|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
137-428 |
3.15e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 137 KEAKSASRLKGKEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRL---IEALTSENLSHKA 213
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELeleLEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 214 LNEQMGQEHADLLERLAAMEQQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAr 293
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 294 ehcsleqaktAENIELVENLQKTNASLLADVVQLKQQIEQDAlsygQEAKSCQAELECLKVERNTLKNDLANKCTLIRSL 373
Cdd:COG1196 375 ----------AEAEEELEELAEELLEALRAAAELAAQLEELE----EAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17137436 374 QDELLDKNCEIDAHCDTIRQLCREQARHTEQQQAVAKVQQQVESDLESAVEREKS 428
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-485 |
5.08e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 220 QEHADLLERLAAMEQQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAREHcsle 299
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER---- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 300 qaktaenielVENLQKTNASLLADVVQLKQQIEQDAlsygQEAKSCQAELECLKVERNTLKNDLANKCTLIRSLQDELLD 379
Cdd:TIGR02168 311 ----------LANLERQLEELEAQLEELESKLDELA----EELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 380 KNCEIDAHCDTIRQLCREQARHTEQQQAVAKVQqqveSDLESAVEREKSYWRAELDKRQKLAENELIKIELEKQDVMVLL 459
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARL----ERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL 452
|
250 260
....*....|....*....|....*.
gi 17137436 460 ETTNDMLRMRDEKLQKCEEQLRNGID 485
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALD 478
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
148-481 |
5.71e-09 |
|
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: 60.08 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 148 KEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKALNEQMGQEHADLLE 227
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 228 RLaameQQLQQQHDEHERQVEALVAESEALrlaNELLQTANEDRQKveeQLQAQLSALQADVAQARehcsleqAKTAENI 307
Cdd:TIGR02169 252 EL----EKLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQL---RVKEKIGELEAEIASLE-------RSIAEKE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 308 ELVENLQKTNASLLADVVQLKQQIEQDALSYGQEAK---SCQAELECLKVERNTLKNDLANKCTLIRSLQDELLDKNCEI 384
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 385 DAHCDTIRQLCREQARHTEQQQAVAKVQQQVESDLESAVEReksywRAELDKRQKLAENELIKIELEKQDVMVLLETTND 464
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK-----INELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
330
....*....|....*..
gi 17137436 465 MLRMRDEKLQKCEEQLR 481
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELS 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
219-585 |
3.43e-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: 54.29 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 219 GQEHADLLERLAAMEQqLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAREHCSL 298
Cdd:TIGR02168 666 AKTNSSILERRREIEE-LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 299 EQaktaeniELVENLQKTNASLLADVVQLKQQIEQDAlsygQEAKSCQAELECLKVERNTLKNDLANKCTLIRSLQDELL 378
Cdd:TIGR02168 745 LE-------ERIAQLSKELTELEAEIEELEERLEEAE----EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 379 DKNCEIDAHCDTIRQLCREQARHTEQQQAVAKVQQQVESDLESAVEReksywRAELDKRQKLAENELIKIELEKQDVMVL 458
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE-----IEELEELIEELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 459 LETTNDMLRMRDEKLQKCEEQLRNGIDYYIQLSDALQQqlvqlkqdmaktitekynYQLTLTNTRATVNILMERLKksda 538
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQ------------------LELRLEGLEVRIDNLQERLS---- 946
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 17137436 539 dvEQYRAELEsvqlakgALEQSYLVLQADAEQLRQQLTESQDALNAL 585
Cdd:TIGR02168 947 --EEYSLTLE-------EAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-398 |
4.20e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 144 RLKGKEALQYEIRHKNELIESQL----SQLDVLRRHVDQLKEAEAKLREEHELATSKTDRL---IEALTSEnlSHKALNE 216
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKeaieRQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkIKDLGEE--EQLRVKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 217 QMGQEHADL-------------LERLAAMEQQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLS 283
Cdd:TIGR02169 295 KIGELEAEIaslersiaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 284 ALQADVAQAREHCSLEQAKTAENIELVENLQKTNASLLADVVQLKQQ----------IEQDALSYGQEAKSCQAELECLK 353
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEladlnaaiagIEAKINELEEEKEDKALEIKKQE 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17137436 354 VERNTLKNDLA-------NKCTLIRSLQDELLDKNCEIDAHCDTIRQLCREQ 398
Cdd:TIGR02169 455 WKLEQLAADLSkyeqelyDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
139-397 |
6.43e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 139 AKSASRLKGKEALQYEIRHKNELIESQLSQLDV----LRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKAL 214
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 215 NEQMGQEHADLLERLAAMEQqLQQQHDEHERQVEALVAESEALRlanellqtanedrqkveeqlqAQLSALQADVAQARE 294
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEE-LEAQIEQLKEELKALREALDELR---------------------AELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 295 HCSLEQAKTAENIELVENLQKTNASLLADVVQLKQQIEqdalSYGQEAKSCQAELECLKVERNTLKNDLAnkctLIRSLQ 374
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALA----LLRSEL 896
|
250 260
....*....|....*....|...
gi 17137436 375 DELLDKNCEIDAHCDTIRQLCRE 397
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEE 919
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-655 |
2.18e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 154 EIRHKNELIESQLSQLDVLRRH--VDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKALNEQMGQEHADLLERLAA 231
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQrrLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLER 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 232 MEQQLQQQHDEHERQVEALVAESEALRL---------------ANELLQTANEDRQKVEEQ---LQAQLSALQADVAQAR 293
Cdd:COG4913 346 EIERLERELEERERRRARLEALLAALGLplpasaeefaalraeAAALLEALEEELEALEEAlaeAEAALRDLRRELRELE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 294 -EHCSLEQAKTaeNI---------ELVENLQKTNASL--LADVVQLK------------------------QQIEQDALS 337
Cdd:COG4913 426 aEIASLERRKS--NIparllalrdALAEALGLDEAELpfVGELIEVRpeeerwrgaiervlggfaltllvpPEHYAAALR 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 338 Y-----------GQEAKSCQAELECLKVERNTLKNDLANKCTLIRS-LQDELLDkncEIDAHC-DTIRQLCREQarhteq 404
Cdd:COG4913 504 WvnrlhlrgrlvYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwLEAELGR---RFDYVCvDSPEELRRHP------ 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 405 qqavakvqqqvesdleSAVERE----KSYWRAELDKRQKLAENELI------KIElEKQDVMVLLETTNDMLRMRDEKLQ 474
Cdd:COG4913 575 ----------------RAITRAgqvkGNGTRHEKDDRRRIRSRYVLgfdnraKLA-ALEAELAELEEELAEAEERLEALE 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 475 KCEEQLRNGIDYYIQLSDalqqqLVQLKQDMAktitekynyqlTLTNTRATVNILMERLKKSDADVEQYRAELESVQLAK 554
Cdd:COG4913 638 AELDALQERREALQRLAE-----YSWDEIDVA-----------SAEREIAELEAELERLDASSDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 555 GALEQSYLVLQADAEQLRQQLTESQDALNALRSSSQTLQSEERIDGDAQLAHYHELRRKDETREAYMVDMKKALDEfatv 634
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDA---- 777
|
570 580
....*....|....*....|.
gi 17137436 635 lqfAQLELDNKEQMLVKVREE 655
Cdd:COG4913 778 ---LRARLNRAEEELERAMRA 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
274-611 |
2.77e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 274 VEEQLQAQLSALQADVAQAREHCSL-EQAKTAENIELVENLQKtnasLLADVVQLKQQIEQDAlsygQEAKSCQAELECL 352
Cdd:COG1196 194 ILGELERQLEPLERQAEKAERYRELkEELKELEAELLLLKLRE----LEAELEELEAELEELE----AELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 353 KVERNTLKNDLANKCTLIRSLQDELLDKNCEIDAHCDTIRQLCREQARHTEQQQAVAKVQQQVESDLESAVEREksywrA 432
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-----E 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 433 ELDKRQKLAENELIKIELEKQDVMVLLETTNDMLRMRDEKLQKCEEQLRngidyyiqlsdALQQQLVQLKQDMAKTITEK 512
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----------EALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 513 YNYQLTLTNTRATVNILMERLKKSDADVEQYRAELESVQLAKGALEQSYLVLQADAEQLRQQLTESQDALNALRSSSQTL 592
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330
....*....|....*....
gi 17137436 593 QSEERIDGDAQLAHYHELR 611
Cdd:COG1196 490 AARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
160-474 |
3.58e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 160 ELIESQL-SQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKALNEQMGQEHADLLERLAAMEQQLQQ 238
Cdd:COG1196 192 EDILGELeRQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 239 QHDEHERQVEALVAESEALRLANELLQT-------ANEDRQKVEEQLQaQLSALQADVAQAREHCSLEQAKTAENIELVE 311
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARleqdiarLEERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 312 NLQKTNASLLADVVQLKQQIEQDALSYGQEAKSCQAELECLKVERNTLKNDLANKCTLIRSLQDELLDKNCEIDAHCDTI 391
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 392 RQLCREQARHTEQQQAVAKVQQQVESDLESAVEReksywRAELDKRQKLAENELIKIELEKQDVMVLLETTNDMLRMRDE 471
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLEL-----LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
...
gi 17137436 472 KLQ 474
Cdd:COG1196 506 FLE 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-374 |
1.32e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 166 LSQLDVLRRHVDQLKEAEAKLREEHElatsKTDRLIEALTSENLSHKALNEQMGQEHADLLERLAAMEQQLQQQHDEHER 245
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDARE----QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 246 QVEALVAESEALRLANELLQTANEDRQKVEEQLQ----AQLSALQADVAQAREHCSLEQAKTAENIELVENLQKTNASLL 321
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 17137436 322 ADVVQLKQQIEQDALSYGQEAKSCQAELECLKVERNTLKNDLANKCTLIRSLQ 374
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
136-655 |
1.34e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 136 VKEAKSASRLKgkEALQYEIRHKNELIE--SQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKA 213
Cdd:PTZ00121 1193 LRKAEDARKAE--AARKAEEERKAEEARkaEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA 1270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 214 LNEQMGQEHADLLERLAAMEQQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEE-QLQAQLSALQADVAQA 292
Cdd:PTZ00121 1271 AIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAaKKKAEEAKKAAEAAKA 1350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 293 REHCSLEQAKTAENIELVENLQKTNASLLADVVQLKQQIEQDALSYGQEAKSCQAELECL-KVERNTLKNDLANKCTLIR 371
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELkKAAAAKKKADEAKKKAEEK 1430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 372 SLQDElLDKNCEIDAHCDTIRQLCrEQARHTEQQQAVAKVQQQVESDLESAVEREKSYWRAELDKRQKLAENELIKIELE 451
Cdd:PTZ00121 1431 KKADE-AKKKAEEAKKADEAKKKA-EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 452 KQdvmvllettndmlrmRDEKLQKCEEQLRngidyyiqlSDALQQQLVQLKQDMAKTITEKynyqltltnTRATVNILME 531
Cdd:PTZ00121 1509 KK---------------KADEAKKAEEAKK---------ADEAKKAEEAKKADEAKKAEEK---------KKADELKKAE 1555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 532 RLKKSDadveqyraELESVQLAKGALEQSYLVLQAdAEQLRQQLTESQDALNALRSSSQTLQSEERIDGDAQLAHYHELR 611
Cdd:PTZ00121 1556 ELKKAE--------EKKKAEEAKKAEEDKNMALRK-AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 17137436 612 RKDETREAYMVDMKKALDEFATVLQFAQLELDNK---EQMLVKVREE 655
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaAEEAKKAEED 1673
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
160-349 |
2.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 160 ELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRL--IEALTSENLSHKALNEqmgqEHADLLERLAAME---- 233
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVASAER----EIAELEAELERLDassd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 234 --QQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSAL-----QADVAQAREHCSLEQAKTAEN 306
Cdd:COG4913 686 dlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAedlarLELRALLEERFAAALGDAVER 765
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 17137436 307 iELVENLQKTNASLLADVVQLKQQIEQDALSYGQEAKSCQAEL 349
Cdd:COG4913 766 -ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADL 807
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-361 |
2.89e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 154 EIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREehelatskTDRLIEALTSENLSHK-ALNEQMGQEHADLLERLAAM 232
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAE--------LEYLRAALRLWFAQRRlELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 233 EQQLQQQHDEHERQVEALvaESEALRLANELLQTANEDRqkveEQLQAQLSALQADVAQAREHCSLEQAKTAENIELVEN 312
Cdd:COG4913 311 LERLEARLDALREELDEL--EAQIRGNGGDRLEQLEREI----ERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 17137436 313 LQKTNASLLADVVQLKQQIEQDALSYGQEAKSCQAELECLKVERNTLKN 361
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
138-335 |
4.24e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 138 EAKSASRLKGKEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALtSENLSHKALNEQ 217
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL-YRLGRQPPLALL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 218 MGQEHADLLERLAAMEQQLQQQHDEherQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAREHCS 297
Cdd:COG4942 126 LSPEDFLDAVRRLQYLKYLAPARRE---QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202
|
170 180 190
....*....|....*....|....*....|....*...
gi 17137436 298 LEQAKTAENIELVENLQKTNASLLADVVQLKQQIEQDA 335
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
167-338 |
1.05e-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: 46.10 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 167 SQLDVLRRHVDQLKEAEAKLREEHElatsKTDRLIEALTSENLSHK--ALNEQMGQEHADLLERLAAMEQQLQQQHDEHE 244
Cdd:COG3096 785 KRLEELRAERDELAEQYAKASFDVQ----KLQRLHQAFSQFVGGHLavAFAPDPEAELAALRQRRSELERELAQHRAQEQ 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 245 RQVEALVAESEALRLANELLQTAN----EDRQKVEEQLQAQLSALQADVAQAREHCsleqaKTAENIE-LVENLQKT--- 316
Cdd:COG3096 861 QLRQQLDQLKEQLQLLNKLLPQANlladETLADRLEELREELDAAQEAQAFIQQHG-----KALAQLEpLVAVLQSDpeq 935
|
170 180
....*....|....*....|....*..
gi 17137436 317 NASLLADVVQLKQQIEQ-----DALSY 338
Cdd:COG3096 936 FEQLQADYLQAKEQQRRlkqqiFALSE 962
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
137-489 |
1.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 137 KEAKSASRLKGKEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKALNE 216
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 217 QMGQEHADLLERLAAMEQQLQQQHDEHERqvealvAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAREHc 296
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEE------LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSL- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 297 sleqaktAENIELVENLQKTNASLLADVVQLKQQIEQDALSYGQEAKSCQAELECLKVERNTLKNDLANKCTLIRSLQDE 376
Cdd:COG4717 269 -------LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 377 LLDKNCEIDAHCDTIRQLCRE---QARHTEQQQAVAKVQQQVESDLESAVEREKSYwrAELDKRQKLAENELIKIELEKQ 453
Cdd:COG4717 342 LLDRIEELQELLREAEELEEElqlEELEQEIAALLAEAGVEDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELE 419
|
330 340 350
....*....|....*....|....*....|....*.
gi 17137436 454 DVMVLLETtnDMLRMRDEKLQKCEEQLRNGIDYYIQ 489
Cdd:COG4717 420 ELLEALDE--EELEEELEELEEELEELEEELEELRE 453
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
129-593 |
2.79e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 129 HSAATTPVKEAKSASRLKGK------EALQYEIRHKNELIESQLSQLDvlrRHVDQLKeaeAKLREEHELATSKTDRLIE 202
Cdd:pfam15921 276 HEVEITGLTEKASSARSQANsiqsqlEIIQEQARNQNSMYMRQLSDLE---STVSQLR---SELREAKRMYEDKIEELEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 203 AL---TSENLSHKALNEQMGQEHADLLERLAAMEQQLQQQHDE---HERQVEALVAESEALRLANELLQTANEDRQKVEE 276
Cdd:pfam15921 350 QLvlaNSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKElslEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 277 QLQAQLSALQADV-AQAREHCSLEQAKTaENIELVENLQ---KTNASLLADVVQ----LKQQIEQDALSYGQEAKSCQAE 348
Cdd:pfam15921 430 RLEALLKAMKSECqGQMERQMAAIQGKN-ESLEKVSSLTaqlESTKEMLRKVVEeltaKKMTLESSERTVSDLTASLQEK 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 349 ---LECLKVERNTLKNDLANKCTLIRSLQDELlDKNCEIDAHCDTIRQLCREQARHTEQQQAVAKVQQQ---VESDLESA 422
Cdd:pfam15921 509 eraIEATNAEITKLRSRVDLKLQELQHLKNEG-DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQlvgQHGRTAGA 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 423 VEREKSYWRAEL-DKRQKLAENELIKielEKQDVMVL-LETTNDMLRMRDEKLQKCEEQLRNGIDYYIQLSDALQQQLVQ 500
Cdd:pfam15921 588 MQVEKAQLEKEInDRRLELQEFKILK---DKKDAKIReLEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKT 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 501 LKQDMaKTITEKY-----NYQLTLTNTRATVNILMERLKKSDADVEQYRAELESVQLAKGALEQSYLVLQadaeqlrQQL 575
Cdd:pfam15921 665 SRNEL-NSLSEDYevlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ-------KQI 736
|
490
....*....|....*...
gi 17137436 576 TESQDALNALRSSSQTLQ 593
Cdd:pfam15921 737 TAKRGQIDALQSKIQFLE 754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
316-669 |
3.18e-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: 44.28 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 316 TNASLLADVVQLKQQIEQDALSygQEAKSCQAELECLKVERNTLKNDLANKCTLIRSLQDELLDKNCEIDAHCDTIRQLC 395
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELE--EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 396 REQARHTEQQQAVAKVqqqvesdlesavereksywRAELDKRQKLAENELIKIELEKQDVMVLLETTNDMLRMRDEKLQK 475
Cdd:TIGR02168 740 AEVEQLEERIAQLSKE-------------------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 476 CEEQLrngidyyiqlsDALQQQLVQLKQDMAKTITEKYNYQLTLTNTRATVNILMERLKKSDADVEQYRAELESvqlakg 555
Cdd:TIGR02168 801 LREAL-----------DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE------ 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 556 aLEQSYLVLQADAEQLRQQLTESQDALNALRSSSQTLQSEERIDGDAQLAHYHELRRKDETREAYMVDMKKALDEFATVL 635
Cdd:TIGR02168 864 -LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
330 340 350
....*....|....*....|....*....|....*...
gi 17137436 636 QF----AQLELDNKEQMLVKVREECEQLKLENIALKSK 669
Cdd:TIGR02168 943 ERlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
167-337 |
4.38e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 167 SQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKALNEqmgqEHADLLERLAAMEQQLQQQHDehERQ 246
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL----EIEEVEARIKKYEEQLGNVRN--NKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 247 VEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAREHcslEQAKTAENIELVENLQKTNASLLADVVQ 326
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEELEAEREE 167
|
170
....*....|.
gi 17137436 327 LKQQIEQDALS 337
Cdd:COG1579 168 LAAKIPPELLA 178
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
218-433 |
4.47e-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: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 218 MGQEHADLLERLAAMEQQLQQQHDEHERQVEALVAESEAL---RLANELLQTANEDRQKVeEQLQAQLSALQADVAQARe 294
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALqerREALQRLAEYSWDEIDV-ASAEREIAELEAELERLD- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 295 hcsleqaktAENIELvENLQKTNASLLADVVQLKQQIEQdalsYGQEAKSCQAELECLKVERNTLKNDLANKCTLIRSLQ 374
Cdd:COG4913 682 ---------ASSDDL-AALEEQLEELEAELEELEEELDE----LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 17137436 375 DELLDKNCEiDAHCDTIRQLCREQARhtEQQQAVAKVQQQVESDLESAVEREKSYWRAE 433
Cdd:COG4913 748 RALLEERFA-AALGDAVERELRENLE--ERIDALRARLNRAEEELERAMRAFNREWPAE 803
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
112-344 |
5.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 112 TATGSGSGASTAASTPLHSAATTPVKEAKS--ASRLKGKEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREE 189
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAelEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 190 HELATSKTDRLIEALTSENLSHKALNEQMGQEH-ADLLERLAAMEQQLQQQHDEherqVEALVAESEALRLANELLQTAN 268
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADL----LEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17137436 269 EDRQKVEEQLQAQLSALQADVAQAREHCSLEQAKTAENIELVENLQKTNASLLADVVQLKQQIEQDALSYGQEAKS 344
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
173-280 |
6.91e-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: 43.40 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 173 RRHVDQLKEAEAKLREEHELATSKTDRLIEalTSENLSHKALNEQM-GQEHADLLERLAAMEQQLQQQhDEHERQVEALV 251
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLVE--MARELEELSARESDlEQDYQAASDHLNLVQTALRQQ-EKIERYQEDLE 357
|
90 100
....*....|....*....|....*....
gi 17137436 252 AESEALRLANELLQTANEDRQKVEEQLQA 280
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEA 386
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
119-361 |
8.82e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 119 GASTAASTPLHSAATTPVKEAKSASRLKGKEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTD 198
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 199 RLIEALTSENLSHKALNEQMGQehadLLERLAAMEQQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQL 278
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAA----LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 279 QAQLSALQADVAQAREHCSLEQAKTAENIELVENLQKtnasLLADVVQLKQQIEQ------DALsygQEAKSCQAELECL 352
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE----LERELERLEREIEAlgpvnlLAI---EEYEELEERYDFL 800
|
....*....
gi 17137436 353 KVERNTLKN 361
Cdd:COG1196 801 SEQREDLEE 809
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
162-375 |
1.43e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.88 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 162 IESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTseNLSHKalNEQMGQehadLLERLAAMEQQLQQQHD 241
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLA--SLKHE--NDNLSS----MLNRKERRLKDLEDQLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 242 EHERQVEALVAESEALR-LANELLQTANEDRQKVeEQLQAQLSALQADVAQAREHCSLEQAKTAENIELVE-NLQKTNAS 319
Cdd:pfam17078 77 ELKNSYEELTESNKQLKkRLENSSASETTLEAEL-ERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKlENEKQLEN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17137436 320 LLADVVQLKQQIEQDALSYGQEAKscqaELECLKVERNtlkNDLANKCTLIRSLQD 375
Cdd:pfam17078 156 YQQRISSNDKDIDTKLDSYNNKFK----NLDNIYVNKN---NKLLTKLDSLAQLLD 204
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
223-363 |
1.43e-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: 41.06 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 223 ADLLERLAAMEQQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQA-----QLSALQADVAQAREHCS 297
Cdd:COG1579 27 KELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkEYEALQKEIESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17137436 298 LEQAKTAENIELVENLQKTNASLLADVVQLKQQIEQDALSYGQEAKSCQAELECLKVERNTLKNDL 363
Cdd:COG1579 107 DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
148-659 |
1.67e-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: 41.97 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 148 KEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENlshkalNEQmgQEHADLLE 227
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN------NEI--ERLEARLE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 228 RLAAMEQQLQQQHDEHER-----QVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAREHCSLEQAK 302
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKkleeaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 303 TAENIELVENLQ---------KTNASLLADVV-QLKQQIEQDAlSYGQE-AKSCQAELECLKVER--------NTLKNDL 363
Cdd:TIGR02168 491 LDSLERLQENLEgfsegvkalLKNQSGLSGILgVLSELISVDE-GYEAAiEAALGGRLQAVVVENlnaakkaiAFLKQNE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 364 ANKCTLIrslqdeLLDknceiDAHCDTIRQLCREQARHTEQQQAVAKVQQQVESDLESAVerekSYW----------RAE 433
Cdd:TIGR02168 570 LGRVTFL------PLD-----SIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL----SYLlggvlvvddlDNA 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 434 LDKRQKLAENELIkIELE--------------KQDVMVLLETTNDMLRMRdEKLQKCEEQLRNG----IDYYIQLSDALQ 495
Cdd:TIGR02168 635 LELAKKLRPGYRI-VTLDgdlvrpggvitggsAKTNSSILERRREIEELE-EKIEELEEKIAELekalAELRKELEELEE 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 496 QQLV--QLKQDMAKTITEKYNYQLTLTNTRATVNILMERLKKSDADVEQYRAE----LESVQLAKGALEQSYLVLQADAE 569
Cdd:TIGR02168 713 ELEQlrKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEleerLEEAEEELAEAEAEIEELEAQIE 792
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 570 QLRQQLTESQDALNALRSSSQTLqseeRIDGDAQLAHYHELRRKDETREAYMVDMKKALDEFATVLQFAQLELDNKEQML 649
Cdd:TIGR02168 793 QLKEELKALREALDELRAELTLL----NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
570
....*....|
gi 17137436 650 VKVREECEQL 659
Cdd:TIGR02168 869 EELESELEAL 878
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
171-662 |
2.07e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 171 VLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTseNLSHKALNEQMGQEhadlleRLAAMEQQLQQQHDEHERQVEAL 250
Cdd:pfam15921 79 VLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVI--DLQTKLQEMQMERD------AMADIRRRESQSQEDLRNQLQNT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 251 VAESEALRLANELLQtanEDRQKVEEQLQAQLSALQADVAQAREHCSLEQAKTAENIELVENLQKTN-ASLLADVVQLKQ 329
Cdd:pfam15921 151 VHELEAAKCLKEDML---EDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHfRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 330 QIEQDALSYGQEAKSCQAELECLKVE-RNTLKNDLANKCTLIRSLQDE-------LLDKNCEIDAHCDTIR---QLCREQ 398
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSEsQNKIELLLQQHQDRIEQLISEheveitgLTEKASSARSQANSIQsqlEIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 399 ARHTEQQQAVAKvqqqveSDLESAVerekSYWRAELDKRQKLAENELIkiELEKQDVMVLLETTndmlRMRDEKLQKCEE 478
Cdd:pfam15921 308 ARNQNSMYMRQL------SDLESTV----SQLRSELREAKRMYEDKIE--ELEKQLVLANSELT----EARTERDQFSQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 479 QlrNGIDYYIQ--LSDALQQQLVQlkqdmakTITEKYNYQLTLTNTRATVNI--LMERLKKSDADVEQYRAELESVQL-A 553
Cdd:pfam15921 372 S--GNLDDQLQklLADLHKREKEL-------SLEKEQNKRLWDRDTGNSITIdhLRRELDDRNMEVQRLEALLKAMKSeC 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 554 KGALEQSYLVLQADAEQLRQ------QLTESQDAL----NALRSSSQTLQSEERIDGDAQlAHYHELRRKDETREAYMVD 623
Cdd:pfam15921 443 QGQMERQMAAIQGKNESLEKvssltaQLESTKEMLrkvvEELTAKKMTLESSERTVSDLT-ASLQEKERAIEATNAEITK 521
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 17137436 624 MKKALDefatvLQFAQLE-LDNKEQMLVKVREECEQLKLE 662
Cdd:pfam15921 522 LRSRVD-----LKLQELQhLKNEGDHLRNVQTECEALKLQ 556
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
136-331 |
3.16e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 136 VKEAKSASRLKGKEALQYEIrhkNELIESQLSQ--LDVLRRHVDQLKEAEAKLREEhelatSKTDRLIEALTSENLSHKA 213
Cdd:PRK10929 35 AKAAKTPAQAEIVEALQSAL---NWLEERKGSLerAKQYQQVIDNFPKLSAELRQQ-----LNNERDEPRSVPPNMSTDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 214 LNEQMGQEHADLLERlaamEQQLQQQHDEHERQVEALVA----ESEALRLANEL---LQTANEDRQKVEeqlQAQLSALQ 286
Cdd:PRK10929 107 LEQEILQVSSQLLEK----SRQAQQEQDRAREISDSLSQlpqqQTEARRQLNEIerrLQTLGTPNTPLA---QAQLTALQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 17137436 287 ADVAQAR---EHCSLEQAKTAENIEL----VENLQKTNASLLADVVQLKQQI 331
Cdd:PRK10929 180 AESAALKalvDELELAQLSANNRQELarlrSELAKKRSQQLDAYLQALRNQL 231
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
189-329 |
3.46e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.33 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 189 EHELA--TSKTDRLIEALTSENLSHKALNEQMGQEHADLLERLAAMEQqLQQQHDEHERQVEAlvAESEALRLANELL-- 264
Cdd:PRK09039 52 DSALDrlNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSR-LQALLAELAGAGAA--AEGRAGELAQELDse 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17137436 265 -QTANEDRQKVEeQLQAQLSALQADVAQAREHCSLEQAKTAENIELVENL-QKTNASLLADVVQLKQ 329
Cdd:PRK09039 129 kQVSARALAQVE-LLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRLNVALAQRVQELNR 194
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
162-289 |
4.21e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 40.84 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 162 IESQLSQLDVLRRHVDQLKEAEAKLREEHELATSktDRLiealtsenlshkalnEQMGQEHADLLERLAAMEQQLQQQHD 241
Cdd:COG0542 406 IDSKPEELDELERRLEQLEIEKEALKKEQDEASF--ERL---------------AELRDELAELEEELEALKARWEAEKE 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 17137436 242 EherqVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADV 289
Cdd:COG0542 469 L----IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
202-293 |
4.23e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 202 EALTSENLSHKALNEQMGQEHADLLERLAAMEQQLQQQHD---EHERQVEALVAESEALRLANEllQTANEDRQKVEEQL 278
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGlaaELEEKQQELEAQLEQLQEKAA--ETSQERKQKRKEIT 222
|
90
....*....|....*
gi 17137436 279 QAQLSALQADVAQAR 293
Cdd:PRK11448 223 DQAAKRLELSEEETR 237
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
515-672 |
4.80e-03 |
|
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: 40.10 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 515 YQLTLTNTRATVNILMERLKKSDADVEQYRAE---LESVQLAKGALEQSYLVLQADAEQLRQQLTESQDALNALRS---- 587
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAEldrLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIdlar 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 588 ----------SSQTLQSEERIDGDAQLAHYHELRRKDETREAYMVDMKKALDEFATVLQFAQLELDNKEQMLVKVREEce 657
Cdd:pfam00529 129 rrvlapiggiSRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLD-- 206
|
170
....*....|....*
gi 17137436 658 qlkLENIALKSKQPG 672
Cdd:pfam00529 207 ---LERTEIRAPVDG 218
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
162-352 |
5.13e-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: 40.58 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 162 IESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKALNEQMGQEHADLLERLAAMEQQLQqqhd 241
Cdd:pfam10174 403 IENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENK---- 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 242 EHERQVEALVAE-SEALRLANELLQTANEDRQKVEEQlQAQLSALQADVAQAREHCS--LEQAKTAENIELVENLQktna 318
Cdd:pfam10174 479 DLKEKVSALQPElTEKESSLIDLKEHASSLASSGLKK-DSKLKSLEIAVEQKKEECSklENQLKKAHNAEEAVRTN---- 553
|
170 180 190
....*....|....*....|....*....|....
gi 17137436 319 sllADVVQLKQQIEQDALSYGQEAKSCQAELECL 352
Cdd:pfam10174 554 ---PEINDRIRLLEQEVARYKEESGKAQAEVERL 584
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
128-647 |
5.64e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 128 LHSAATTPV--KEAKSASRLKGKEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALT 205
Cdd:TIGR00618 297 AHIKAVTQIeqQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 206 senLSHKALNEQMGQEHADLLERLAAmeqQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSAL 285
Cdd:TIGR00618 377 ---LTQHIHTLQQQKTTLTQKLQSLC---KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 286 QADVAQAREHCSLEQAKTAENIELVENLQktnaSLLADVVQLKQQIEQDALSYGQEAKSCQAELECLKVERNTLKNDLAN 365
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKE----QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPL 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 366 KCTLIRSLQDelLDKNCEIDAHCDTIRQLCREQARHTEQQQAVAKVQQQVESDLESAVEREKSYWRAELDKRQKLAENEL 445
Cdd:TIGR00618 527 TRRMQRGEQT--YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLS 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 446 ---IKIELEKQDVMVLLETTNDMLRMRDEKLQKCEEQlrngidyyiqlsdalqqqlvqlkqdmAKTITEKYNYQLTLTNT 522
Cdd:TIGR00618 605 eaeDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQEL--------------------------ALKLTALHALQLTLTQE 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 523 RATVNILMER------LKKSDADVEQYRAELESVQLAKGALEQSYLVLQADAEQLRQQLTESQDALNALRSSSQTLQSEE 596
Cdd:TIGR00618 659 RVREHALSIRvlpkelLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 17137436 597 RIDGDAQLAHYHELRRK-DETREAYMVDMKKALDEFATVLQFAQLELDNKEQ 647
Cdd:TIGR00618 739 DALNQSLKELMHQARTVlKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
220-311 |
5.75e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.32 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 220 QEHADLLERLAAMEQQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAREHCSLE 299
Cdd:PRK11448 142 NLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEI 221
|
90
....*....|..
gi 17137436 300 QAKTAENIELVE 311
Cdd:PRK11448 222 TDQAAKRLELSE 233
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
146-453 |
7.32e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 7.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 146 KGKEALQYEIRHKNELIESQLSQLDVLRRHVDQLKEAEAKLREEHELATSKTDRLIEALTSENLSHKALNEQMGQEHADL 225
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 226 LERLAAMEQQLQQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSALQADVAQAREHCS---LEQAK 302
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKekkKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 303 TAENIELVENLQKTNASLLADVVQLKQQIEQDALSYGQEAKSCQAELECLKVERNTLKNDlankctlIRSLQDELLDKNC 382
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA-------AKLKEEELELKSE 402
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17137436 383 EIDAHCDTIRQLCREQARHTEQQQAVAKVQQQVESDLESAVEREKSYWRAELDKRQKLAENELIKIELEKQ 453
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
216-333 |
8.41e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.94 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 216 EQMGQEHADLLERLAAMEQQLQQQHDEhERQVEALVAESEALRL-ANELLQTANEDR---QKVEEQLQAQLS-------- 283
Cdd:PRK04863 526 EQRLRQQQRAERLLAEFCKRLGKNLDD-EDELEQLQEELEARLEsLSESVSEARERRmalRQQLEQLQARIQrlaarapa 604
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17137436 284 --ALQADVAQAREHCSLEQAKTAENIELVENLQKTNASLLADVVQLKQQIEQ 333
Cdd:PRK04863 605 wlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
164-294 |
9.36e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 164 SQLSQL-DVL---RRHVDQLKEAEAKLREEHELATSKTDRLiealtsenlshKALNEQMGQEHADLLERLAAMEQQL--- 236
Cdd:PRK09039 60 SQIAELaDLLsleRQGNQDLQDSVANLRASLSAAEAERSRL-----------QALLAELAGAGAAAEGRAGELAQELdse 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17137436 237 QQQHDEHERQVEALVAESEALRLANELLQTANEDRQKVEEQLQAQLSAL--QADVAQARE 294
Cdd:PRK09039 129 KQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgrRLNVALAQR 188
|
|
| |
