSSLQNQaLQTLQ 349
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidnpgpltrrmqrgEQTYAQLETSEEDVYHQ-LTSER 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 350 ERLHEADATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQvkLHRASLESAKQELVDY 429
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL--LRKLQPEQDLQDVRLH 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 430 KQKATRILQSKEKLINSLKEGSSFEGLESSTASSMELEEL------RHEKEMQkEEIQKLMGQMHQLRSELQDMEAQQVS 503
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllasrqLALQKMQ-SEKEQLTYWKEMLAQCQTLLRELETH 712
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 504 EAESARE------QLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKtl 577
Cdd:TIGR00618 713 IEEYDREfneienASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF-- 790
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 7305095 578 snssQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHS 626
Cdd:TIGR00618 791 ----NRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS 835
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
198-467 |
3.54e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 198 STAPSATSE-EHSSTPSDGSSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEkwnvdnsksdr 276
Cdd:COG3883 7 AAPTPAFADpQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 277 itrELRAQVDDLTEAVAAKDSQLAVLKVRLQEADQVLSSR--TEALEalrseksrimqdhkegsslQNQALQTLQERLHE 354
Cdd:COG3883 76 ---EAEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsfSDFLD-------------------RLSALSKIADADAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 355 ADATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKAT 434
Cdd:COG3883 134 LLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAA 213
|
250 260 270
....*....|....*....|....*....|...
gi 7305095 435 RILQSKEKLINSLKEGSSFEGLESSTASSMELE 467
Cdd:COG3883 214 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
327-563 |
3.66e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 327 KSRIMQDHKEGSSLQNQaLQTLQERLheadATLKREQESYKQMQSEFAARLNKMEVDRQNLAEAVtlaerkyseeKKKVD 406
Cdd:PHA02562 173 KDKIRELNQQIQTLDMK-IDHIQQQI----KTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTI----------KAEIE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 407 ELQQQVKLHRASLESAKQELVDYKQKATRI---LQSKEKLINSLKEG----------SSFEGLESSTASSMEleELRHEK 473
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALNKLNTAAAKIkskIEQFQKVIKMYEKGgvcptctqqiSEGPDRITKIKDKLK--ELQHSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 474 EMQKEEIQKLMGQMHQLRSelQDMEAQQV-SEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKN 552
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNE--QSKKLLELkNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
250
....*....|.
gi 7305095 553 TLQSRIKDREE 563
Cdd:PHA02562 394 TKSELVKEKYH 404
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
355-571 |
3.70e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 355 ADATLKREQESYKQMQSEfaarLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKAT 434
Cdd:COG3883 14 ADPQIQAKQKELSELQAE----LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 435 RILQSKEK------LINSLKEGSSFEG-LESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQvseaES 507
Cdd:COG3883 90 ERARALYRsggsvsYLDVLLGSESFSDfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK----AE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7305095 508 AREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKLRNQ 571
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
216-581 |
3.97e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 216 SSRSQELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKWNVDNSKsdritreLRAQVDDLTEAVAAK 295
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIK-------NNSEIKDLTNQDSVK 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 296 DSQLavlkvrlqeadqvlssrtEALEALRSEksrimqdhkegsslQNQALQTLQERLHEADATLKREQESYKQMQSEfaa 375
Cdd:TIGR04523 453 ELII------------------KNLDNTRES--------------LETQLKVLSRSINKIKQNLEQKQKELKSKEKE--- 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 376 rLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEG 455
Cdd:TIGR04523 498 -LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 456 LESSTASSMELEELRHEKEMQKEEIQKLMGQMHQLRSELQDmeaqqvsEAESAREQLQDLQDQIAKQRTSKQELETELER 535
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK-------ELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 7305095 536 MKQEFRYMEEdlhrTKNTLQSRIKDREEEIQKLrNQLTNKTLSNSS 581
Cdd:TIGR04523 650 IKETIKEIRN----KWPEIIKKIKESKTKIDDI-IELMKDWLKELS 690
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
241-607 |
4.19e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.51 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 241 QEMASLLQRSKETQEELNKARVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDsqlaVLKVRLQEADQ--------- 311
Cdd:pfam07111 73 QELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAE----MVRKNLEEGSQreleeiqrl 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 312 ---VLSSRTEALE-ALRSEKSRIMQDHKEGSSLQ-NQALQTLQERLHEADATLKREQESykQMQSEFAARLNKMEVDRQN 386
Cdd:pfam07111 149 hqeQLSSLTQAHEeALSSLTSKAEGLEKSLNSLEtKRAGEAKQLAEAQKEAELLRKQLS--KTQEELEAQVTLVESLRKY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 387 LAEAV--TLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQ-SKEKLINSLKEGSSFEGLESSTASS 463
Cdd:pfam07111 227 VGEQVppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLAlQEEELTRKIQPSDSLEPEFPKKCRS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 464 M------ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMK 537
Cdd:pfam07111 307 LlnrwreKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQ 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 538 QEFRYMEEdlhrtkntlqsRIKDREEEIQKLRNQLtnktlsNSSQSELESRLHQLTETLIQKQTMLESLS 607
Cdd:pfam07111 387 EARRRQQQ-----------QTASAEEQLKFVVNAM------SSTQIWLETTMTRVEQAVARIPSLSNRLS 439
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
391-613 |
4.29e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 391 VTLAERKYSEEKKKVDELQqqvklhrASLESAKQELVDYKQKATRILQSKEKLINSLKEgsSFEGLEsstassmelEELR 470
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELI-------ASLEELERELEQKAEEAEALLKEAEKLKEELEE--KKEKLQ---------EEED 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 471 HEKEMQKEEIQKLMGQ----MHQLRSELQDMEAQQVSEAesAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEED 546
Cdd:PRK00409 566 KLLEEAEKEAQQAIKEakkeADEIIKELRQLQKGGYASV--KAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEV 643
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7305095 547 LHRT---KNTLQSRIKDREEEIQ----KLRNQLtnktlsnssqSELESRLHQLTETLIQKQTMLESLSTEKNSL 613
Cdd:PRK00409 644 KYLSlgqKGEVLSIPDDKEAIVQagimKMKVPL----------SDLEKIQKPKKKKKKKPKTVKPKPRTVSLEL 707
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
465-629 |
4.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 ELEELRhEKEMQKEEIQKLMGQMHQLRSELQDMEA-QQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYM 543
Cdd:COG4913 243 ALEDAR-EQIELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 544 EEDL-----------HRTKNTLQSRIKDREEEIQKLRNQLTN-----KTL---SNSSQSELESRLHQLTETLIQKQTMLE 604
Cdd:COG4913 322 REELdeleaqirgngGDRLEQLEREIERLERELEERERRRARleallAALglpLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180
....*....|....*....|....*
gi 7305095 605 SLSTEKNSLVFQLERLEQQVHSASS 629
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEA 426
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
478-575 |
4.48e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 38.66 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 478 EEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTS-----KQELETELERMKQEFrymeedlhrtkn 552
Cdd:COG2825 32 QRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATlseeeRQKKERELQKKQQEL------------ 99
|
90 100
....*....|....*....|...
gi 7305095 553 tlQSRIKDREEEIQKLRNQLTNK 575
Cdd:COG2825 100 --QRKQQEAQQDLQKRQQELLQP 120
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
469-573 |
4.49e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.45 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 469 LRHEKEMqkEEIQKLMGQMHQLRSELQdmeaQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLH 548
Cdd:pfam11559 45 QQRDRDL--EFRESLNETIRTLEAEIE----RLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQ 118
|
90 100 110
....*....|....*....|....*....|..
gi 7305095 549 RTKNTLQSR-------IKDREEEIQKLRNQLT 573
Cdd:pfam11559 119 RLKNALQQIktqfaheVKKRDREIEKLKERLA 150
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
319-539 |
4.73e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.42 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 319 ALEALRSEKSRIMQDHKEGSSLQN-------QALQTLQERLHEADATLKREQEsYKQMQSEFAaRLNKmEVDRQNLAEAv 391
Cdd:PRK10929 17 AYAATAPDEKQITQELEQAKAAKTpaqaeivEALQSALNWLEERKGSLERAKQ-YQQVIDNFP-KLSA-ELRQQLNNER- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 392 tlAERKYSEEKKKVDELQQQVkLHRAS--LESAKQ----------------ELVDYKQKATRILQSKEKLINSLKEGSSF 453
Cdd:PRK10929 93 --DEPRSVPPNMSTDALEQEI-LQVSSqlLEKSRQaqqeqdrareisdslsQLPQQQTEARRQLNEIERRLQTLGTPNTP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 454 EGLESSTASSME-------LEEL--------------RHEKEMQKEEIQKLMGQMHQLRSELQDmeaQQVSEAESA---- 508
Cdd:PRK10929 170 LAQAQLTALQAEsaalkalVDELelaqlsannrqelaRLRSELAKKRSQQLDAYLQALRNQLNS---QRQREAERAlest 246
|
250 260 270
....*....|....*....|....*....|....
gi 7305095 509 ---REQLQDLQDQIAKQRTSKQELETELERMKQE 539
Cdd:PRK10929 247 ellAEQSGDLPKSIVAQFKINRELSQALNQQAQR 280
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
185-482 |
4.95e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 185 DSVPEVHKEPSEESTAPSATSEEHSSTPSDGSsrsQELSNLRLENQLLRNEVQSLN-QEMASLLQRSKETQEELNK---- 259
Cdd:pfam12128 614 QSAREKQAAAEEQLVQANGELEKASREETFAR---TALKNARLDLRRLFDEKQSEKdKKNKALAERKDSANERLNSleaq 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 260 ARVRVEKWNVDNSKSDRITRELRAQVDD-LTEAVAAKDSQLAVLKVRLQEADQVLSSRTEALEALRSEKSRIMQDHKEGS 338
Cdd:pfam12128 691 LKQLDKKHQAWLEEQKEQKREARTEKQAyWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVI 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 339 SLQNQALQTLQERLHEADatlKREQE--SYKQ-MQSEFAARlnkmevdRQNLAEAVTLAERKYSEEKKKVDELQQQVKLH 415
Cdd:pfam12128 771 AKLKREIRTLERKIERIA---VRRQEvlRYFDwYQETWLQR-------RPRLATQLSNIERAISELQQQLARLIADTKLR 840
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7305095 416 RASLESAKQELVDYKQKAT---RILQSKEKLINSLKEGSSFEGLESSTASSME-LEELRHEKEMQKEEIQK 482
Cdd:pfam12128 841 RAKLEMERKASEKQQVRLSenlRGLRCEMSKLATLKEDANSEQAQGSIGERLAqLEDLKLKRDYLSESVKK 911
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
408-624 |
5.17e-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: 39.88 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 408 LQQQVKLHRAsLESAKQELVDYKQKATRILQSKEKLINSLKegSSFEGLESSTASSMELEElrhEKEMQKEEIQKLMGQM 487
Cdd:pfam07888 40 LQERAELLQA-QEAANRQREKEKERYKRDREQWERQRRELE--SRVAELKEELRQSREKHE---ELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 488 HQLRSELQDMEAQQVseaesarEQLQDLQDQIAKQRTSKQELETELERMKQEFRYM---EEDLHRTKNTLQSRIKDREEE 564
Cdd:pfam07888 114 SEEKDALLAQRAAHE-------ARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqRKEEEAERKQLQAKLQQTEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7305095 565 I-------QKLRNQLTNKTLSNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQV 624
Cdd:pfam07888 187 LrslskefQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKV 253
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
465-591 |
5.29e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.04 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEaQQVSEAESAREQLQDLQ----DQIAKQRTS-------KQELETEL 533
Cdd:pfam05911 689 EFEQLKSEKENLEVELASCTENLESTKSQLQESE-QLIAELRSELASLKESNslaeTQLKCMAESyedletrLTELEAEL 767
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7305095 534 ERMKQEFRYMEEDLHRTKNT---LQSRIKDREEEIQklRNqlTNKTLSNSSQSELESRLHQ 591
Cdd:pfam05911 768 NELRQKFEALEVELEEEKNCheeLEAKCLELQEQLE--RN--EKKESSNCDADQEDKKLQQ 824
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
215-629 |
5.77e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 215 GSSRSQELSNLRLENqlLRNEVQSLNQEMASLLQRSKETQEELNKARV------RVEKWNVDnsksdriTRELRAQVDDL 288
Cdd:PRK04863 297 TSRRQLAAEQYRLVE--MARELAELNEAESDLEQDYQAASDHLNLVQTalrqqeKIERYQAD-------LEELEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 289 TEAVAAKDSQLAVLKVRLQEADQ-VLSSRT------EALEALrseksrimqdHKEGSSLQN--QALQTLQERLHEADATL 359
Cdd:PRK04863 368 NEVVEEADEQQEENEARAEAAEEeVDELKSqladyqQALDVQ----------QTRAIQYQQavQALERAKQLCGLPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 360 kreqESYKQMQSEFAARLnkmevdrQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQElvdykqkatrilQS 439
Cdd:PRK04863 438 ----DNAEDWLEEFQAKE-------QEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRS------------EA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 440 KEKLINSLKEGSSFEGL-ESSTASSMELEEL--RHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQ 516
Cdd:PRK04863 495 WDVARELLRRLREQRHLaEQLQQLRMRLSELeqRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 517 DQIAKQRTskqELETELERMKQEFRymeedlhrtkntlqsRIKDREEEIQKLRNQLTnkTLSNSSQSELESRlHQLTETL 596
Cdd:PRK04863 575 SEARERRM---ALRQQLEQLQARIQ---------------RLAARAPAWLAAQDALA--RLREQSGEEFEDS-QDVTEYM 633
|
410 420 430
....*....|....*....|....*....|...
gi 7305095 597 IQKQTMLESLSTEKNSLVFQLERLEQQVHSASS 629
Cdd:PRK04863 634 QQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
359-588 |
6.22e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 359 LKREQESYKQMQSEFAARLNKMEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRIlq 438
Cdd:COG1340 20 LREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDEL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 439 sKEKLINSLKEGSSFEGLESSTAS---SMELEELRHEKEMQ--------KEEIQKLMgQMHQLRSELQDMEAQQVS---E 504
Cdd:COG1340 98 -RKELAELNKAGGSIDKLRKEIERlewRQQTEVLSPEEEKElvekikelEKELEKAK-KALEKNEKLKELRAELKElrkE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 505 AESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEED----------LHRTKNTLQSRIKDREEEIQKLRNQlTN 574
Cdd:COG1340 176 AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEiveaqekadeLHEEIIELQKELRELRKELKKLRKK-QR 254
|
250
....*....|....
gi 7305095 575 KTLSNSSQSELESR 588
Cdd:COG1340 255 ALKREKEKEELEEK 268
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
234-611 |
6.42e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.03 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 234 NEVQSLNQEMASLLQRS----KETQEELNkarVRVEKWNVDNSKSDRITRELRAQVDDLTEAVAAKDSQLAVLKVRLQEA 309
Cdd:TIGR01612 1372 KEIEENNKNIKDELDKSekliKKIKDDIN---LEECKSKIESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADEN 1448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 310 DQVLSSRTEALEALRSEKSRIMQDHKE-GSSLQNQALQTLQERLH-------EADATLK---REQESYKQMQSEFAARLN 378
Cdd:TIGR01612 1449 NENVLLLFKNIEMADNKSQHILKIKKDnATNDHDFNINELKEHIDkskgckdEADKNAKaieKNKELFEQYKKDVTELLN 1528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 379 KM-EVDRQNlaeavTLAERKYSEEK--KKVDELQQQVKLHRaslESAKQELVDYKQKATRILQSKEKLINSLKEG----S 451
Cdd:TIGR01612 1529 KYsALAIKN-----KFAKTKKDSEIiiKEIKDAHKKFILEA---EKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAidiqL 1600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 452 SFEGLESSTASSMELEELRHEKEMQKEEIQKlmgQMHQLRSELQDMEaqqVSEAESAREQLQDLQDQIAKQRTSKQELET 531
Cdd:TIGR01612 1601 SLENFENKFLKISDIKKKINDCLKETESIEK---KISSFSIDSQDTE---LKENGDNLNSLQEFLESLKDQKKNIEDKKK 1674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 532 ELERMKQEFRYMEEDLHRTKNTLQSRIKDREEEIQKlrnqlTNKTLSNSSQSELESRLHQLTETL-------IQKQTMLE 604
Cdd:TIGR01612 1675 ELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAI-----ANKEEIESIKELIEPTIENLISSFntndlegIDPNEKLE 1749
|
....*..
gi 7305095 605 SLSTEKN 611
Cdd:TIGR01612 1750 EYNTEIG 1756
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
465-627 |
6.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 465 ELEELRHEKEMQKEEIQKLMGQMHQLRSELQDMEAQQvseaESAREQLQDLQDQIAKQrtsKQELETELERMKQEFRYM- 543
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----EALQAEIDKLQAEIAEA---EAEIEERREELGERARALy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 544 ------------------EEDLHRTK--NTLQSRIKDREEEIQKLRNQLTNKTLSNSS--------QSELESRLHQLTET 595
Cdd:COG3883 97 rsggsvsyldvllgsesfSDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEAklaelealKAELEAAKAELEAQ 176
|
170 180 190
....*....|....*....|....*....|..
gi 7305095 596 LIQKQTMLESLSTEKNSLVFQLERLEQQVHSA 627
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
220-468 |
7.28e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 220 QELSNLRLENQLLRNEVQSLNQEMASLLQRSKETQEELNKARVRVEKwnvdnsksdritreLRAQVDDLTEAVAAKDSQL 299
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDK--------------LQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 300 AVLKVRLQEADQVLSSrteaLEALrseksrimqdhkegssLQNQALQTLQERLHeadaTLKREQESYKQMQSEFAARLNK 379
Cdd:COG3883 89 GERARALYRSGGSVSY----LDVL----------------LGSESFSDFLDRLS----ALSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 380 MEVDRQNLAEAVTLAERKYSEEKKKVDELQQQVKLHRASLESAKQELVDYKQKATRILQSKEKLINSLKEGSSFEGLESS 459
Cdd:COG3883 145 LEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
....*....
gi 7305095 460 TASSMELEE 468
Cdd:COG3883 225 AAAAAAAAA 233
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
233-495 |
8.20e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.13 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 233 RNEVQSLNQEMASLLQRSKETQEELNKARVRVEKW--------NVDNSKSDRITRELRAQVDDLTEAVAAKDSQL----- 299
Cdd:pfam00038 3 KEQLQELNDRLASYIDKVRFLEQQNKLLETKISELrqkkgaepSRLYSLYEKEIEDLRRQLDTLTVERARLQLELdnlrl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 300 AVLKVRLQEADQvLSSRTEALEALRSEKSRIMQDHKEGSSLQNQaLQTLQERLheadATLKRE-QESYKQMQSEFAARLN 378
Cdd:pfam00038 83 AAEDFRQKYEDE-LNLRTSAENDLVGLRKDLDEATLARVDLEAK-IESLKEEL----AFLKKNhEEEVRELQAQVSDTQV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 379 KMEVD---RQNLAEAvtLAE------------RKYSEE--KKKVDELQQQVKLHRASLESAKQELVDYKqkatRILQSKE 441
Cdd:pfam00038 157 NVEMDaarKLDLTSA--LAEiraqyeeiaaknREEAEEwyQSKLEELQQAAARNGDALRSAKEEITELR----RTIQSLE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 7305095 442 KLINSLKegSSFEGLESSTAssmELEElRHEKEMQ--KEEIQKLMGQMHQLRSELQ 495
Cdd:pfam00038 231 IELQSLK--KQKASLERQLA---ETEE-RYELQLAdyQELISELEAELQETRQEMA 280
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
464-623 |
8.45e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.34 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 464 MELEELRHEKEMQKEEIQKlmgqmhqlrselqdmeAQQVSEAESAREQLQDLQDQI-AKQRTSKQELETELERMKQEFRY 542
Cdd:pfam17380 296 MEQERLRQEKEEKAREVER----------------RRKLEEAEKARQAEMDRQAAIyAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 543 MEEDLHRTKNTLQSRIKDREEEIQKLRNQLTNKTLsnssQSELE-SRLHQLTETLIQKQTMLESLSTEK------NSLVF 615
Cdd:pfam17380 360 RELERIRQEEIAMEISRMRELERLQMERQQKNERV----RQELEaARKVKILEEERQRKIQQQKVEMEQiraeqeEARQR 435
|
....*...
gi 7305095 616 QLERLEQQ 623
Cdd:pfam17380 436 EVRRLEEE 443
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
475-627 |
8.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 475 MQKEEIQKLMGQMHQLRSELQDMEAQQVSEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLHRTKNTL 554
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7305095 555 QsrIKDREEEIQKLRNQLTNKTlsnSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQVHSA 627
Cdd:COG4717 126 Q--LLPLYQELEALEAELAELP---ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
474-624 |
9.67e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305095 474 EMQKEEIQKLMGQMHQLRSELQDMEAqqvsEAESAREQLQDLQDQIAKQRTSKQELETELERMKQEFRYMEEDLhrtkNT 553
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQARE----ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL----ES 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7305095 554 LQSRIKDREEEIQKLRNQLTNKtlsNSSQSELESRLHQLTETLIQKQTMLESLSTEKNSLVFQLERLEQQV 624
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDL---EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
|
| |
