|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
49-485 |
1.22e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 49 DLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEG--DVE 126
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERrrELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 127 ALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGEN 206
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 207 QMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRLQ 286
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 287 DADVSAASLQSELAHSLDDGDQGQGADAPGDTPTTRSPKTRKASSPQPSP-PEEILEPPKKRTSLSPAEILEEKEVEVAK 365
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvAVLIGVEAAYEAALEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 366 LQDEISLQQAELQS-------LREELQRQKELRAQEDPGEALHSALSDRDEAVNKALELSLQLNRVSLERDSLSRELLRA 438
Cdd:COG1196 556 DEVAAAAIEYLKAAkagratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1614228177 439 IRQKVALTQELEAWQDDMQVVIGQQLRSQRQKELSASASSSTPRRAA 485
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-296 |
1.85e-12 |
|
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: 70.09 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 53 QLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAE---WEARAVELEGDVEALR 129
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 130 AQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQ---ELQRELDALRGQCQAQALAGAELRTRLESLQGEN 206
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 207 QMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRLQ 286
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
250
....*....|
gi 1614228177 287 DADVSAASLQ 296
Cdd:TIGR02168 921 REKLAQLELR 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
74-498 |
1.41e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 74 RNEELRRQLETLSAQHLEREERLQQENHELRRgLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSEL 153
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 154 SeqnlRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGR 233
Cdd:COG1196 298 A----RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 234 LQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEE-SRLQDADVSAASLQSELAHSLDDGDQGQGA 312
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEElEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 313 DApgdtpttrspktrkasspqpsppeeileppkkRTSLSPAEILEEKEVEVAKLQDEISLQQAELQSLREELQRQKELRA 392
Cdd:COG1196 454 LE--------------------------------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 393 QEDPGEALHSALSDRDEAVNKALELSLQLNRVSLERDSLSRELLRAIRQKVALTQELEAWQDDmqvvIGQQLRSQRQKEL 472
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE----YLKAAKAGRATFL 577
|
410 420
....*....|....*....|....*.
gi 1614228177 473 SASASSSTPRRAAPRFSLRLGPGPAG 498
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDL 603
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
70-385 |
9.94e-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: 64.70 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 70 MLLERNEELRRQLETLsaqhLEREERLQQENHELRRGLA---ARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRER 146
Cdd:TIGR02169 678 RLRERLEGLKRELSSL----QSELRRIENRLDELSQELSdasRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 147 ARALSELSEQNLRLSQQLAQASQTE---------------QELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQS 211
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEealndlearlshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 212 RRQ-------DLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELE---- 280
Cdd:TIGR02169 834 EIQelqeqriDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEaqie 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 281 -EESRLQDADVSAASLQSELAHSLDDGDQGQgadapgdtpttrspktrkaSSPQPSPPEEILEPPKKR-----TSLSPAE 354
Cdd:TIGR02169 914 kKRKRLSELKAKLEALEEELSEIEDPKGEDE-------------------EIPEEELSLEDVQAELQRveeeiRALEPVN 974
|
330 340 350
....*....|....*....|....*....|..
gi 1614228177 355 ILEEKEVE-VAKLQDEISLQQAELQSLREELQ 385
Cdd:TIGR02169 975 MLAIQEYEeVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-282 |
2.45e-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: 63.15 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 50 LALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELrrglaargAEWEARAVELEGDVEALR 129
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL--------KALREALDELRAELTLLN 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 130 AQLGEQRSEQQDSGRERARA----------LSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRL 199
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATerrledleeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 200 ESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRE-RREHSLELERARSEAGEALSALRRLQRRVSE 278
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
....
gi 1614228177 279 LEEE 282
Cdd:TIGR02168 977 LENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
76-422 |
3.71e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 76 EELRRQLETLSAQhLEREERLQQENHELRrglAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSE 155
Cdd:TIGR02168 196 NELERQLKSLERQ-AEKAERYKELKAELR---ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 156 QNLRLSqqlaQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQ 235
Cdd:TIGR02168 272 LRLEVS----ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 236 TTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVS-AASLQSELAHSLDDGDQGQGADA 314
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErLEARLERLEDRRERLQQEIEELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 315 PgdtptTRSPKTRKASSPQPSPPEEILEPPKKRtslspaeiLEEKEVEVAKLQDEISLQQAELQSLREELQRqkeLRAQE 394
Cdd:TIGR02168 428 K-----KLEEAELKELQAELEELEEELEELQEE--------LERLEEALEELREELEEAEQALDAAERELAQ---LQARL 491
|
330 340
....*....|....*....|....*...
gi 1614228177 395 DPGEALHSALSDRDEAVNKALELSLQLN 422
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-235 |
7.91e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 50 LALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQqenhELRRGLAARGAEWEARA---VELEGDVE 126
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE----ELESRLEELEEQLETLRskvAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 127 ALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSqqlaqaSQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGEN 206
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLE------EAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
170 180
....*....|....*....|....*....
gi 1614228177 207 QMLQSRRQDLEAQIRGLREEVEKGEGRLQ 235
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
53-234 |
8.87e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 53 QLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELR-RGLAARGAEWEARAVELE---GDVEAL 128
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDassDDLAAL 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 129 RAQLGEQRSEQQDSGRERARALSELSeqnlRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAElrTRLESLQGENQM 208
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIG----RLEKELEQAEEELDELQDRLEAAEDLARLELRALLE--ERFAAALGDAVE 764
|
170 180
....*....|....*....|....*.
gi 1614228177 209 LQSRRQdLEAQIRGLREEVEKGEGRL 234
Cdd:COG4913 765 RELREN-LEERIDALRARLNRAEEEL 789
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
53-300 |
1.12e-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: 54.68 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 53 QLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELR------RGLAARGAEWEARAVELEGDVE 126
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYalaneiSRLEQQKQILRERLANLERQLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 127 ALRAQLGEQRSEQQDSGRERAR---ALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQ 203
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAEleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 204 GENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTheellllrrERREHSLELERARSEAGEALSALRRLQRRVSELEEES 283
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEA---------ELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250 260
....*....|....*....|..
gi 1614228177 284 R-----LQDADVSAASLQSELA 300
Cdd:TIGR02168 471 EeaeqaLDAAERELAQLQARLD 492
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
65-296 |
1.24e-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: 54.68 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 65 AELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQdsgr 144
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE---- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 145 ERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLR 224
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1614228177 225 EEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQ 296
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
49-236 |
6.79e-07 |
|
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: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 49 DLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAA--RGAEWEARAVELEGD-- 124
Cdd:COG4942 52 ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEdf 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 125 VEALRAQ--LGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESL 202
Cdd:COG4942 132 LDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
170 180 190
....*....|....*....|....*....|....
gi 1614228177 203 QGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQT 236
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
78-457 |
7.04e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 78 LRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQrSEQQDSGRERARALSELSEQN 157
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEA-DEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 158 LRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTT 237
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAH 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 238 HEELLLLRRERREHSLELERARSEAGE-------ALSALRRLQRRVSELEEESRLQDADVSAASLQSELAHSLDDGDQGQ 310
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAEleseleeAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 311 GADAPGDTPTTRSpkTRKASSPQPSPPEEILEPPKKRTSLSP------AEILEEKEVEVAKLQDEISLQQAELQSLREEL 384
Cdd:PRK02224 421 RDELREREAELEA--TLRTARERVEEAEALLEAGKCPECGQPvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERL 498
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1614228177 385 QRQKELRAQEDPGEalhsALSDRDEAVNKALElslqLNRVSLERDSLSRELLRAirQKVALTQELEAWQDDMQ 457
Cdd:PRK02224 499 ERAEDLVEAEDRIE----RLEERREDLEELIA----ERRETIEEKRERAEELRE--RAAELEAEAEEKREAAA 561
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
76-386 |
1.42e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 76 EELRRQLETLSAQ--HLEREERLQQENHELR-RGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSE 152
Cdd:TIGR02169 194 DEKRQQLERLRREreKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 153 LSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQalagaelrtrLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEG 232
Cdd:TIGR02169 274 LEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS----------IAEKERELEDAEERLAKLEAEIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 233 RLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEEsrLQDADVSAASLQSELAHSLDDGDQ--GQ 310
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK--LEKLKREINELKRELDRLQEELQRlsEE 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1614228177 311 GADAPGDTPTTRSPKTRKASSPQpsppEEILEPPKKRTSLSP-AEILEEKEVEVAKLQDEISLQQAELQSLREELQR 386
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKE----DKALEIKKQEWKLEQlAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
108-282 |
1.95e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 108 AARGAEWEARAVELEGDVEALRAQLG--EQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQR------ELD 179
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEalEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERldassdDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 180 ALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERrehsLELERAR 259
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA----ALGDAVE 764
|
170 180
....*....|....*....|....
gi 1614228177 260 SEAGEALSA-LRRLQRRVSELEEE 282
Cdd:COG4913 765 RELRENLEErIDALRARLNRAEEE 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
37-265 |
8.51e-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: 47.84 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 37 FLGGGPGPEEPEDLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRgLAARGAEWEA 116
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 117 RAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELR 196
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1614228177 197 TRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEA 265
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
29-228 |
1.04e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 29 FVLERRDSFLGGGPGPEEPEDL------ALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHE 102
Cdd:COG4913 216 YMLEEPDTFEAADALVEHFDDLeraheaLEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 103 LRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSG--------RERARALSELSEQN---LRLSQQLAQASQTE 171
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrleqleREIERLERELEERErrrARLEALLAALGLPL 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1614228177 172 QELQRELDALRGQCQAQALAGAELRTRLESLQGEnqmLQSRRQDLEAQIRGLREEVE 228
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAE---AEAALRDLRRELRELEAEIA 429
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
92-223 |
1.29e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 92 REERLQQENHELRRGLAARGAEwEARAVELEGDVEALRAQLGEQRSEQ---QDSGRERARALSELSEQNLRLSQQLAQAS 168
Cdd:PRK09039 51 KDSALDRLNSQIAELADLLSLE-RQGNQDLQDSVANLRASLSAAEAERsrlQALLAELAGAGAAAEGRAGELAQELDSEK 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1614228177 169 QTEQELQRELDALRGQCqaqalagAELRTRLESLQGENQMLQSRRQDLEAQIRGL 223
Cdd:PRK09039 130 QVSARALAQVELLNQQI-------AALRRQLAALEAALDASEKRDRESQAKIADL 177
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
61-294 |
1.36e-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: 47.45 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 61 LLLAAELGKMLLERNEELRRQLETLSAQhLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQ 140
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQE-IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 141 DSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELdALRGQCQAQALAGAE-LRTRLESLQGENQMLQSRRQDLEAQ 219
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL-LLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1614228177 220 IRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAAS 294
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
55-229 |
2.02e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 55 QQKEKDLLLAAELGKMLLERNEELRRQLETLsaqhlEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLgE 134
Cdd:PRK04863 495 WDVARELLRRLREQRHLAEQLQQLRMRLSEL-----EQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL-E 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 135 QRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQ 214
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERD 648
|
170
....*....|....*
gi 1614228177 215 DLEAQIRGLREEVEK 229
Cdd:PRK04863 649 ELAARKQALDEEIER 663
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
56-236 |
6.98e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 56 QKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAArgaeweARAVELEGDVEALRAQLGEQ 135
Cdd:COG3206 202 RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA------LPELLQSPVIQQLRAQLAEL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 136 RseqqdsgRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQAlagAELRTRLESLQGENQMLQSRRQD 215
Cdd:COG3206 276 E-------AELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAEL---EALQAREASLQAQLAQLEARLAE 345
|
170 180
....*....|....*....|....
gi 1614228177 216 L---EAQIRGLREEVEKGEGRLQT 236
Cdd:COG3206 346 LpelEAELRRLEREVEVARELYES 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
143-305 |
7.56e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 143 GRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQA-QALAG-AELRTRLESLQGENQMLQSRRQDLEA-- 218
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEySWDEIDVASAEREIAELEAELERLDAss 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 219 -QIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVS-----ELEEESRLQDADVSA 292
Cdd:COG4913 685 dDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlelraLLEERFAAALGDAVE 764
|
170
....*....|...
gi 1614228177 293 ASLQSELAHSLDD 305
Cdd:COG4913 765 RELRENLEERIDA 777
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
145-449 |
7.77e-05 |
|
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: 45.58 E-value: 7.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 145 ERARALSELSEQNLRLSQQ----LAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQI 220
Cdd:pfam10174 447 EKERIIERLKEQREREDRErleeLESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAV 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 221 RGLREEVEKGEGRLQTTHEELLLLRR----ERREHSLELE--RARSEAGEALSALRRLQRRVSELEEESRLQDADVSAAS 294
Cdd:pfam10174 527 EQKKEECSKLENQLKKAHNAEEAVRTnpeiNDRIRLLEQEvaRYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 295 L--------QSELAHSLDDGDQGQGADAPGDTPTTRSPKTRKASSPQPSPPEEILEPPKKRTSlspaeILEEKEVEVAKL 366
Cdd:pfam10174 607 SltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQ-----ELDATKARLSST 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 367 QDEISLQQAELQSLREELQRQKElRAQEDPGEALHSALSDRDEAVnKALELSlqlnrvSLERDSLSRELLRAIRQKVALT 446
Cdd:pfam10174 682 QQSLAEKDGHLTNLRAERRKQLE-EILEMKQEALLAAISEKDANI-ALLELS------SSKKKKTQEEVMALKREKDRLV 753
|
...
gi 1614228177 447 QEL 449
Cdd:pfam10174 754 HQL 756
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
49-176 |
1.13e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 44.27 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 49 DLALQLQQKEKDLLlAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRR--GLAARGAEWEARAVELEGDVE 126
Cdd:COG1566 80 DLQAALAQAEAQLA-AAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERyqALYKKGAVSQQELDEARAALD 158
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1614228177 127 ALRAQLGEQRSeQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQR 176
Cdd:COG1566 159 AAQAQLEAAQA-QLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
81-228 |
1.13e-04 |
|
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: 44.94 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 81 QLETLSAQHLEREERLQQENHELRRG-----LAARGAEWEARAVELE------GDVEALRAQLGEQRSEQQDSGRERARA 149
Cdd:COG3096 479 ELVCKIAGEVERSQAWQTARELLRRYrsqqaLAQRLQQLRAQLAELEqrlrqqQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 150 LSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQ---AQALAGAELRTRLESLQGE-NQMLQSRRQDLEAQIRGLRE 225
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelaARAPAWLAAQDALERLREQsGEALADSQEVTAAMQQLLER 638
|
...
gi 1614228177 226 EVE 228
Cdd:COG3096 639 ERE 641
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
50-386 |
1.17e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 50 LALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQ----QENHELRRGLAARGAEWEARAVELEGDV 125
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEgvkaALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 126 EALRAQLGEQRSEQQDsgRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGE 205
Cdd:COG1196 541 EAALAAALQNIVVEDD--EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 206 NQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAgEALSALRRLQRRVSELEEESRL 285
Cdd:COG1196 619 GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL-EAEAELEELAERLAEEELELEE 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 286 QDADVSAASLQSELAHSLDDGDQGQGADAPGDtpttrspktrkasspqpsppEEILEPPKKRTSLSPAEILEEKEVEVAK 365
Cdd:COG1196 698 ALLAEEEEERELAEAEEERLEEELEEEALEEQ--------------------LEAEREELLEELLEEEELLEEEALEELP 757
|
330 340
....*....|....*....|.
gi 1614228177 366 LQDEISLQQAELQSLREELQR 386
Cdd:COG1196 758 EPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
115-454 |
1.53e-04 |
|
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: 44.66 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 115 EARAVELEGDVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAE 194
Cdd:TIGR02168 644 GYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 195 LRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQR 274
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 275 RVSELEEEsrLQDADVSAASLQSELAHSLDDgdqgqgadapgdtpttrspktrkasspqpsppeeileppkkrtslspae 354
Cdd:TIGR02168 804 ALDELRAE--LTLLNEEAANLRERLESLERR------------------------------------------------- 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 355 iLEEKEVEVAKLQDEISLQQAELQSLreelqrQKELRAQEDPGEALHSALsdrDEAVNKALELSLQLNRVSLERDSLSRE 434
Cdd:TIGR02168 833 -IAATERRLEDLEEQIEELSEDIESL------AAEIEELEELIEELESEL---EALLNERASLEEALALLRSELEELSEE 902
|
330 340
....*....|....*....|
gi 1614228177 435 LLRAIRQKVALTQELEAWQD 454
Cdd:TIGR02168 903 LRELESKRSELRRELEELRE 922
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
149-419 |
1.92e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 44.07 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 149 ALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAqalagaeLRTRLESLQGENQMLQSRRQDLEAQIRGLREEVE 228
Cdd:pfam09726 396 ALVRLEQDIKKLKAELQASRQTEQELRSQISSLTSLERS-------LKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQ 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 229 KGEGRLQttheellllrrerrehslELERARSEAGEALSALRRLQRrvselEEESRLQDADVSAASLQSELAHSLddgdq 308
Cdd:pfam09726 469 QLEKRLK------------------AEQEARASAEKQLAEEKKRKK-----EEEATAARAVALAAASRGECTESL----- 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 309 gqgadapgdtpttrspKTRKasspqpsppeeileppkkrtslspaeilEEKEVEVAKLQDEISLQQAELQSLREELQRQK 388
Cdd:pfam09726 521 ----------------KQRK----------------------------RELESEIKKLTHDIKLKEEQIRELEIKVQELR 556
|
250 260 270
....*....|....*....|....*....|.
gi 1614228177 389 ELRAQEDPGEALHSALSDRDEAvNKALELSL 419
Cdd:pfam09726 557 KYKESEKDTEVLMSALSAMQDK-NQHLENSL 586
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
134-300 |
2.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 134 EQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAG--AELRTRLESLQGENQMLQS 211
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQelEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 212 R---RQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLE-LERARSEAGEALSALRRLQRRVSELEEESRLQD 287
Cdd:COG4717 154 RleeLRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEeLEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170
....*....|...
gi 1614228177 288 ADVSAASLQSELA 300
Cdd:COG4717 234 NELEAAALEERLK 246
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
58-416 |
3.11e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 58 EKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEwEARAVELEGDVEALRAQLGEQRS 137
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE-DAKRVEIARKAEDARKAEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 138 EQQDSGRERARALSELSEQNLRLSQQL--AQASQTEQELQRELDALRGQCQAQAlagAELRTRLESLQGENQMLQSRRQD 215
Cdd:PTZ00121 1173 EDAKKAEAARKAEEVRKAEELRKAEDArkAEAARKAEEERKAEEARKAEDAKKA---EAVKKAEEAKKDAEEAKKAEEER 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 216 LEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERArsEAGEALSALRRLQRRVSELEEESRLQDADVSAASL 295
Cdd:PTZ00121 1250 NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA--DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 296 QSELAHSLDDGDQGQGADAPGDTPTTRSPKTRKASSPQPSPPEEILEPPKKRtslspAEILEEKEVEVAKlQDEISLQQA 375
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-----ADAAKKKAEEKKK-ADEAKKKAE 1401
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1614228177 376 ELQSLREELQRQKELRAQEDPGEALHSALSDRDEAVNKALE 416
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
49-184 |
5.08e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 49 DLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEAL 128
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1614228177 129 RAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQ 184
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
73-402 |
6.14e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 73 ERNEELRRQLETLSAQ------HLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRS---EQQDSG 143
Cdd:PRK02224 384 EEIEELEEEIEELRERfgdapvDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecGQPVEG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 144 RERARALSELSEQNLRLSQQLAQASQTEQELQRELDalrgqcqaQALAGAELRTRLESLQgenqmlqSRRQDLEAQIRGL 223
Cdd:PRK02224 464 SPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE--------RAEDLVEAEDRIERLE-------ERREDLEELIAER 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 224 REEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEE----SRLQDADVSAASLQSEL 299
Cdd:PRK02224 529 RETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERieslERIRTLLAAIADAEDEI 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 300 AhSLDDGDQGQGADAPGDTPTTRSPKTRKASSPQPSPPEEILEPPKKRTSLSP-----AEILEEKEVEVAKLQDEISLQQ 374
Cdd:PRK02224 609 E-RLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEyleqvEEKLDELREERDDLQAEIGAVE 687
|
330 340
....*....|....*....|....*...
gi 1614228177 375 AELQSLREELQRQKELRAQEDPGEALHS 402
Cdd:PRK02224 688 NELEELEELRERREALENRVEALEALYD 715
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
49-288 |
6.62e-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: 42.47 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 49 DLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAAR---GAEWEARAVELEGDV 125
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRrdlGEELEALKTELEDTL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 126 EALRAQlGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQA-SQTEQELQRELDALRGQCQAQALAGAELRTRLESLQG 204
Cdd:pfam01576 313 DTTAAQ-QELRSKREQEVTELKKALEEETRSHEAQLQEMRQKhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 205 ENQMLQSRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELeeESR 284
Cdd:pfam01576 392 ELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL--ESQ 469
|
....
gi 1614228177 285 LQDA 288
Cdd:pfam01576 470 LQDT 473
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
64-282 |
6.98e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 64 AAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSG 143
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 144 RERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRgqcqAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGL 223
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE----EEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1614228177 224 REEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGE----ALSALRRLQRRVSELEEE 282
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnllAIEEYEELEERYDFLSEQ 803
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
144-312 |
7.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 144 RERARALSELSEQNlrlsQQLAQASQTEQELQRELDALRGQCQAQALAgaELRTRLESLQGENQMLQSRRQDLEAQIRGL 223
Cdd:COG4913 248 REQIELLEPIRELA----ERYAAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 224 REEVEKGEGRLQTTHEELLLLRRErrehslELERARSEAGEALSALRRLQRRVSELEEESRLQDADVsaASLQSELAHSL 303
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLER------EIERLERELEERERRRARLEALLAALGLPLPASAEEF--AALRAEAAALL 393
|
....*....
gi 1614228177 304 DDGDQGQGA 312
Cdd:COG4913 394 EALEEELEA 402
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
73-393 |
9.96e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 73 ERNEELRRQLETLSAQHLEREERLQQENHELRRGLAA-RGAEWEARAVElegDVEALRAQLGEQR--SEQQDSGRERARA 149
Cdd:PRK04863 307 YRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTAlRQQEKIERYQA---DLEELEERLEEQNevVEEADEQQEENEA 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 150 LSELSEQN-LRLSQQLA-----------QASQTEQELQReLDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLE 217
Cdd:PRK04863 384 RAEAAEEEvDELKSQLAdyqqaldvqqtRAIQYQQAVQA-LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 218 AQIRGLREEVEKGEGRLQttheellllrrerREHSLELERARSEAGE-ALSALRRLqrrvseleEESRLQDADVSAasLQ 296
Cdd:PRK04863 463 QKLSVAQAAHSQFEQAYQ-------------LVRKIAGEVSRSEAWDvARELLRRL--------REQRHLAEQLQQ--LR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 297 SELAHSLDDGDQGQGAdapgdtpttrspktrkasspqpsppEEILEPPKKRTSLSP--AEILEEKEVEVAKLQDEISLQQ 374
Cdd:PRK04863 520 MRLSELEQRLRQQQRA-------------------------ERLLAEFCKRLGKNLddEDELEQLQEELEARLESLSESV 574
|
330 340
....*....|....*....|
gi 1614228177 375 AELQSLREELQRQ-KELRAQ 393
Cdd:PRK04863 575 SEARERRMALRQQlEQLQAR 594
|
|
| Nucleoporin_FG2 |
pfam15967 |
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ... |
124-236 |
1.16e-03 |
|
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.
Pssm-ID: 435043 [Multi-domain] Cd Length: 586 Bit Score: 41.58 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 124 DVEALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRgQCQAQALAGAELRTRLES-- 201
Cdd:pfam15967 252 DVENFQKFVKEQKQVQEEISRMSSKAMLKVQDDIKALKQLLSVAASGLQRNSLAIDKLK-IETAQELKNADIALRTQKtp 330
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1614228177 202 --LQGEN----QMLQSRRQDLEAQIRGLREEVEKGEGRLQT 236
Cdd:pfam15967 331 pgLQHENtapaDYFRSLVEQFEVQLQQYRQQIEELENHLTT 371
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
73-229 |
1.45e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 73 ERNEELRRQLETLSAQHLEREERLQ--QENHEL-------------RRGLAARGAEWEARAVELEGDVEALRAQLGEQRS 137
Cdd:COG3206 175 KALEFLEEQLPELRKELEEAEAALEefRQKNGLvdlseeaklllqqLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 138 EQQDSGreRARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQA-QALAGAELRTRLESLQGENQMLQSRRQDL 216
Cdd:COG3206 255 ALPELL--QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASL 332
|
170
....*....|...
gi 1614228177 217 EAQIRGLREEVEK 229
Cdd:COG3206 333 QAQLAQLEARLAE 345
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
73-237 |
1.46e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 73 ERNEELRRQLETLSAQHLEREERLQ--QENHELRRGLAARGAewearAVELEGDVEALRAQLGEQRSEQQdsgreraRAL 150
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQklQRLHQAFSRFIGSHL-----AVAFEADPEAELRQLNRRRVELE-------RAL 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 151 SELSEQNLRLSQQLAQASQTEQELQR---------------ELDALRGQCQAQALAGAELRT---RLESLQGENQMLQSR 212
Cdd:PRK04863 854 ADHESQEQQQRSQLEQAKEGLSALNRllprlnlladetladRVEEIREQLDEAEEAKRFVQQhgnALAQLEPIVSVLQSD 933
|
170 180
....*....|....*....|....*
gi 1614228177 213 RQDLEAqirgLREEVEKGEGRLQTT 237
Cdd:PRK04863 934 PEQFEQ----LKQDYQQAQQTQRDA 954
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-229 |
1.70e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 49 DLALQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAvELEGDVEAL 128
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA-LLRSELEEL 899
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 129 RAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQEL----QRELDALRGQCQAQALAGAELRTRLESLQG 204
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
170 180 190
....*....|....*....|....*....|....*....
gi 1614228177 205 --------------ENQMLQSRRQDLEAQIRGLREEVEK 229
Cdd:TIGR02168 980 kikelgpvnlaaieEYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
74-417 |
1.90e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 74 RNEELRRQLETLSAQHLEREERLQQEnHELRRGLAARGAE-----WEARAVELEGDVEALRAQLGEQRSEQQDSGRERAR 148
Cdd:PTZ00121 1171 KAEDAKKAEAARKAEEVRKAEELRKA-EDARKAEAARKAEeerkaEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEER 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 149 ALSELSE-QNLRLSQQLAQASQTEQELQRELDALRG---QCQAQALAGAELRTRLESLQGENQMlQSRRQDLEAQIRGLR 224
Cdd:PTZ00121 1250 NNEEIRKfEEARMAHFARRQAAIKAEEARKADELKKaeeKKKADEAKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAK 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 225 EEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQSELAHSLD 304
Cdd:PTZ00121 1329 KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD 1408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 305 DGDQGQGADAPGDTPTTRSPKTRKASSPQPSPPEeileppKKRTSLSPAEILEEKEVEVAKLQDEISLQQAELQSLREEL 384
Cdd:PTZ00121 1409 ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE------AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
330 340 350
....*....|....*....|....*....|...
gi 1614228177 385 QRQKELRAQEDPGEALHSALSDRDEAVNKALEL 417
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
62-183 |
2.21e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 62 LLAAELGkmLLERNEELRRQL--------ETLSAQHLEREERLQQENHELRrglAARGAEWEARAVELEGDVEALRAQLG 133
Cdd:PRK11281 196 LLQAEQA--LLNAQNDLQRKSlegntqlqDLLQKQRDYLTARIQRLEHQLQ---LLQEAINSKRLTLSEKTVQEAQSQDE 270
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1614228177 134 EQRSE-----QQDSGRERA---------RALSELSEQNLRLSQQLAQASQTEQELQRELDALRG 183
Cdd:PRK11281 271 AARIQanplvAQELEINLQlsqrllkatEKLNTLTQQNLRVKNWLDRLTQSERNIKEQISVLKG 334
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
70-457 |
2.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 70 MLLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELegdvEALRAQLGEQRSEQQDSGRERARA 149
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 150 lsELSEQNLRLSQQLAQASQTEQELQRELDALRgqcqAQALAGAELRTRLESLQGEnqmLQSRRQDLEAQIRGLREEVEK 229
Cdd:COG4717 122 --EKLLQLLPLYQELEALEAELAELPERLEELE----ERLEELRELEEELEELEAE---LAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 230 GEGRLQTTHEELLLLRRERREhslELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQSELAHSLDDGDQG 309
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEE---ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 310 QGADAPGDTPTTRSPKTRKASSPQPSPPEEILEPPKKRTSLSPAEILEEKEVE--VAKLQDEISLQQAELQSLREELQRQ 387
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEelLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 388 KELRAQEDpgEALHSALSDRDEAVNKALelslqLNRVSLERDSLSRELLRAIRQKVALTQELEAWQDDMQ 457
Cdd:COG4717 350 QELLREAE--ELEEELQLEELEQEIAAL-----LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE 412
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
97-282 |
2.29e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 97 QQENHELRRGLAARGAEW-EARAVELEGDVEALRAQLGEQRSEQQ--DSGRERARALSELSEqnlrLSQQLAQASQTEQE 173
Cdd:COG3206 162 LEQNLELRREEARKALEFlEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE----LESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 174 LQRELDALRGQCQAQALAGAE---------LRTRLESLQGENQMLQSR-------RQDLEAQIRGLREEVEKGEGRLQTT 237
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPEllqspviqqLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1614228177 238 HEELLLLRRERREhslELERARSEAGEALSALRRLQRRVSELEEE 282
Cdd:COG3206 318 LEAELEALQAREA---SLQAQLAQLEARLAELPELEAELRRLERE 359
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
71-479 |
2.49e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 40.28 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 71 LLERNEELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQQDSGRERARAL 150
Cdd:COG5278 122 ELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALA 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 151 SELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGENQMLQSRRQDLEAQIRGLREEVEKG 230
Cdd:COG5278 202 ALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 231 EGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRLQDADVSAASLQSELAHSLDDGDQGQ 310
Cdd:COG5278 282 ALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 311 GADAPGDTPTTRSPKTRKASSPQPSPPEEILEPPKKRTSLSPAEILEEKEVEVAKLQDEISLQQAELQSLREELQRQKEL 390
Cdd:COG5278 362 AEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALA 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 391 RAQEDPGEALHSALSDRDEAVNKALELSLQLNRVSLERDSLSRELLRAIRQKVALTQELEAWQDDMQVVIGQQLRSQRQK 470
Cdd:COG5278 442 LAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAAL 521
|
....*....
gi 1614228177 471 ELSASASSS 479
Cdd:COG5278 522 AAALASAEL 530
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
76-300 |
3.37e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 76 EELRRQLETLSAQHLEREERLQQENHELRRGLAARGAEWEARAVELEGDVEALRAQLGEQRSEQ----QDSG-------- 143
Cdd:pfam15921 302 EIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERdqfsQESGnlddqlqk 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 144 -----RERARALSELSEQNLRLSQQLAQASQTEQELQRELD--------------ALRGQCQAQalagaeLRTRLESLQG 204
Cdd:pfam15921 382 lladlHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmevqrleallkAMKSECQGQ------MERQMAAIQG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 205 ENQMLQ---SRRQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSlELERARSEAGEALSALR-RLQRRVSELE 280
Cdd:pfam15921 456 KNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ-EKERAIEATNAEITKLRsRVDLKLQELQ 534
|
250 260
....*....|....*....|....
gi 1614228177 281 ----EESRLQDADVSAASLQSELA 300
Cdd:pfam15921 535 hlknEGDHLRNVQTECEALKLQMA 558
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
73-228 |
4.14e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 73 ERNEELRRQLETLSAQHLEREERLQ----QENHELRRGLAARgaewearavelegDVEALRAQLGEQRSEQQDSGRERAR 148
Cdd:PRK11281 80 EETEQLKQQLAQAPAKLRQAQAELEalkdDNDEETRETLSTL-------------SLRQLESRLAQTLDQLQNAQNDLAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 149 ALSELSEQNLRLSQ---QLAQASQTEQELQRELD-----------ALRGQCQA-QALAGAELRTRLESLQGENQM---LQ 210
Cdd:PRK11281 147 YNSQLVSLQTQPERaqaALYANSQRLQQIRNLLKggkvggkalrpSQRVLLQAeQALLNAQNDLQRKSLEGNTQLqdlLQ 226
|
170
....*....|....*...
gi 1614228177 211 SRRQDLEAQIRGLREEVE 228
Cdd:PRK11281 227 KQRDYLTARIQRLEHQLQ 244
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
51-394 |
4.86e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 51 ALQLQQKEKDLLLAAELGKMLLE--RNEELRRQLE-TLSAQHLERE-ERLQQENHELRRGLAARGAEWEARAVELEGDVE 126
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEakKADEAKKKAEeAKKADEAKKKaEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 127 ALRAQLGEQRSEQQDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGEN 206
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 207 QM-LQSRRQDLEAQIRGlrEEVEKGEgRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRRLQRRVSELEEESRL 285
Cdd:PTZ00121 1606 KMkAEEAKKAEEAKIKA--EELKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 286 QDADVSAASLQseLAHSLDDGDQGQGADAPGDTPTTRSPKTRKASSPQPSPPEEI-LEPPKKRTSLSPAEILEEKEVEVA 364
Cdd:PTZ00121 1683 AEEDEKKAAEA--LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAkKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
330 340 350
....*....|....*....|....*....|....*
gi 1614228177 365 KLQDEISLQQAELQS-----LREELQRQKELRAQE 394
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKekeavIEEELDEEDEKRRME 1795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
52-229 |
5.99e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.37 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 52 LQLQQKEKDLLLAAELGKMLLERNEELRRQLETLSAQHLEREERLQQENHELRRglaargaewearaveLEGDVEALRAQ 131
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR---------------LELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 132 LgEQRSEQQDSGRErARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALAGAELRTRLESLQGEnqmLQS 211
Cdd:COG1579 75 I-KKYEEQLGNVRN-NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE---LDE 149
|
170
....*....|....*...
gi 1614228177 212 RRQDLEAQIRGLREEVEK 229
Cdd:COG1579 150 ELAELEAELEELEAEREE 167
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
81-234 |
6.37e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 81 QLETLSAQHLEREERLQQENH------ELRRGLAARGAEWEARAVELEGD-VEALRAQLgEQRSEQQDSGRERAR-ALSE 152
Cdd:PRK04863 936 QFEQLKQDYQQAQQTQRDAKQqafaltEVVQRRAHFSYEDAAEMLAKNSDlNEKLRQRL-EQAEQERTRAREQLRqAQAQ 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 153 LSEQNLRLSQ---QLAQASQTEQELQRELDALrgqcQAQALAGAE--LRTRLESLQGENQMLQSRRQDLEAQIRGLREEV 227
Cdd:PRK04863 1015 LAQYNQVLASlksSYDAKRQMLQELKQELQDL----GVPADSGAEerARARRDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
....*..
gi 1614228177 228 EKGEGRL 234
Cdd:PRK04863 1091 DNLTKKL 1097
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
367-490 |
7.31e-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: 38.59 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 367 QDEISLQQAELQSLREELQRQKELRAQEdpgEALHSALSDRDEAVNKAL-ELSLQLNRVSLERDSLSRELLRAIRQKVAL 445
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL---KKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1614228177 446 TQELEAWQDDMQVVIGQQLRSQRQKELSASASSSTPRRAAPRFSL 490
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQY 140
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
58-339 |
8.03e-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: 38.95 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 58 EKDLLLAAELGKMLLERNEEL--------RRQLETLSAQHLERE-------ERL----QQENHELRRGL-AARG-----A 112
Cdd:pfam17380 330 DRQAAIYAEQERMAMERERELerirqeerKRELERIRQEEIAMEisrmrelERLqmerQQKNERVRQELeAARKvkileE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 113 EWEARAVELEGDVEALRAQLGEQRSEQ-QDSGRERARALSELSEQNLRLSQQLAQASQTEQELQRELDALRGQCQAQALA 191
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRA 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1614228177 192 GAELRTRLEslqgenqmlqsrrQDLEAQIRGLREEVEKGEGRLQTTHEELLLLRRERREHSLELERARSEAGEALSALRR 271
Cdd:pfam17380 490 EEQRRKILE-------------KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1614228177 272 LQRRVSelEEESRLQdadvsAASLQSELAHSLDDGDQGQGADAPGDTPTTRSPKTRKASSPQPSPPEE 339
Cdd:pfam17380 557 QMRKAT--EERSRLE-----AMEREREMMRQIVESEKARAEYEATTPITTIKPIYRPRISEYQPPDVE 617
|
|
| |
