|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-560 |
1.62e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 321 ELPSLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEANI 400
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 401 ELngelnslkshgSEKTSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAENAESKC 480
Cdd:COG1196 334 EL-----------EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 481 TLLTDTNLELSEELSFLRGRAESLENSLHEANHVKMSTVKDIGIRTKIITDLVTKLALERERLHQQISLLTKKNKILAQK 560
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-492 |
1.06e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 260 KELVDKVSTVECHLSASRCREGDLESKLGESLMGLSSLQVNAENIQEGSQHSGGTETHPSPELPSLQDKVKELEKQLRES 339
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 340 DSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCM--------------QLTEANIELNGE 405
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAaterrledleeqieELSEDIESLAAE 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 406 LNSlkshgsektslLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAENAESKctlLTD 485
Cdd:TIGR02168 861 IEE-----------LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK---LAQ 926
|
....*..
gi 1002272288 486 TNLELSE 492
Cdd:TIGR02168 927 LELRLEG 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
325-506 |
3.52e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 325 LQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEANIELNG 404
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 405 ELNSLKSHGSEKTSLLERkLKESHTQLEHAKASLDATVEQQSM---------LRSTMSDMEHMIDDLKGKVLKAETRAEN 475
Cdd:TIGR02168 387 KVAQLELQIASLNNEIER-LEARLERLEDRRERLQQEIEELLKkleeaelkeLQAELEELEEELEELQEELERLEEALEE 465
|
170 180 190
....*....|....*....|....*....|.
gi 1002272288 476 AESKCTLLTDTNLELSEELSFLRGRAESLEN 506
Cdd:TIGR02168 466 LREELEEAEQALDAAERELAQLQARLDSLER 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
186-590 |
1.47e-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: 55.12 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 186 EDQRRNVLQMLEQSIASELDLEKKLSESRCIIEELK----LKLHHHDQEKYF---------------LEESIESLCGKTF 246
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEeasgKKIYEHDSMSTMhfrslgsaiskilreLDTEISYLKGRIF 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 247 AAENASEVLLGTSKELVDKV-----STVECHLSASRCREGDLESKLGESLMGLSSLQVNAENIQEGSQHSGGTETHPSPE 321
Cdd:pfam15921 242 PVEDQLEALKSESQNKIELLlqqhqDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSD 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 322 LPS---------------LQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQ 386
Cdd:pfam15921 322 LEStvsqlrselreakrmYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNK 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 387 NAELRCM-----------QLTEANIELNGELNSLKSHGSEKTSLLER-------------KLKESHTQLEHAKASLDATV 442
Cdd:pfam15921 402 RLWDRDTgnsitidhlrrELDDRNMEVQRLEALLKAMKSECQGQMERqmaaiqgknesleKVSSLTAQLESTKEMLRKVV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 443 EQQSMLRSTMSDMEHMIDDLKGKVLKAETRAENAESKCT-LLTDTNLELsEELSFLRGRAESLENSLHEANHVKMSTVKd 521
Cdd:pfam15921 482 EELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITkLRSRVDLKL-QELQHLKNEGDHLRNVQTECEALKLQMAE- 559
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002272288 522 igiRTKIItdlvtklalerERLHQQISLLTKKNKILAQKCKGSVKDDTQLSKNVTGKDVELHSTKLAEE 590
Cdd:pfam15921 560 ---KDKVI-----------EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
321-560 |
7.87e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 321 ELPSLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEANI 400
Cdd:TIGR02168 254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 401 ELNGELNSLKShgsEKTSL------LERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAE 474
Cdd:TIGR02168 334 ELAEELAELEE---KLEELkeelesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 475 NAESKCTLLTDTNLELSEELSFLRGRAESLENSLHEANHVKMSTVKDigirtkiitDLVTKLALERERLHQQISLLTKKN 554
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE---------RLEEALEELREELEEAEQALDAAE 481
|
....*.
gi 1002272288 555 KILAQK 560
Cdd:TIGR02168 482 RELAQL 487
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
321-549 |
4.70e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.90 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 321 ELPSLQDKVKELEKQLRESDSQLQLAKasaetfqeeQNVLHAEISTlENIIKSLKEDVSRAESRAQNAELRCMQLT---E 397
Cdd:PLN02939 164 EKEALQGKINILEMRLSETDARIKLAA---------QEKIHVEILE-EQLEKLRNELLIRGATEGLCVHSLSKELDvlkE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 398 ANIELNGELNSLKSHGSEKTSLLERKLKeshtqLEHAKASLDATV-EQQSMLRSTMSDMEHMiDDLKGKVL--KAET--- 471
Cdd:PLN02939 234 ENMLLKDDIQFLKAELIEVAETEERVFK-----LEKERSLLDASLrELESKFIVAQEDVSKL-SPLQYDCWweKVENlqd 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 472 ---RAENAESKCTLLTDTNLElseelsfLRGRAESLENSLHEANHVKMSTVKdIGIRTKIITDLVTKLALERERLHQQIS 548
Cdd:PLN02939 308 lldRATNQVEKAALVLDQNQD-------LRDKVDKLEASLKEANVSKFSSYK-VELLQQKLKLLEERLQASDHEIHSYIQ 379
|
.
gi 1002272288 549 L 549
Cdd:PLN02939 380 L 380
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
326-512 |
4.91e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 326 QDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKE--DVSRAESRAQNAELRCMQLTEANIELn 403
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDeiDVASAEREIAELEAELERLDASSDDL- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 404 gelnslkshgsektslleRKLKEshtQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAENAESKCTLL 483
Cdd:COG4913 688 ------------------AALEE---QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190
....*....|....*....|....*....|...
gi 1002272288 484 TDTNLE--LSEELSFLRGR--AESLENSLHEAN 512
Cdd:COG4913 747 LRALLEerFAAALGDAVERelRENLEERIDALR 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
325-553 |
5.41e-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: 50.06 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 325 LQDKVKELEKQLRESDSQLQLAKASAETFQEEQNV-----------LHAEISTLENIIKSLKEDVSRAESRAQNAELRCM 393
Cdd:TIGR02168 191 LEDILNELERQLKSLERQAEKAERYKELKAELRELelallvlrleeLREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 394 QLTEANIELNGELNSLKSHGSEKTSLLERKlkesHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRA 473
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 474 ENAESKCTLLTDTNLELSEELSFLRGRAESLENSLHEAN---HVKMSTVKDIGIRTKIITDLVTKLALERERLHQQISLL 550
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
...
gi 1002272288 551 TKK 553
Cdd:TIGR02168 427 LKK 429
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
328-560 |
7.62e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 328 KVKELEKQLRESDSQLQLAKAsaETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEANIELNGELN 407
Cdd:COG1196 214 RYRELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 408 SLKShgseKTSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAENAESKCTLLTDTN 487
Cdd:COG1196 292 ELLA----ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002272288 488 LELSEELSFLRGRAESLENSLHEANHVKMSTVKDIGIRTKIITDLVTKLA-LERERLHQQISLLTKKNKILAQK 560
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLErLEEELEELEEALAELEEEEEEEE 441
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
173-635 |
1.42e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.54 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 173 ENGIVSSHTSMRTEDQRRNVLQMLEQSIASELDLEKKLSesRCIIEELKLKLHHhdqekyfleesiESLCGKTFAAENAS 252
Cdd:COG5022 793 WRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKK--LRETEEVEFSLKA------------EVLIQKFGRSLKAK 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 253 EVLLGTSKELVDKVSTVECHLSASRCREGDLESKLGESLMglsslQVNAENIQEGSQHSGGTETHPSPELPSLQDKVKEL 332
Cdd:COG5022 859 KRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLK-----LVNLELESEIIELKKSLSSDLIENLEFKTELIARL 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 333 EKQLRESDSQLQLAKASAET-----FQEEQNVLHAEISTLENIIKSLKEDVSraESRAQNAElrcMQLTEANIelnGELN 407
Cdd:COG5022 934 KKLLNNIDLEEGPSIEYVKLpelnkLHEVESKLKETSEEYEDLLKKSTILVR--EGNKANSE---LKNFKKEL---AELS 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 408 SLKSHGSEKTSLLERKLKE--SHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAENaeskcTLLTD 485
Cdd:COG5022 1006 KQYGALQESTKQLKELPVEvaELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRREN-----SLLDD 1080
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 486 TNLELSEelsflrgRAESLENSLheanhvkmsTVKDIgirtkiitdLVTKLALERERLHQQISLLTKKNKILAQKCKGSV 565
Cdd:COG5022 1081 KQLYQLE-------STENLLKTI---------NVKDL---------EVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFL 1135
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 566 KDDTQLSKNVTGKdveLHSTKLAEEIVPDFSSSQTKAEKPVDPSNEEEKTRSSEDDDSGGEGTAEAVRTI 635
Cdd:COG5022 1136 SQLVNTLEPVFQK---LSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVNDL 1202
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
317-507 |
2.01e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 317 HPSPELPSLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAE------L 390
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReelgerA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 391 RCMQLTEANI-------------ELNGELNSLKSHGSEKTSLLERkLKESHTQLEHAKASLDatvEQQSMLRSTMSDMEH 457
Cdd:COG3883 93 RALYRSGGSVsyldvllgsesfsDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELE---AKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002272288 458 MIDDLKGKVLKAETRAENAESKCTLLTDTNLELSEELSFLRGRAESLENS 507
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
326-511 |
2.38e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 326 QDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEANIELNGE 405
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 406 LN----SLKSHGSEKTSL------LERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAEN 475
Cdd:PRK02224 330 LEecrvAAQAHNEEAESLredaddLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN 409
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002272288 476 AESKCTLLTDTNLELSEELSFLRGRAESLENSLHEA 511
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTARERVEEA 445
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
322-511 |
4.52e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 322 LPSLQDKVKELEKQLRESD-SQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSraESRAQNAELRcmqltEANI 400
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK--KLAELEKKLD-----ELEE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 401 ELNGELNSLKSHGSEKTSLLERKLKE------SHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAE 474
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKElepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1002272288 475 NAESKCTL-----LTDTNLELSEELSFLRGRAESLENSLHEA 511
Cdd:PRK03918 651 ELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEI 692
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
125-528 |
5.98e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 125 IKARLDAAMVSLKQMKELVSDIRKEsaKFEKAIEFPHDKEGITgdagyengivsshtsmRTEDQRRNVLQMLEQSIASEL 204
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKE--LEELSRQISALRKDLA----------------RLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 205 DLEKKLSESRCIIEELKLKLHHHDQEKYFLEESIEslcgktfaaenasevllgtskELVDKVSTVECHLSASRCREGDLE 284
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIE---------------------QLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 285 SKLGESLMGLSSLQVNAEniqegsqhsggtethpspelpSLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEI 364
Cdd:TIGR02168 817 EEAANLRERLESLERRIA---------------------ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 365 STLENIIKSLKEDVSRAESRAQNAELRCMQLTEANIELNGELNSLKSHgsektsllerkLKESHTQLEHAKASLDatvEQ 444
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK-----------LAQLELRLEGLEVRID---NL 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 445 QSMLRS----TMSDMEHMIDDLKGKVLKAETRAENAESKCTLLTDTNLELSEELSFLRGRAESLENSLHEANHVK---MS 517
Cdd:TIGR02168 942 QERLSEeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKetlEE 1021
|
410
....*....|.
gi 1002272288 518 TVKDIGIRTKI 528
Cdd:TIGR02168 1022 AIEEIDREARE 1032
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
321-612 |
6.71e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 321 ELPSLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTL-----ENIIKSLKEDVSRAESRAQNAELRCMQL 395
Cdd:TIGR04523 254 QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQN 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 396 TEANIELNGELNSLKSHGSEKTS---LLERKLKESHTQLEHAKAsldatvEQQSMLRStMSDMEHMIDDLKGKVLKAETR 472
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESensEKQRELEEKQNEIEKLKK------ENQSYKQE-IKNLESQINDLESKIQNQEKL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 473 AENAESKCTLLTDTNLELSEELSFLRGRAESLEN---SLHEANHVKMSTVKDIGIRTKIITDLVTKLAL----------- 538
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSeikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkikqnleq 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 539 ----------ERERLHQQISLLTKKNKILAQKCKGSVKDDTQLSKNVTGKDVELhSTKLAEEIVPDFSSSQTKAEKPVDP 608
Cdd:TIGR04523 487 kqkelkskekELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-SDLEDELNKDDFELKKENLEKEIDE 565
|
....
gi 1002272288 609 SNEE 612
Cdd:TIGR04523 566 KNKE 569
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
325-512 |
1.88e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 325 LQDKVKELEKQLRESDSQLQ--LAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAE--LRCMQLTEANI 400
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRaqLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 401 ELNGELNSLKSHGSE---KTSLLERKLKESHTQLEHAKASLDATVEQ-QSMLRSTMSDMEHMIDDLKGKVLKAETRAENA 476
Cdd:COG3206 260 LQSPVIQQLRAQLAEleaELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
170 180 190
....*....|....*....|....*....|....*....
gi 1002272288 477 ESKCTLLTDTNLELSE---ELSFLRGRAESLENSLHEAN 512
Cdd:COG3206 340 EARLAELPELEAELRRlerEVEVARELYESLLQRLEEAR 378
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
328-639 |
3.21e-04 |
|
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: 44.04 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 328 KVKELEKQLRESDSQLQLAKASAETFQEEQnvlHAEISTLE----------NIIKSLKEDVSRAESRAQNAELRCMQLTE 397
Cdd:pfam10174 241 KISSLERNIRDLEDEVQMLKTNGLLHTEDR---EEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKLETLTN 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 398 ANIELNGELNSLKSHGSEK----------TSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVL 467
Cdd:pfam10174 318 QNSDCKQHIEVLKESLTAKeqraailqteVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKIN 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 468 KAETRAENAESKctlLTDTNLELSEelsfLRGRAESLENSLHEANHVKMSTVKDIGIRTKIITDLVTKLALERERLHQQI 547
Cdd:pfam10174 398 VLQKKIENLQEQ---LRDKDKQLAG----LKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEEL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 548 SLLTKKNKILAQKCKGSVKDDTqlSKNVTGKDVELHSTKLAEEIVPDFS-------SSQTKAEKPVDPSNEEEKTRSSED 620
Cdd:pfam10174 471 ESLKKENKDLKEKVSALQPELT--EKESSLIDLKEHASSLASSGLKKDSklksleiAVEQKKEECSKLENQLKKAHNAEE 548
|
330
....*....|....*....
gi 1002272288 621 DDSGGEGTAEAVRTIQPSV 639
Cdd:pfam10174 549 AVRTNPEINDRIRLLEQEV 567
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
321-511 |
3.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 321 ELPSLQDKVKELEKQLRESDsqLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEAnI 400
Cdd:COG4913 256 PIRELAERYAAARERLAELE--YLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ-I 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 401 ELNG--ELNSLK---SHGSEKTSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAEN 475
Cdd:COG4913 333 RGNGgdRLEQLEreiERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEA 412
|
170 180 190
....*....|....*....|....*....|....*.
gi 1002272288 476 AESKCTLLTDtnlELSEELSFLRGRAESLENSLHEA 511
Cdd:COG4913 413 ALRDLRRELR---ELEAEIASLERRKSNIPARLLAL 445
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
321-455 |
4.66e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 321 ELPSLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLEN--IIKSLKEDVSRAESRAQNAELRcmqLTEA 398
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSAR---YTPN 289
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 399 N---IELNGELNSLKshgSEKTSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDM 455
Cdd:COG3206 290 HpdvIALRAQIAALR---AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
321-508 |
6.97e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 321 ELPSLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDvsRAESRAQNAE-LRCMQLTEAN 399
Cdd:COG4942 42 ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE--LEAQKEELAElLRALYRLGRQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 400 IELNGELNSLKSHGSEKT-SLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAENAES 478
Cdd:COG4942 120 PPLALLLSPEDFLDAVRRlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
170 180 190
....*....|....*....|....*....|
gi 1002272288 479 KCTLLTDTNLELSEELSFLRGRAESLENSL 508
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALI 229
|
|
| DUF745 |
pfam05335 |
Protein of unknown function (DUF745); This family consists of several uncharacterized ... |
329-441 |
7.46e-04 |
|
Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.
Pssm-ID: 398808 [Multi-domain] Cd Length: 180 Bit Score: 41.01 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 329 VKELEKQLRESD-------SQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAelrcmqlteanie 401
Cdd:pfam05335 61 VEQLEQELREAEavvqeesASLQQSQANANAAQRAAQQAQQQLEALTAALKAAQANLENAEQVAAGA------------- 127
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1002272288 402 lNGELnslkshgSEKTSLLE---RKLKESHTQLEHAKASLDAT 441
Cdd:pfam05335 128 -QQEL-------AEKTQLLEaakKRVERLQRQLAEARADLEKT 162
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
325-505 |
7.67e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 325 LQDKVKELEKQLRESDSQLQLAKASAETFQEeqnvLHAEISTLENIIKSLKEDVSRAESRAQNAElrcMQLTEANIELNG 404
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQ---AQLAQAQIDLAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 405 eLNSLkshgSEKTSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTM-SDMEHMIDDLKGKVLKAETRAENAESKCTlL 483
Cdd:pfam00529 129 -RRVL----APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQItQSAAENQAEVRSELSGAQLQIAEAEAELK-L 202
|
170 180
....*....|....*....|..
gi 1002272288 484 TDTNLELSEELSFLRGRAESLE 505
Cdd:pfam00529 203 AKLDLERTEIRAPVDGTVAFLS 224
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
185-444 |
9.44e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 185 TEDQRRNVLQMLEQSIASELDLEKKLSESRCIIEELKLKLHHH-----DQEKYFLEESIESLCGKTFAAENASEVLLGTS 259
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 260 KELVDKVSTVECHLSASRCREGDLESKLGESLMGLSSLQVNAENIQegsqhsgGTETHPSPELPSLQDKVKELEKQLRES 339
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE-------AALRDLESRLGDLKKERDELEAQLREL 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 340 DSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQN-AELRCMQLT----EANIELNGELNSLKSHGS 414
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEeLSLEDVQAElqrvEEEIRALEPVNMLAIQEY 981
|
250 260 270
....*....|....*....|....*....|
gi 1002272288 415 EKTSLLERKLKESHTQLEHAKASLDATVEQ 444
Cdd:TIGR02169 982 EEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
184-511 |
1.10e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 184 RTEDQRRNVLQMLEQSIAS--ELDLEKKLSESRCIIEELKLKLHHHDQEKYFLEESIEslcgktfaaeNASEVLlGTSKE 261
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEkeEKDLHERLNGLESELAELDEEIERYEEQREQARETRD----------EADEVL-EEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 262 LVDKVSTVECHLSASRCREGDLESKLGESLMGLSSLQVNAENIQEGSQHSGGTETHPSPELPSLQDKVKELEKQLRESDS 341
Cdd:PRK02224 249 RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 342 QLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEANIELNGELNSLkshgSEKTSLLE 421
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL----RERFGDAP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 422 RKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLK-----GKVLKAETRAENAESKCTLLTDTNL--ELSEEL 494
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleaGKCPECGQPVEGSPHVETIEEDRERveELEAEL 484
|
330
....*....|....*..
gi 1002272288 495 SFLRGRAESLENSLHEA 511
Cdd:PRK02224 485 EDLEEEVEEVEERLERA 501
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
322-554 |
1.14e-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: 42.31 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 322 LPSLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEANIE 401
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 402 LNGELNSLKSHGSEK--------TSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRA 473
Cdd:TIGR04523 286 LEKQLNQLKSEISDLnnqkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 474 ENAESKCTLLTDTNLELSEELSFLRGRAESLENSLHEANhvKMSTVKDIGIRTK-----IITDLVTKLALERERLHQQIS 548
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE--KLNQQKDEQIKKLqqekeLLEKEIERLKETIIKNNSEIK 443
|
....*.
gi 1002272288 549 LLTKKN 554
Cdd:TIGR04523 444 DLTNQD 449
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
273-461 |
1.16e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 273 LSASRCREGDLESKLGESLMGLSSLQVNAENIQEGSQHSGGTETHPSPELPSLQDKVKELEKQLRESDSQLQLAKASAET 352
Cdd:pfam09787 39 LDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 353 FQEEQ-----------NVLHAEISTLENIIKSLKEDV-SRAESRAQNAEL--RCMQLTEANIELNGELNSLkshGSEKTS 418
Cdd:pfam09787 119 LQEELryleeelrrskATLQSRIKDREAEIEKLRNQLtSKSQSSSSQSELenRLHQLTETLIQKQTMLEAL---STEKNS 195
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002272288 419 LLerklkeshTQLEHAKASLDATveQQSMLRSTMSDMEHMIDD 461
Cdd:pfam09787 196 LV--------LQLERMEQQIKEL--QGEGSNGTSINMEGISDG 228
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
188-429 |
1.68e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 188 QRRNVLQ-MLEQSIASELD--LEKKLSESRCIIEELKLKLHHHDQEKYFLEESIESLCGKTFAA----ENASEVLLGTSK 260
Cdd:PHA02562 151 ARRKLVEdLLDISVLSEMDklNKDKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENiarkQNKYDELVEEAK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 261 ELVDKVSTVECHLSASRCREGDLESKLGESLMGLSSLQVNAENIQ--EGSQHSGGT--------ETHPsPELPSLQDKVK 330
Cdd:PHA02562 231 TIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQkvIKMYEKGGVcptctqqiSEGP-DRITKIKDKLK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 331 ELEKQLRESDSQLQLAKASAETFQEEQNVLHAeistLENIIKSLKEDVSRAESRAQNAELRCMQLTEANIELNGELNSLK 410
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLLE----LKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQ 385
|
250
....*....|....*....
gi 1002272288 411 SHGSEKTSLLERKLKESHT 429
Cdd:PHA02562 386 DELDKIVKTKSELVKEKYH 404
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
324-503 |
1.71e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 324 SLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQ----------------- 386
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpplalllspedf 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 387 -NAELRCMQLTEANIELNGELNSLKshgsEKTSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGK 465
Cdd:COG4942 132 lDAVRRLQYLKYLAPARREQAEELR----ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002272288 466 VLKAETRAENAESKCTLLTDTNLELSEELSFLRGRAES 503
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
319-564 |
1.93e-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: 40.90 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 319 SPELPSLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQnaelrcmqltea 398
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 399 niELNGELNSLKshgsEKTSLLERKLKESHTQLEHAKASLDATVEQQSML----RSTMSDMEHMIDDLKGKVLKAETRAE 474
Cdd:COG4942 80 --ALEAELAELE----KEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 475 NAESKCTLLTDTNLELSEE---LSFLRGRAESLENSLHEANHVKMSTVKDIGIRTKIITDLVTKLALERERLHQQISLLT 551
Cdd:COG4942 154 ELRADLAELAALRAELEAEraeLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|...
gi 1002272288 552 KKNKILAQKCKGS 564
Cdd:COG4942 234 AEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
334-515 |
1.99e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 334 KQLRESDSQLQLAKASAETFQEEQNVLH---AEISTLENIIKSLKEDVSRAESRAQNAEL--RCMQLTEANIELNGELNS 408
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEeleEELEELEAELEELREELEKLEKLLQLLPLyqELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 409 LKSHGSEKTSlLERKLKESHTQLEHAKASLDATVEQQS-MLRSTMSDMEHMIDDLKGKVLKAETRAENAEskctlltdtn 487
Cdd:COG4717 151 LEERLEELRE-LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQ---------- 219
|
170 180
....*....|....*....|....*...
gi 1002272288 488 lelsEELSFLRGRAESLENSLHEANHVK 515
Cdd:COG4717 220 ----EELEELEEELEQLENELEAAALEE 243
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
324-582 |
2.44e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 324 SLQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEANIELN 403
Cdd:TIGR04523 395 DLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 404 GELNSLKSHGSEKTSLLERK------LKESHTQLEHAKASL----DATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETra 473
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKekelkkLNEEKKELEEKVKDLtkkiSSLKEKIEKLESEKKEKESKISDLEDELNKDDF-- 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 474 enaESKCTLLTDTNLELSEELSFLRGRAESLENSLHEANhvkmstvKDIGIRTKIITDLVTKLALER---ERLHQQISLL 550
Cdd:TIGR04523 553 ---ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQ-------ELIDQKEKEKKDLIKEIEEKEkkiSSLEKELEKA 622
|
250 260 270
....*....|....*....|....*....|..
gi 1002272288 551 TKKNKILAqkckgSVKDDTQLSKNVTGKDVEL 582
Cdd:TIGR04523 623 KKENEKLS-----SIIKNIKSKKNKLKQEVKQ 649
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
321-443 |
4.13e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 321 ELPSLQDKVKELEK---QLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTE 397
Cdd:COG4913 669 EIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002272288 398 ANIE------------------LNGELNSLKSHGSEKTSLLERKLKESHTQLEHAKASLDATVE 443
Cdd:COG4913 749 ALLEerfaaalgdaverelrenLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLE 812
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-451 |
4.80e-03 |
|
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: 40.44 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 92 DAEVGELDDMISTLETDIQNVEhmvcqdesggkikARLDAAMVSLKQMKELVSDIRKESAKFEKAIEfphdkegitgdag 171
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIE-------------RQLASLEEELEKLTEEISELEKRLEEIEQLLE------------- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 172 yengIVSSHTSMRTEDQRRNVLQMLEqsiaselDLEKKLSESRCIIEELKLKLHHHDQEKYFLEESIESLCGKTFAAENA 251
Cdd:TIGR02169 276 ----ELNKKIKDLGEEEQLRVKEKIG-------ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 252 SEVLLGTSKELVDKVSTVECHLSASRCREGDLESKLGESLMGLSSLQVNAENIQEgsqhsggtETHPS-PELPSLQDKVK 330
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR--------EINELkRELDRLQEELQ 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 331 ELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAElrcmqlteanielngelnslk 410
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK--------------------- 475
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1002272288 411 shgsEKTSLLERKLKESHTQLEHAKASLDATVEQQSMLRST 451
Cdd:TIGR02169 476 ----EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
328-547 |
5.01e-03 |
|
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: 40.05 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 328 KVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAelrcmqlteanieLNGELN 407
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR-------------VKEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 408 SLKShgseKTSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLKAETRAENAESKCTLLTDTN 487
Cdd:TIGR02169 298 ELEA----EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 488 LELSEELSFLRGRAESLENSLHEANHvKMSTVKDIGIRtkiITDLVTKLALERERLHQQI 547
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYREKLEKLKR-EINELKRELDR---LQEELQRLSEELADLNAAI 429
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
323-505 |
5.12e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.33 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 323 PSLQDKVKELEKQLRESDSqlqlAKASAETFQEEQNVLHAEISTLEN---IIKSLKEDVSRAESRAQNAELRCMQLTEAN 399
Cdd:PRK04863 890 ETLADRVEEIREQLDEAEE----AKRFVQQHGNALAQLEPIVSVLQSdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVV 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 400 -----------IELNGELNSLKSHGSEKTSLLERKLKESHTQLEHAKASLDATVEQQSMLRSTMSDMEHMIDDLKGKVLK 468
Cdd:PRK04863 966 qrrahfsyedaAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQD 1045
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002272288 469 AETRA-ENAESKCTLLTDtnlELSEELSFLRGRAESLE 505
Cdd:PRK04863 1046 LGVPAdSGAEERARARRD---ELHARLSANRSRRNQLE 1080
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
325-506 |
6.02e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 325 LQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLENIIKSLKEDVSRAESRAQNAELRCMQLTEANIELNG 404
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 405 ELNSLKSHGSEKTSLLERKLKESHTQLEHAKASLDATVEqqsmLRSTMSDMEHMIDDLKGKVLKAETRAENAESKCTLLT 484
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE----EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
170 180
....*....|....*....|..
gi 1002272288 485 DTNLELSEELSFLRGRAESLEN 506
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLE 498
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
325-479 |
6.40e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 325 LQDKVKELEKQLRESDSQLQLAKASAETFQEEQNVLHAEISTLEN-------IIKSLKEDVSRaESRAQNAELRcmQLTE 397
Cdd:pfam10174 399 LQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEalsekerIIERLKEQRER-EDRERLEELE--SLKK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002272288 398 ANIELNGELNSLKSHGSEK-TSLLERKlkeshtqlEHAKASLDATVEQQSMLRSTMSDMEHMIDD---LKGKVLKAETRA 473
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKeSSLIDLK--------EHASSLASSGLKKDSKLKSLEIAVEQKKEEcskLENQLKKAHNAE 547
|
....*.
gi 1002272288 474 ENAESK 479
Cdd:pfam10174 548 EAVRTN 553
|
|
| |
