|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
289-519 |
4.18e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 289 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSF 367
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 368 LREREMLLEEARMLKRDLEREQLTAMALRAELEqfipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLw 447
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL- 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 557440739 448 erlyveAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKE 519
Cdd:COG1196 406 ------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
252-457 |
4.43e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 252 DELDGVKGYLSQRKqeqESFLDFKSLKENLERCwtvtesEKITFEtQKKNLAaenqylriSLEKE-EQALS--SLQEELR 328
Cdd:COG1196 162 EEAAGISKYKERKE---EAERKLEATEENLERL------EDILGE-LERQLE--------PLERQaEKAERyrELKEELK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 329 QLREQIRLLEDKGTSTQLVRENQVLKQyLEVEKQKTDSFLREREMLLEEARmLKRDLEREQLTAM-----ALRAELEQFI 403
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAELEAELEELR-LELEELELELEEAqaeeyELLAELARLE 301
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 557440739 404 PGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQ 457
Cdd:COG1196 302 QDIARLEERRRELEERLEE---LEEELAELEEELEELEEELEELEEELEEAEEE 352
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
275-437 |
7.99e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 275 KSLKENLercwTVTESEK-----ITFETQKKNLAAE------NQYLRISLEKE----EQALSSLQEELRQLREQIRLLED 339
Cdd:COG3206 121 ERLRKNL----TVEPVKGsnvieISYTSPDPELAAAvanalaEAYLEQNLELRreeaRKALEFLEEQLPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 340 KgtstqlvrenqvLKQYleveKQKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAELEQFI----------PGQAQS 409
Cdd:COG3206 197 A------------LEEF----RQKNGLVDLSEEAKLLLQQL--SELESQLAEARAELAEAEARLaalraqlgsgPDALPE 258
|
170 180
....*....|....*....|....*...
gi 557440739 410 RAESPSVQTEEKEVGLLQQRLAELEQKL 437
Cdd:COG3206 259 LLQSPVIQQLRAQLAELEAELAELSARY 286
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
297-449 |
1.64e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.22 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 297 TQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVlkqyleVEKQKTDSFLREREMLLE 376
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQA------AELAELTRRLAELETQLD 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 557440739 377 EARMLKRDLEREQLTAMALRAELEqfipgqAQSRAESPSVQTEEKEVGL----LQQRLAELEQKLIfeQQRSDLWER 449
Cdd:pfam19220 206 ATRARLRALEGQLAAEQAERERAE------AQLEEAVEAHRAERASLRMkleaLTARAAATEQLLA--EARNQLRDR 274
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
261-530 |
3.31e-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: 50.84 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 261 LSQRKQEQESFLDFKSLKENLErcWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQ---EELRQLREQI-RL 336
Cdd:TIGR02169 203 LRREREKAERYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEkrlEEIEQLLEELnKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 337 LEDKGTSTQL-------------------VRENQVLKQYLEVEKQKTDSflrEREMLLEEARMLKRDLEREQLTAMALRA 397
Cdd:TIGR02169 281 IKDLGEEEQLrvkekigeleaeiaslersIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 398 ELEQFIPGQAQSRAEspsVQTEEKEVGLLQQRLAELEQKLifeqqrSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAK 477
Cdd:TIGR02169 358 EYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKL------EKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 557440739 478 SKSKET----FLGTVKETFDAMKNSTKEF--VRHHKEKIKQAKEAVKENLKKFSDSVKS 530
Cdd:TIGR02169 429 IAGIEAkineLEEEKEDKALEIKKQEWKLeqLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
298-457 |
1.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 298 QKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSfLREREMLLEE 377
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE-LEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 378 ARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEE--KEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAK 455
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
..
gi 557440739 456 DQ 457
Cdd:COG4717 241 LE 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-450 |
3.18e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 262 SQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG 341
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 342 TSTQL-VRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQltamaLRAELEQFIPGQAQSRAESPSVQTEE 420
Cdd:TIGR02168 396 ASLNNeIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE-----LEEELEELQEELERLEEALEELREEL 470
|
170 180 190
....*....|....*....|....*....|
gi 557440739 421 KEvglLQQRLAELEQKLIFEQQRSDLWERL 450
Cdd:TIGR02168 471 EE---AEQALDAAERELAQLQARLDSLERL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
260-533 |
4.18e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 260 YLSQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED 339
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 340 KGTSTQ-----LVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLE-------REQLTAMALRAELEQFipgQA 407
Cdd:TIGR02168 825 RLESLErriaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEEL---SE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 408 QSRAESPSVQTEEKEVGLLQQRLAELEQKLI-FEQQRSDLWERLYVEAKD--QHGKQETDGRKRGSRGSHR--AKSKSKE 482
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRrlKRLENKI 981
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 557440739 483 TFLGTVkeTFDAM-----KNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFR 533
Cdd:TIGR02168 982 KELGPV--NLAAIeeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
264-601 |
4.53e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 264 RKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAEN-QYLRISLEKEEQALSSLQEELRQLR-EQIRLLED-K 340
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEaK 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 341 GTSTQLVRENQV------LKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQfipgqaQSRAESP 414
Cdd:PTZ00121 1620 IKAEELKKAEEEkkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEA 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 415 SVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlYVEAKDQHGKQETDGRKrgsrgSHRAKSKSKETflgtvKETFDA 494
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN-KIKAEEAKKEAEEDKKK-----AEEAKKDEEEK-----KKIAHL 1762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 495 MKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGSKRFRAPKEAATEKTRTAYSYSSYS 572
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842
|
330 340 350
....*....|....*....|....*....|.
gi 557440739 573 QQEAP--NQNQNCRRPSAQRDGGREKPSHSE 601
Cdd:PTZ00121 1843 LEEADafEKHKFNKNNENGEDGNKEADFNKE 1873
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
239-482 |
5.98e-05 |
|
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: 46.66 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 239 IQIQKQLVRKTHEDELDgvkgylsqrKQEQESFLDFKSLK-ENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEE 317
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE---------KMEQERLRQEKEEKaREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 318 QALSSLQEELRQLREQIRLlEDKGTSTQLVREnqvlKQYLEVEKQKTDSFLRERemlLEEARMLKRDLEREQLTAMALRA 397
Cdd:pfam17380 349 ELERIRQEERKRELERIRQ-EEIAMEISRMRE----LERLQMERQQKNERVRQE---LEAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 398 ELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlyveaKDQHGKQETDGRKRGSRGSHRAK 477
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLELEKEKRDRKRAEEQRRK 495
|
....*
gi 557440739 478 SKSKE 482
Cdd:pfam17380 496 ILEKE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
240-446 |
6.94e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 6.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 240 QIQKQLVRKthEDELDGVKGYLSQRKQEQESFLDfkSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQA 319
Cdd:TIGR02169 241 AIERQLASL--EEELEKLTEEISELEKRLEEIEQ--LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 320 LSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVE-------------------------KQKTDSFLREREM 373
Cdd:TIGR02169 317 LEDAEERLAKLEAEIdKLLAEIEELEREIEEERKRRDKLTEEyaelkeeledlraeleevdkefaetRDELKDYREKLEK 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557440739 374 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLifEQQRSDL 446
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED---KALEIKKQEWKL--EQLAADL 464
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
252-426 |
8.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 252 DELDGVKGYLSQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKE--EQALSSLQEELRQ 329
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEalEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 330 LREQIRLLEDKGTS-TQLVRENQVLKQYLEVEKQKTD--------SFLREREMLLEEARMLKRDLEREQLTAMALRAELE 400
Cdd:COG4717 151 LEERLEELRELEEElEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180
....*....|....*....|....*.
gi 557440739 401 QFipgQAQSRAESPSVQTEEKEVGLL 426
Cdd:COG4717 231 QL---ENELEAAALEERLKEARLLLL 253
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
298-437 |
1.07e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 298 QKKNLAAENQYLR--ISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQlVRENQVLKQYLEVEKQKTDSFLREREMLL 375
Cdd:COG4913 266 AARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLE-ARLDALREELDELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 557440739 376 EEARMLKRDLER---------EQLTAMALRAEL--EQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKL 437
Cdd:COG4913 345 REIERLERELEErerrrarleALLAALGLPLPAsaEEFAALRAEAAALLEALEEELEA---LEEALAEAEAAL 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
257-437 |
1.18e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 257 VKGYLSQRKQEQESFLDF-----KSLKENLERcwtvTESEKITFETQKK--NLAAENQYLRISLEKEEQALSSLQEELRQ 329
Cdd:COG3206 162 LEQNLELRREEARKALEFleeqlPELRKELEE----AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 330 LREQIRLLEDK----GTSTQLVRENQVLKQYLEvekqktdsflREREMLLEEARMLKRDLER--EQLTAMALRAELEQFI 403
Cdd:COG3206 238 AEARLAALRAQlgsgPDALPELLQSPVIQQLRA----------QLAELEAELAELSARYTPNhpDVIALRAQIAALRAQL 307
|
170 180 190
....*....|....*....|....*....|....*.
gi 557440739 404 PGQAQSRAESPSVQTE--EKEVGLLQQRLAELEQKL 437
Cdd:COG3206 308 QQEAQRILASLEAELEalQAREASLQAQLAQLEARL 343
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
300-462 |
1.19e-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: 45.82 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 300 KNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG--TSTQLVRENQVLKQYL-EVEK--QKTDSFLREREML 374
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLEaEVEQleERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 375 LEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTE----EKEVGLLQQRLAELEQKLIFEQQRSDLWERL 450
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170
....*....|..
gi 557440739 451 YVEAKDQHGKQE 462
Cdd:TIGR02168 840 LEDLEEQIEELS 851
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
288-465 |
1.45e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 288 TESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--------------------------- 340
Cdd:COG4942 46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqkeelaellralyrlgrqpplall 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 341 ---GTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEearmLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQ 417
Cdd:COG4942 126 lspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----LRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 557440739 418 TE-EKEVGLLQQRLAELEQKlifEQQRSDLWERLYVEAKDQHGKQETDG 465
Cdd:COG4942 202 ARlEKELAELAAELAELQQE---AEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
314-434 |
2.55e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 314 EKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAM 393
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 557440739 394 ALRAELEQFIPGqAQSRAESPSVQTEEKEVGLLQQRLAELE 434
Cdd:COG1196 741 LLEEEELLEEEA-LEELPEPPDLEELERELERLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
313-531 |
2.55e-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: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 313 LEKEEQALSSLQEELRQLREQIRLLEdkgtstqlvRENQVLKQYLEVEKQKTD-----------SFLREREMLLEEARML 381
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLE---------RQAEKAERYKELKAELRElelallvlrleELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 382 KRDLEREQLTAMALRAELEQFipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQhgkQ 461
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEEL---RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ---L 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 462 ETDGRKRGSRgshRAKSKSKETFLGTVKETFDAMKNSTKEFvRHHKEKIKQAKEAVKENLKKFSDSVKST 531
Cdd:TIGR02168 326 EELESKLDEL---AEELAELEEKLEELKEELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQL 391
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
296-462 |
2.57e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 296 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-KGTSTQLVRENQVLKQYLEVEKQ-----KTDSFLR 369
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAElerldASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 370 EREMLLEEARMLKRDLEREQLTAMALRAELEQFIPG------QAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQR 443
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQaeeeldELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170
....*....|....*....
gi 557440739 444 SDLWERLYVEAKDQHGKQE 462
Cdd:COG4913 769 ENLEERIDALRARLNRAEE 787
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
299-519 |
2.92e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 299 KKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTstQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEA 378
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--QLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 379 RMLKRDLEREQLTAMALRAELE--------QFIPgqaQSRAESPSVqteEKEVGLLQQRLAELEQKLIFEQQRSDLWERL 450
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNdlearlshSRIP---EIQAELSKL---EEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557440739 451 YVEAKDQhgKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEF------VRHHKEKIKQAKEAVKE 519
Cdd:TIGR02169 835 IQELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLRELERKIEE 907
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
296-468 |
3.10e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 296 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--GTSTQLVRENQVLKQYLEVEKQKTDSFLREREM 373
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 374 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLifEQQRSDLwERLYVE 453
Cdd:COG4942 106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL--EAERAEL-EALLAE 182
|
170
....*....|....*
gi 557440739 454 AKDQHGKQETDGRKR 468
Cdd:COG4942 183 LEEERAALEALKAER 197
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
86-232 |
3.43e-04 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 44.21 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 86 EVEEAPSPEDNVYfGTTSDDSDI---VTLEPPKleemgnQEVTIQEAPSSDDLNMGSSSSSQYAFCQPE-----PVFSSQ 157
Cdd:PLN02328 4 ETKEPEDPADNVN-DVVSEASSPetdLSLSPSQ------SEQNIENDGQNSPETQSPLTELQPSPLPPNttldaPVSDSQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 158 PSDEES---SSDDTSHEPSPAPRRRRNRKKTVSiseseepplaepedEPSKEPS-KRHFSR-GLNKCVILALVIAVSMGF 232
Cdd:PLN02328 77 GDESSSeqqPQNPNSTEPAPPPKKRRRRKRFFT--------------EINANPAfRRHRVRgGLGKEVDVEALIAISVGF 142
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
253-446 |
4.23e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 253 ELDGVKGYLSQRKQEQESFLDfkSLKENLERCwtvtesekitfETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 332
Cdd:pfam07888 133 ELEEDIKTLTQRVLERETELE--RMKERAKKA-----------GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRN 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 333 qirLLEDKGTSTQLVREN-QVLKQYLEVEKQKTdsflREREMLLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRA 411
Cdd:pfam07888 200 ---SLAQRDTQVLQLQDTiTTLTQKLTTAHRKE----AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQA 272
|
170 180 190
....*....|....*....|....*....|....*..
gi 557440739 412 E--SPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDL 446
Cdd:pfam07888 273 ElhQARLQAAQLTLQLADASLALREGRARWAQERETL 309
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
265-598 |
5.99e-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: 43.57 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 265 KQEQESFL-DFKSLKENLErcwTVTESekitFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEdkGTS 343
Cdd:pfam15921 652 KQERDQLLnEVKTSRNELN---SLSED----YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME--GSD 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 344 TQLVRENQVLKQYLEVEKQKTDS------FL--------REREMLLEEARMLKRDLEREQLTAMALRAELEQFipgQAQS 409
Cdd:pfam15921 723 GHAMKVAMGMQKQITAKRGQIDAlqskiqFLeeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL---RSQE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 410 RAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSdlwerlyVEAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVK 489
Cdd:pfam15921 800 RRLKEKVANMEVALDKASLQFAECQDIIQRQEQES-------VRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRT 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 490 ETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKG--------SKRFRAPKEAATEK 561
Cdd:pfam15921 873 HSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGrapslgalDDRVRDCIIESSLR 952
|
330 340 350
....*....|....*....|....*....|....*...
gi 557440739 562 TRTAYSYSSYSQQEAPNQNQNC-RRPSAQRDGGREKPS 598
Cdd:pfam15921 953 SDICHSSSNSLQTEGSKSSETCsREPVLLHAGELEDPS 990
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
302-401 |
6.20e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 302 LAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-----KGTSTQLVRENQVLKQYLEVEKQKTDSFLRER---EM 373
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeveelEAELEEKDERIERLERELSEARSEERREIRKDreiSR 469
|
90 100
....*....|....*....|....*...
gi 557440739 374 LLEEARMLKRDLEREQLTAMALRAELEQ 401
Cdd:COG2433 470 LDREIERLERELEEERERIEELKRKLER 497
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
320-450 |
8.53e-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: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 320 LSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAEL 399
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERL 314
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 557440739 400 EQFIpGQAQSRAESPSVQTEE---KEVGLLQQRLAELEQKLifeQQRSDLWERL 450
Cdd:COG4913 315 EARL-DALREELDELEAQIRGnggDRLEQLEREIERLEREL---EERERRRARL 364
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
253-455 |
1.05e-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: 42.74 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 253 ELDGVKGYLSQRKQEQEsflDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 332
Cdd:TIGR02168 352 ELESLEAELEELEAELE---ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 333 QIRLLEDKGTSTQLVRENQVLKqylevEKQKTDSFLRERemlLEEARMLKRDLEREQLtamALRAELEqfipgQAQSRAE 412
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELE-----ELQEELERLEEA---LEELREELEEAEQALD---AAERELA-----QLQARLD 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 557440739 413 SPSVQTEEKEvGLLQQRLAELEQKLIFEQQRSDLWERLYVEAK 455
Cdd:TIGR02168 493 SLERLQENLE-GFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
309-453 |
2.00e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 309 LRISLEKEEQALSSLQ--------EELRQLREQIRLLEDK-GTSTQLVRENQVLKQYLEvEKQKTDSFLREREMLLEEAR 379
Cdd:COG4717 47 LLERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKeEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557440739 380 MLKRDLEREQltamALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVE 453
Cdd:COG4717 126 QLLPLYQELE----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
488-545 |
2.06e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.41 E-value: 2.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 557440739 488 VKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 545
Cdd:COG4980 36 LKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
310-437 |
2.47e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 310 RISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQ 389
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 557440739 390 LTAMALRAELEQFIPGQAQSRAEspsvqteekevglLQQRLAELEQKL 437
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEE-------------LERELERLEREI 776
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
290-441 |
2.83e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.51 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 290 SEKITFETQKKNLAAENQYLRISLEKEEqalSSLQEELRQLREQIRLLEDKgtstqlvrenqvlkqyLEVEKQKTDSFLR 369
Cdd:pfam09787 54 QERDLLREEIQKLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQ----------------LATERSARREAEA 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557440739 370 EREMLLEEARMLKRDLEREQLTAMALRAELEQFI---PGQAQSRAESPSVQTEekevglLQQRLAELEQKLIFEQ 441
Cdd:pfam09787 115 ELERLQEELRYLEEELRRSKATLQSRIKDREAEIeklRNQLTSKSQSSSSQSE------LENRLHQLTETLIQKQ 183
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
289-450 |
4.33e-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: 39.52 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 289 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLE-DKGTSTQLVRENQvlKQYLEVEKQKT-DS 366
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLElEIEEVEARIKKYE--EQLGNVRNNKEyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 367 FLREremlLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEVglLQQRLAELEQKL-IFEQQRSD 445
Cdd:COG1579 94 LQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE--LDEELAELEAELeELEAEREE 167
|
....*
gi 557440739 446 LWERL 450
Cdd:COG1579 168 LAAKI 172
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
288-446 |
4.96e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.49 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 288 TESEKITFETQKKNLAAENQYlrislEKEEQALSSLQEELRQLREqiRLLEDKGTSTQLVRENQVLKQYLEVEKQKtdsf 367
Cdd:pfam05557 23 LEHKRARIELEKKASALKRQL-----DRESDRNQELQKRIRLLEK--REAEAEEALREQAELNRLKKKYLEALNKK---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 368 LREREMLLEEARMLKRDLERE--QLTAMALRAELEqfipgqaqsraespsVQTEEKEVGLLQQRLAELEQKLI-FEQQRS 444
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNElsELRRQIQRAELE---------------LQSTNSELEELQERLDLLKAKASeAEQLRQ 156
|
..
gi 557440739 445 DL 446
Cdd:pfam05557 157 NL 158
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
240-552 |
5.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 240 QIQKQLVRKthEDELDGVKGYLSQRKQE-QESFLDFKSLKENLERcwtvTESEKITFETQKKNLAAENQYLRISLEKEEQ 318
Cdd:COG4372 63 QLEEELEQA--RSELEQLEEELEELNEQlQAAQAELAQAQEELES----LQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 319 ALSSLQEELRQLREQIRLLEDKGTSTQlvreNQVLKQYLEVEKQKTDSFLREREMLLEEARmlkRDLEREQLTAMALRAE 398
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQ----EELAALEQELQALSEAEAEQALDELLKEAN---RNAEKEEELAEAEKLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 399 LEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAKS 478
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 557440739 479 KSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKGSKRFR 552
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-534 |
5.97e-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: 40.43 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 314 EKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVReNQVLKQYLEVEKQKTDSFLREREM--LLEEARMLKRDLEREQLT 391
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELsrQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 392 AMALRAELEQFIPGQAQSRAESPS-VQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETDGRKRGS 470
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEErLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 557440739 471 R-GSHRAKSKSKETFLGTVKETFDAMKNSTkEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRH 534
Cdd:TIGR02168 825 RlESLERRIAATERRLEDLEEQIEELSEDI-ESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
|
| DUF6627 |
pfam20332 |
Family of unknown function (DUF6627); This family of proteins is functionally uncharacterized. ... |
355-433 |
7.15e-03 |
|
Family of unknown function (DUF6627); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 130 amino acids in length.
Pssm-ID: 466482 Cd Length: 125 Bit Score: 37.51 E-value: 7.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 557440739 355 QYLEVEKQKTDsflreREMLLEearMLKRDLEREQLTAMALRaeleqfiPGQAQSRAESPSVQteekEVGLLQQRLAEL 433
Cdd:pfam20332 29 QVIASEQAQVD-----RAQLLS---TLDRDDVQQQLTAMGVD-------PAQAAERVNRMTDQ----EVAQLNERLEDL 88
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
296-381 |
8.42e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 557440739 296 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTS-TQLVRENQVLKQYLEVEKQKTDSfLREREML 374
Cdd:COG2433 419 EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREiSRLDREIERLERELEEERERIEE-LKRKLER 497
|
....*..
gi 557440739 375 LEEARML 381
Cdd:COG2433 498 LKELWKL 504
|
|
| YtxH |
pfam12732 |
YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are ... |
476-529 |
9.22e-03 |
|
YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are typically between 100 and 143 amino acids in length. The N-terminal region is the most conserved. Proteins is this family are functionally uncharacterized.
Pssm-ID: 432750 [Multi-domain] Cd Length: 71 Bit Score: 35.66 E-value: 9.22e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 557440739 476 AKSKSKETFlGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVK 529
Cdd:pfam12732 19 APKSGKETR-KDLKDKAEDLKDKAKDLAEEAKEKAEDLKEKVKEKADELKEKVK 71
|
|
| |
