|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
321-551 |
3.70e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 321 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSF 399
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 400 LREREMLLEEARMLKRDLEREQLTAMALRAELEqfipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLw 479
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL- 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317886134 480 erlyveAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKE 551
Cdd:COG1196 406 ------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
284-489 |
3.38e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 284 DELDGVKGYLSQRKqeqESFLDFKSLKENLERCwtvtesEKITFEtQKKNLAaenqylriSLEKE-EQALS--SLQEELR 360
Cdd:COG1196 162 EEAAGISKYKERKE---EAERKLEATEENLERL------EDILGE-LERQLE--------PLERQaEKAERyrELKEELK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 361 QLREQIRLLEDKGTSTQLVRENQVLKQyLEVEKQKTDSFLREREMLLEEARmLKRDLEREQLTAM-----ALRAELEQFI 435
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAELEAELEELR-LELEELELELEEAqaeeyELLAELARLE 301
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1317886134 436 PGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQ 489
Cdd:COG1196 302 QDIARLEERRRELEERLEE---LEEELAELEEELEELEEELEELEEELEEAEEE 352
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
307-469 |
6.34e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 307 KSLKENLercwTVTESEK-----ITFETQKKNLAAE------NQYLRISLEKE----EQALSSLQEELRQLREQIRLLED 371
Cdd:COG3206 121 ERLRKNL----TVEPVKGsnvieISYTSPDPELAAAvanalaEAYLEQNLELRreeaRKALEFLEEQLPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 372 KgtstqlvrenqvLKQYleveKQKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAELEQFI----------PGQAQS 441
Cdd:COG3206 197 A------------LEEF----RQKNGLVDLSEEAKLLLQQL--SELESQLAEARAELAEAEARLaalraqlgsgPDALPE 258
|
170 180
....*....|....*....|....*...
gi 1317886134 442 RAESPSVQTEEKEVGLLQQRLAELEQKL 469
Cdd:COG3206 259 LLQSPVIQQLRAQLAELEAELAELSARY 286
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
329-481 |
1.12e-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: 51.61 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 329 TQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVlkqyleVEKQKTDSFLREREMLLE 408
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQA------AELAELTRRLAELETQLD 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1317886134 409 EARMLKRDLEREQLTAMALRAELEqfipgqAQSRAESPSVQTEEKEVGL----LQQRLAELEQKLIfeQQRSDLWER 481
Cdd:pfam19220 206 ATRARLRALEGQLAAEQAERERAE------AQLEEAVEAHRAERASLRMkleaLTARAAATEQLLA--EARNQLRDR 274
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
293-562 |
1.59e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 293 LSQRKQEQESFLDFKSLKENLErcWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQ---EELRQLREQI-RL 368
Cdd:TIGR02169 203 LRREREKAERYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEkrlEEIEQLLEELnKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 369 LEDKGTSTQL-------------------VRENQVLKQYLEVEKQKTDSflrEREMLLEEARMLKRDLEREQLTAMALRA 429
Cdd:TIGR02169 281 IKDLGEEEQLrvkekigeleaeiaslersIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 430 ELEQFIPGQAQSRAEspsVQTEEKEVGLLQQRLAELEQKLifeqqrSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAK 509
Cdd:TIGR02169 358 EYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKL------EKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1317886134 510 SKSKET----FLGTVKETFDAMKNSTKEF--VRHHKEKIKQAKEAVKENLKKFSDSVKS 562
Cdd:TIGR02169 429 IAGIEAkineLEEEKEDKALEIKKQEWKLeqLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-489 |
1.31e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 330 QKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSfLREREMLLEE 409
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE-LEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 410 ARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEE--KEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAK 487
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEElqQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
..
gi 1317886134 488 DQ 489
Cdd:COG4717 241 LE 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
294-482 |
2.44e-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: 48.13 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 294 SQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG 373
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 374 TSTQL-VRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQltamaLRAELEQFIPGQAQSRAESPSVQTEE 452
Cdd:TIGR02168 396 ASLNNeIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE-----LEEELEELQEELERLEEALEELREEL 470
|
170 180 190
....*....|....*....|....*....|
gi 1317886134 453 KEvglLQQRLAELEQKLIFEQQRSDLWERL 482
Cdd:TIGR02168 471 EE---AEQALDAAERELAQLQARLDSLERL 497
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
296-633 |
2.54e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 296 RKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAEN-QYLRISLEKEEQALSSLQEELRQLR-EQIRLLED-K 372
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEaK 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 373 GTSTQLVRENQV------LKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQfipgqaQSRAESP 446
Cdd:PTZ00121 1620 IKAEELKKAEEEkkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEA 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 447 SVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlYVEAKDQHGKQETDGRKrgsrgSHRAKSKSKETflgtvKETFDA 526
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN-KIKAEEAKKEAEEDKKK-----AEEAKKDEEEK-----KKIAHL 1762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 527 MKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGSKRFRAPKEAATEKTRTAYSYSSYS 604
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842
|
330 340 350
....*....|....*....|....*....|.
gi 1317886134 605 QQEAP--NQNQNCRRPSAQRDGGREKPSHSE 633
Cdd:PTZ00121 1843 LEEADafEKHKFNKNNENGEDGNKEADFNKE 1873
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
292-565 |
2.59e-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: 48.13 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 292 YLSQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED 371
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 372 KGTSTQ-----LVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLE-------REQLTAMALRAELEQFipgQA 439
Cdd:TIGR02168 825 RLESLErriaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEEL---SE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 440 QSRAESPSVQTEEKEVGLLQQRLAELEQKLI-FEQQRSDLWERLYVEAKD--QHGKQETDGRKRGSRGSHR--AKSKSKE 514
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRrlKRLENKI 981
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1317886134 515 TFLGTVkeTFDAM-----KNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFR 565
Cdd:TIGR02168 982 KELGPV--NLAAIeeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
271-514 |
3.89e-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: 47.43 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 271 IQIQKQLVRKTHEDELDgvkgylsqrKQEQESFLDFKSLK-ENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEE 349
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE---------KMEQERLRQEKEEKaREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 350 QALSSLQEELRQLREQIRLlEDKGTSTQLVREnqvlKQYLEVEKQKTDSFLRERemlLEEARMLKRDLEREQLTAMALRA 429
Cdd:pfam17380 349 ELERIRQEERKRELERIRQ-EEIAMEISRMRE----LERLQMERQQKNERVRQE---LEAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 430 ELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlyveaKDQHGKQETDGRKRGSRGSHRAK 509
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLELEKEKRDRKRAEEQRRK 495
|
....*
gi 1317886134 510 SKSKE 514
Cdd:pfam17380 496 ILEKE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
272-478 |
4.27e-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: 47.37 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 272 QIQKQLVRKthEDELDGVKGYLSQRKQEQESFLdfKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQA 351
Cdd:TIGR02169 241 AIERQLASL--EEELEKLTEEISELEKRLEEIE--QLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 352 LSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVE-------------------------KQKTDSFLREREM 405
Cdd:TIGR02169 317 LEDAEERLAKLEAEIdKLLAEIEELEREIEEERKRRDKLTEEyaelkeeledlraeleevdkefaetRDELKDYREKLEK 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317886134 406 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLifEQQRSDL 478
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED---KALEIKKQEWKL--EQLAADL 464
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
284-458 |
8.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 284 DELDGVKGYLSQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKE--EQALSSLQEELRQ 361
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEalEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 362 LREQIRLLEDKGTS-TQLVRENQVLKQYLEVEKQKTD--------SFLREREMLLEEARMLKRDLEREQLTAMALRAELE 432
Cdd:COG4717 151 LEERLEELRELEEElEELEAELAELQEELEELLEQLSlateeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180
....*....|....*....|....*.
gi 1317886134 433 QFipgQAQSRAESPSVQTEEKEVGLL 458
Cdd:COG4717 231 QL---ENELEAAALEERLKEARLLLL 253
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
332-494 |
8.72e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 332 KNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG--TSTQLVRENQVLKQYL-EVEK--QKTDSFLREREML 406
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLEaEVEQleERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 407 LEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTE----EKEVGLLQQRLAELEQKLIFEQQRSDLWERL 482
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170
....*....|..
gi 1317886134 483 YVEAKDQHGKQE 494
Cdd:TIGR02168 840 LEDLEEQIEELS 851
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
289-469 |
9.43e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 289 VKGYLSQRKQEQESFLDF-----KSLKENLERcwtvTESEKITFETQKK--NLAAENQYLRISLEKEEQALSSLQEELRQ 361
Cdd:COG3206 162 LEQNLELRREEARKALEFleeqlPELRKELEE----AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 362 LREQIRLLEDK----GTSTQLVRENQVLKQYLEvekqktdsflREREMLLEEARMLKRDLER--EQLTAMALRAELEQFI 435
Cdd:COG3206 238 AEARLAALRAQlgsgPDALPELLQSPVIQQLRA----------QLAELEAELAELSARYTPNhpDVIALRAQIAALRAQL 307
|
170 180 190
....*....|....*....|....*....|....*.
gi 1317886134 436 PGQAQSRAESPSVQTE--EKEVGLLQQRLAELEQKL 469
Cdd:COG3206 308 QQEAQRILASLEAELEalQAREASLQAQLAQLEARL 343
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
330-469 |
1.18e-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: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 330 QKKNLAAENQYLR--ISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQlVRENQVLKQYLEVEKQKTDSFLREREMLL 407
Cdd:COG4913 266 AARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLE-ARLDALREELDELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1317886134 408 EEARMLKRDLER---------EQLTAMALRAEL--EQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKL 469
Cdd:COG4913 345 REIERLERELEErerrrarleALLAALGLPLPAsaEEFAALRAEAAALLEALEEELEA---LEEALAEAEAAL 414
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
320-497 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 320 TESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--------------------------- 372
Cdd:COG4942 46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqkeelaellralyrlgrqpplall 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 373 ---GTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEearmLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQ 449
Cdd:COG4942 126 lspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----LRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1317886134 450 TE-EKEVGLLQQRLAELEQKlifEQQRSDLWERLYVEAKDQHGKQETDG 497
Cdd:COG4942 202 ARlEKELAELAAELAELQQE---AEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
345-563 |
1.81e-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: 45.43 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 345 LEKEEQALSSLQEELRQLREQIRLLEdkgtstqlvRENQVLKQYLEVEKQKTD-----------SFLREREMLLEEARML 413
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLE---------RQAEKAERYKELKAELRElelallvlrleELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 414 KRDLEREQLTAMALRAELEQFipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQhgkQ 493
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEEL---RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ---L 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 494 ETDGRKRGSRgshRAKSKSKETFLGTVKETFDAMKNSTKEFvRHHKEKIKQAKEAVKENLKKFSDSVKST 563
Cdd:TIGR02168 326 EELESKLDEL---AEELAELEEKLEELKEELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQL 391
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
331-551 |
1.90e-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: 45.06 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 331 KKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTstQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEA 410
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--QLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 411 RMLKRDLEREQLTAMALRAELE--------QFIPgqaQSRAESPSVqteEKEVGLLQQRLAELEQKLIFEQQRSDLWERL 482
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNdlearlshSRIP---EIQAELSKL---EEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317886134 483 YVEAKDQhgKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEF------VRHHKEKIKQAKEAVKE 551
Cdd:TIGR02169 835 IQELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLRELERKIEE 907
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-466 |
2.39e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 346 EKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAM 425
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1317886134 426 ALRAELEQFIPGqAQSRAESPSVQTEEKEVGLLQQRLAELE 466
Cdd:COG1196 741 LLEEEELLEEEA-LEELPEPPDLEELERELERLEREIEALG 780
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
297-630 |
2.42e-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: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 297 KQEQESFL-DFKSLKENLErcwTVTESekitFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEdkGTS 375
Cdd:pfam15921 652 KQERDQLLnEVKTSRNELN---SLSED----YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME--GSD 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 376 TQLVRENQVLKQYLEVEKQKTDS------FL--------REREMLLEEARMLKRDLEREQLTAMALRAELEQFipgQAQS 441
Cdd:pfam15921 723 GHAMKVAMGMQKQITAKRGQIDAlqskiqFLeeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL---RSQE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 442 RAESPSVQTeeKEVGLLQQRLAELEQKLIFEQQrsdlwERLYVEAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVK 521
Cdd:pfam15921 800 RRLKEKVAN--MEVALDKASLQFAECQDIIQRQ-----EQESVRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRT 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 522 ETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKG--------SKRFRAPKEAATEK 593
Cdd:pfam15921 873 HSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGrapslgalDDRVRDCIIESSLR 952
|
330 340 350
....*....|....*....|....*....|....*...
gi 1317886134 594 TRTAYSYSSYSQQEAPNQNQNC-RRPSAQRDGGREKPS 630
Cdd:pfam15921 953 SDICHSSSNSLQTEGSKSSETCsREPVLLHAGELEDPS 990
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
285-478 |
2.83e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 285 ELDGVKGYLSQRKQEQESFLDfkSLKENLERCwtvtesekitfETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 364
Cdd:pfam07888 133 ELEEDIKTLTQRVLERETELE--RMKERAKKA-----------GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRN 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 365 qirLLEDKGTSTQLVREN-QVLKQYLEVEKQKTdsflREREMLLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRA 443
Cdd:pfam07888 200 ---SLAQRDTQVLQLQDTiTTLTQKLTTAHRKE----AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQA 272
|
170 180 190
....*....|....*....|....*....|....*..
gi 1317886134 444 E--SPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDL 478
Cdd:pfam07888 273 ElhQARLQAAQLTLQLADASLALREGRARWAQERETL 309
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
328-494 |
2.94e-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: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 328 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-KGTSTQLVRENQVLKQYLEVEKQ-----KTDSFLR 401
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAElerldASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 402 EREMLLEEARMLKRDLEREQLTAMALRAELEQFIPG------QAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQR 475
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQaeeeldELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170
....*....|....*....
gi 1317886134 476 SDLWERLYVEAKDQHGKQE 494
Cdd:COG4913 769 ENLEERIDALRARLNRAEE 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
328-500 |
3.50e-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: 43.60 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 328 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--GTSTQLVRENQVLKQYLEVEKQKTDSFLREREM 405
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 406 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLifEQQRSDLwERLYVE 485
Cdd:COG4942 106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL--EAERAEL-EALLAE 182
|
170
....*....|....*
gi 1317886134 486 AKDQHGKQETDGRKR 500
Cdd:COG4942 183 LEEERAALEALKAER 197
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
334-433 |
5.66e-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: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 334 LAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-----KGTSTQLVRENQVLKQYLEVEKQKTDSFLRER---EM 405
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeveelEAELEEKDERIERLERELSEARSEERREIRKDreiSR 469
|
90 100
....*....|....*....|....*...
gi 1317886134 406 LLEEARMLKRDLEREQLTAMALRAELEQ 433
Cdd:COG2433 470 LDREIERLERELEEERERIEELKRKLER 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
285-487 |
8.14e-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: 43.12 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 285 ELDGVKGYLSQRKQEQEsflDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 364
Cdd:TIGR02168 352 ELESLEAELEELEAELE---ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 365 QIRLLEDKGTSTQLVRENQVLKqylevEKQKTDSFLRERemlLEEARMLKRDLEREQLtamALRAELEqfipgQAQSRAE 444
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELE-----ELQEELERLEEA---LEELREELEEAEQALD---AAERELA-----QLQARLD 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1317886134 445 SPSVQTEEKEvGLLQQRLAELEQKLIFEQQRSDLWERLYVEAK 487
Cdd:TIGR02168 493 SLERLQENLE-GFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
352-482 |
9.40e-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: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 352 LSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAEL 431
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERL 314
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1317886134 432 EQFIpGQAQSRAESPSVQTEE---KEVGLLQQRLAELEQKLifeQQRSDLWERL 482
Cdd:COG4913 315 EARL-DALREELDELEAQIRGnggDRLEQLEREIERLEREL---EERERRRARL 364
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
520-577 |
1.71e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.80 E-value: 1.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1317886134 520 VKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 577
Cdd:COG4980 36 LKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
341-485 |
2.04e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 341 LRISLEKEEQALSSLQ--------EELRQLREQIRLLEDK-GTSTQLVRENQVLKQYLEvEKQKTDSFLREREMLLEEAR 411
Cdd:COG4717 47 LLERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKeEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317886134 412 MLKRDLEREQltamALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVE 485
Cdd:COG4717 126 QLLPLYQELE----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
322-473 |
2.13e-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: 40.90 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 322 SEKITFETQKKNLAAENQYLRISLEKEEqalSSLQEELRQLREQIRLLEDKgtstqlvrenqvlkqyLEVEKQKTDSFLR 401
Cdd:pfam09787 54 QERDLLREEIQKLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQ----------------LATERSARREAEA 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317886134 402 EREMLLEEARMLKRDLEREQLTAMALRAELEQFI---PGQAQSRAESPSVQTEekevglLQQRLAELEQKLIFEQ 473
Cdd:pfam09787 115 ELERLQEELRYLEEELRRSKATLQSRIKDREAEIeklRNQLTSKSQSSSSQSE------LENRLHQLTETLIQKQ 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-469 |
2.31e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 342 RISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQ 421
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1317886134 422 LTAMALRAELEQFIPGQAQSRAEspsvqteekevglLQQRLAELEQKL 469
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEE-------------LERELERLEREI 776
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
272-584 |
2.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 272 QIQKQLVRKthEDELDGVKGYLSQRKQE-QESFLDFKSLKENLERcwtvTESEKITFETQKKNLAAENQYLRISLEKEEQ 350
Cdd:COG4372 63 QLEEELEQA--RSELEQLEEELEELNEQlQAAQAELAQAQEELES----LQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 351 ALSSLQEELRQLREQIRLLEDKGTSTQlvreNQVLKQYLEVEKQKTDSFLREREMLLEEARmlkRDLEREQLTAMALRAE 430
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQ----EELAALEQELQALSEAEAEQALDELLKEAN---RNAEKEEELAEAEKLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 431 LEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAKS 510
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317886134 511 KSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKGSKRFR 584
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
321-482 |
3.34e-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: 39.91 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 321 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLE-DKGTSTQLVRENQvlKQYLEVEKQKT-DS 398
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLElEIEEVEARIKKYE--EQLGNVRNNKEyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 399 FLREremlLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEVglLQQRLAELEQKL-IFEQQRSD 477
Cdd:COG1579 94 LQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE--LDEELAELEAELeELEAEREE 167
|
....*
gi 1317886134 478 LWERL 482
Cdd:COG1579 168 LAAKI 172
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
320-478 |
3.50e-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: 40.88 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 320 TESEKITFETQKKNLAAENQYlrislEKEEQALSSLQEELRQLREqiRLLEDKGTSTQLVRENQVLKQYLEVEKQKtdsf 399
Cdd:pfam05557 23 LEHKRARIELEKKASALKRQL-----DRESDRNQELQKRIRLLEK--REAEAEEALREQAELNRLKKKYLEALNKK---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 400 LREREMLLEEARMLKRDLERE--QLTAMALRAELEqfipgqaqsraespsVQTEEKEVGLLQQRLAELEQKLI-FEQQRS 476
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNElsELRRQIQRAELE---------------LQSTNSELEELQERLDLLKAKASeAEQLRQ 156
|
..
gi 1317886134 477 DL 478
Cdd:pfam05557 157 NL 158
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
346-566 |
4.84e-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: 40.81 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 346 EKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVReNQVLKQYLEVEKQKTDSFLREREM--LLEEARMLKRDLEREQLT 423
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELsrQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 424 AMALRAELEQFIPGQAQSRAESPS-VQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETDGRKRGS 502
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEErLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317886134 503 R-GSHRAKSKSKETFLGTVKETFDAMKNSTkEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRH 566
Cdd:TIGR02168 825 RlESLERRIAATERRLEDLEEQIEELSEDI-ESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
279-617 |
6.24e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 279 RKTHEDELDGVKGYLSQ-------RKQEQESFLDFKSLKENLERcwTVTESEKITFETQKKNLAAENQYLRISLEKEEQA 351
Cdd:COG5185 207 IKESETGNLGSESTLLEkakeiinIEEALKGFQDPESELEDLAQ--TSDKLEKLVEQNTDLRLEKLGENAESSKRLNENA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 352 lSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSfLREREMLLEEarmLKRDLEREQLTAM----AL 427
Cdd:COG5185 285 -NNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEES-KRETETGIQN---LTAEIEQGQESLTenleAI 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 428 RAELEQFIPGQAQSR----AESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKdqhgkqETDGRKRGSR 503
Cdd:COG5185 360 KEEIENIVGEVELSKsseeLDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIE------ELQRQIEQAT 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 504 GSHRAKSKSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDeKGSKRF 583
Cdd:COG5185 434 SSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRA-KLERQL 512
|
330 340 350
....*....|....*....|....*....|....
gi 1317886134 584 RAPKEAATEKTRTAYSYSSYSQQEAPNQNQNCRR 617
Cdd:COG5185 513 EGVRSKLDQVAESLKDFMRARGYAHILALENLIP 546
|
|
| DUF6627 |
pfam20332 |
Family of unknown function (DUF6627); This family of proteins is functionally uncharacterized. ... |
387-465 |
7.72e-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: 7.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317886134 387 QYLEVEKQKTDsflreREMLLEearMLKRDLEREQLTAMALRaeleqfiPGQAQSRAESPSVQteekEVGLLQQRLAEL 465
Cdd:pfam20332 29 QVIASEQAQVD-----RAQLLS---TLDRDDVQQQLTAMGVD-------PAQAAERVNRMTDQ----EVAQLNERLEDL 88
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
328-413 |
7.74e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 328 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTS-TQLVRENQVLKQYLEVEKQKTDSfLREREML 406
Cdd:COG2433 419 EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREiSRLDREIERLERELEEERERIEE-LKRKLER 497
|
....*..
gi 1317886134 407 LEEARML 413
Cdd:COG2433 498 LKELWKL 504
|
|
| YtxH |
pfam12732 |
YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are ... |
508-561 |
8.64e-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: 8.64e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1317886134 508 AKSKSKETFlGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVK 561
Cdd:pfam12732 19 APKSGKETR-KDLKDKAEDLKDKAKDLAEEAKEKAEDLKEKVKEKADELKEKVK 71
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
289-614 |
8.72e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.68 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 289 VKGYLSQRKQEQESFLDFKSLKENLERCWTvtESEKITFETQKKNLAAENQYLRisLEKEEQALSSLQEELRQLREQIRL 368
Cdd:COG5022 812 YRSYLACIIKLQKTIKREKKLRETEEVEFS--LKAEVLIQKFGRSLKAKKRFSL--LKKETIYLQSAQRVELAERQLQEL 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 369 LEDKGTSTQLVREN-QVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSraESPS 447
Cdd:COG5022 888 KIDVKSISSLKLVNlELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHE--VESK 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 448 VQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETD-------GRKRGSRGSHRAKSKSKETFLGTV 520
Cdd:COG5022 966 LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQEStkqlkelPVEVAELQSASKIISSESTELSIL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317886134 521 KETFDAMKNSTKEFVRHHKE----KIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKGSKrfrapKEAATEKTRT 596
Cdd:COG5022 1046 KPLQKLKGLLLLENNQLQARykalKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVK-----PANVLQFIVA 1120
|
330
....*....|....*...
gi 1317886134 597 AYSYSSYSQQEAPNQNQN 614
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQL 1138
|
|
| |
