|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
330-560 |
3.82e-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: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 330 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSF 408
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 409 LREREMLLEEARMLKRDLEREQLTAMALRAELEqfipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLw 488
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAE-----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL- 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907200551 489 erlyveAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKE 560
Cdd:COG1196 406 ------EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
293-498 |
3.71e-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: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 293 DELDGVKGYLSQRKqeqESFLDFKSLKENLERCwtvtesEKITFEtQKKNLAaenqylriSLEKE-EQALS--SLQEELR 369
Cdd:COG1196 162 EEAAGISKYKERKE---EAERKLEATEENLERL------EDILGE-LERQLE--------PLERQaEKAERyrELKEELK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 370 QLREQIRLLEDKGTSTQLVRENQVLKQyLEVEKQKTDSFLREREMLLEEARmLKRDLEREQLTAM-----ALRAELEQFI 444
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEE-LEAELEELEAELAELEAELEELR-LELEELELELEEAqaeeyELLAELARLE 301
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907200551 445 PGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQ 498
Cdd:COG1196 302 QDIARLEERRRELEERLEE---LEEELAELEEELEELEEELEELEEELEEAEEE 352
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
316-478 |
5.44e-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: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 316 KSLKENLercwTVTESEK-----ITFETQKKNLAAE------NQYLRISLEKE----EQALSSLQEELRQLREQIRLLED 380
Cdd:COG3206 121 ERLRKNL----TVEPVKGsnvieISYTSPDPELAAAvanalaEAYLEQNLELRreeaRKALEFLEEQLPELRKELEEAEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 381 KgtstqlvrenqvLKQYleveKQKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAELEQFI----------PGQAQS 450
Cdd:COG3206 197 A------------LEEF----RQKNGLVDLSEEAKLLLQQL--SELESQLAEARAELAEAEARLaalraqlgsgPDALPE 258
|
170 180
....*....|....*....|....*...
gi 1907200551 451 RAESPSVQTEEKEVGLLQQRLAELEQKL 478
Cdd:COG3206 259 LLQSPVIQQLRAQLAELEAELAELSARY 286
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
338-490 |
1.10e-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: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 338 TQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVlkqyleVEKQKTDSFLREREMLLE 417
Cdd:pfam19220 132 EQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQA------AELAELTRRLAELETQLD 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907200551 418 EARMLKRDLEREQLTAMALRAELEqfipgqAQSRAESPSVQTEEKEVGL----LQQRLAELEQKLIfeQQRSDLWER 490
Cdd:pfam19220 206 ATRARLRALEGQLAAEQAERERAE------AQLEEAVEAHRAERASLRMkleaLTARAAATEQLLA--EARNQLRDR 274
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
302-571 |
2.32e-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: 51.61 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 302 LSQRKQEQESFLDFKSLKENLErcWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQ---EELRQLREQI-RL 377
Cdd:TIGR02169 203 LRREREKAERYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEkrlEEIEQLLEELnKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 378 LEDKGTSTQL-------------------VRENQVLKQYLEVEKQKTDSflrEREMLLEEARMLKRDLEREQLTAMALRA 438
Cdd:TIGR02169 281 IKDLGEEEQLrvkekigeleaeiaslersIAEKERELEDAEERLAKLEA---EIDKLLAEIEELEREIEEERKRRDKLTE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 439 ELEQFIPGQAQSRAEspsVQTEEKEVGLLQQRLAELEQKLifeqqrSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAK 518
Cdd:TIGR02169 358 EYAELKEELEDLRAE---LEEVDKEFAETRDELKDYREKL------EKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200551 519 SKSKET----FLGTVKETFDAMKNSTKEF--VRHHKEKIKQAKEAVKENLKKFSDSVKS 571
Cdd:TIGR02169 429 IAGIEAkineLEEEKEDKALEIKKQEWKLeqLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
267-478 |
2.95e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 267 FYGKNEgnKGKGTIQiqkQLVRKTHEDELDGVKGYLSqRKQEQESFLDFKSLKEnLERCWTVTESEKITFETQKKNLAAe 346
Cdd:COG4717 28 IYGPNE--AGKSTLL---AFIRAMLLERLEKEADELF-KPQGRKPELNLKELKE-LEEELKEAEEKEEEYAELQEELEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 347 nqyLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRE-NQVLKQYLEVEKQKTD--SFLREREMLLEEARMLK 423
Cdd:COG4717 100 ---LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEElrELEEELEELEAELAELQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200551 424 RDLERE-QLTAMALRAELEQFIPGQAQSRAEspsVQTEEKEVGLLQQRLAELEQKL 478
Cdd:COG4717 177 EELEELlEQLSLATEEELQDLAEELEELQQR---LAELEEELEEAQEELEELEEEL 229
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
303-491 |
2.70e-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: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 303 SQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG 382
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 383 TSTQL-VRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQltamaLRAELEQFIPGQAQSRAESPSVQTEE 461
Cdd:TIGR02168 396 ASLNNeIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE-----LEEELEELQEELERLEEALEELREEL 470
|
170 180 190
....*....|....*....|....*....|
gi 1907200551 462 KEvglLQQRLAELEQKLIFEQQRSDLWERL 491
Cdd:TIGR02168 471 EE---AEQALDAAERELAQLQARLDSLERL 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
301-574 |
3.29e-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: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 301 YLSQRKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED 380
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 381 KGTSTQ-----LVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLE-------REQLTAMALRAELEQFipgQA 448
Cdd:TIGR02168 825 RLESLErriaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEEL---SE 901
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 449 QSRAESPSVQTEEKEVGLLQQRLAELEQKLI-FEQQRSDLWERLYVEAKD--QHGKQETDGRKRGSRGSHR--AKSKSKE 523
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLSEEYSLtlEEAEALENKIEDDEEEARRrlKRLENKI 981
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907200551 524 TFLGTVkeTFDAM-----KNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFR 574
Cdd:TIGR02168 982 KELGPV--NLAAIeeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
305-642 |
3.69e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 305 RKQEQESFLDFKSLKENLERCWTVTESEKITFETQKKNLAAEN-QYLRISLEKEEQALSSLQEELRQLR-EQIRLLED-K 381
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEaK 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 382 GTSTQLVRENQV------LKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQfipgqaQSRAESP 455
Cdd:PTZ00121 1620 IKAEELKKAEEEkkkveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEA 1693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 456 SVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlYVEAKDQHGKQETDGRKrgsrgSHRAKSKSKETflgtvKETFDA 535
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN-KIKAEEAKKEAEEDKKK-----AEEAKKDEEEK-----KKIAHL 1762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 536 MKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGSKRFRAPKEAATEKTRTAYSYSSYS 613
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKEMEDSAIKEVADSKNMQ 1842
|
330 340 350
....*....|....*....|....*....|.
gi 1907200551 614 QQEAP--NQNQNCRRPSAQRDGGREKPSHSE 642
Cdd:PTZ00121 1843 LEEADafEKHKFNKNNENGEDGNKEADFNKE 1873
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
280-523 |
4.24e-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: 47.04 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 280 IQIQKQLVRKTHEDELDgvkgylsqrKQEQESFLDFKSLK-ENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEE 358
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE---------KMEQERLRQEKEEKaREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 359 QALSSLQEELRQLREQIRLlEDKGTSTQLVREnqvlKQYLEVEKQKTDSFLRERemlLEEARMLKRDLEREQLTAMALRA 438
Cdd:pfam17380 349 ELERIRQEERKRELERIRQ-EEIAMEISRMRE----LERLQMERQQKNERVRQE---LEAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 439 ELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERlyveaKDQHGKQETDGRKRGSRGSHRAK 518
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLELEKEKRDRKRAEEQRRK 495
|
....*
gi 1907200551 519 SKSKE 523
Cdd:pfam17380 496 ILEKE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
281-487 |
4.89e-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: 46.98 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 281 QIQKQLVRKthEDELDGVKGYLSQRKQEQESFLDfkSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQA 360
Cdd:TIGR02169 241 AIERQLASL--EEELEKLTEEISELEKRLEEIEQ--LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 361 LSSLQEELRQLREQI-RLLEDKGTSTQLVRENQVLKQYLEVE-------------------------KQKTDSFLREREM 414
Cdd:TIGR02169 317 LEDAEERLAKLEAEIdKLLAEIEELEREIEEERKRRDKLTEEyaelkeeledlraeleevdkefaetRDELKDYREKLEK 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200551 415 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKLifEQQRSDL 487
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED---KALEIKKQEWKL--EQLAADL 464
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
298-478 |
8.74e-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: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 298 VKGYLSQRKQEQESFLDF-----KSLKENLERcwtvTESEKITFETQKK--NLAAENQYLRISLEKEEQALSSLQEELRQ 370
Cdd:COG3206 162 LEQNLELRREEARKALEFleeqlPELRKELEE----AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 371 LREQIRLLEDK----GTSTQLVRENQVLKQYLEvekqktdsflREREMLLEEARMLKRDLER--EQLTAMALRAELEQFI 444
Cdd:COG3206 238 AEARLAALRAQlgsgPDALPELLQSPVIQQLRA----------QLAELEAELAELSARYTPNhpDVIALRAQIAALRAQL 307
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907200551 445 PGQAQSRAESPSVQTE--EKEVGLLQQRLAELEQKL 478
Cdd:COG3206 308 QQEAQRILASLEAELEalQAREASLQAQLAQLEARL 343
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-478 |
1.02e-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: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 339 QKKNLAAENQYLR--ISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQlVRENQVLKQYLEVEKQKTDSFLREREMLL 416
Cdd:COG4913 266 AARERLAELEYLRaaLRLWFAQRRLELLEAELEELRAELARLEAELERLE-ARLDALREELDELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907200551 417 EEARMLKRDLER---------EQLTAMALRAEL--EQFIPGQAQSRAESPSVQTEEKEvglLQQRLAELEQKL 478
Cdd:COG4913 345 REIERLERELEErerrrarleALLAALGLPLPAsaEEFAALRAEAAALLEALEEELEA---LEEALAEAEAAL 414
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-503 |
1.04e-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: 46.20 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 341 KNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKG--TSTQLVRENQVLKQYL-EVEK--QKTDSFLREREML 415
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeeLSRQISALRKDLARLEaEVEQleERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 416 LEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTE----EKEVGLLQQRLAELEQKLIFEQQRSDLWERL 491
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAldelRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170
....*....|..
gi 1907200551 492 YVEAKDQHGKQE 503
Cdd:TIGR02168 840 LEDLEEQIEELS 851
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
329-506 |
1.57e-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: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 329 TESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--------------------------- 381
Cdd:COG4942 46 LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqkeelaellralyrlgrqpplall 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 382 ---GTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEearmLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQ 458
Cdd:COG4942 126 lspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA----LRAELEAERAELEALLAELEEERAALEALKAERQKLL 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907200551 459 TE-EKEVGLLQQRLAELEQKlifEQQRSDLWERLYVEAKDQHGKQETDG 506
Cdd:COG4942 202 ARlEKELAELAAELAELQQE---AEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
354-572 |
2.06e-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: 45.05 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 354 LEKEEQALSSLQEELRQLREQIRLLEdkgtstqlvRENQVLKQYLEVEKQKTD-----------SFLREREMLLEEARML 422
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLE---------RQAEKAERYKELKAELRElelallvlrleELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 423 KRDLEREQLTAMALRAELEQFipgQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQhgkQ 502
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEEL---RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ---L 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 503 ETDGRKRGSRgshRAKSKSKETFLGTVKETFDAMKNSTKEFvRHHKEKIKQAKEAVKENLKKFSDSVKST 572
Cdd:TIGR02168 326 EELESKLDEL---AEELAELEEKLEELKEELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQL 391
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
340-560 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 340 KKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTstQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEA 419
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--QLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 420 RMLKRDLEREQLTAMALRAELE--------QFIPgqaQSRAESPSVqteEKEVGLLQQRLAELEQKLIFEQQRSDLWERL 491
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNdlearlshSRIP---EIQAELSKL---EEEVSRIEARLREIEQKLNRLTLEKEYLEKE 834
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200551 492 YVEAKDQhgKQETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEF------VRHHKEKIKQAKEAVKE 560
Cdd:TIGR02169 835 IQELQEQ--RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLgdlkkeRDELEAQLRELERKIEE 907
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
355-475 |
2.46e-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: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 355 EKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAM 434
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907200551 435 ALRAELEQFIPGqAQSRAESPSVQTEEKEVGLLQQRLAELE 475
Cdd:COG1196 741 LLEEEELLEEEA-LEELPEPPDLEELERELERLEREIEALG 780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
337-503 |
2.59e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 337 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-KGTSTQLVRENQVLKQYLEVEKQ-----KTDSFLR 410
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAElerldASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 411 EREMLLEEARMLKRDLEREQLTAMALRAELEQFIPG------QAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQR 484
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQaeeeldELQDRLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170
....*....|....*....
gi 1907200551 485 SDLWERLYVEAKDQHGKQE 503
Cdd:COG4913 769 ENLEERIDALRARLNRAEE 787
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
337-509 |
3.42e-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: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 337 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDK--GTSTQLVRENQVLKQYLEVEKQKTDSFLREREM 414
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 415 LLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLifEQQRSDLwERLYVE 494
Cdd:COG4942 106 LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL--EAERAEL-EALLAE 182
|
170
....*....|....*
gi 1907200551 495 AKDQHGKQETDGRKR 509
Cdd:COG4942 183 LEEERAALEALKAER 197
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
306-639 |
3.53e-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: 44.34 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 306 KQEQESFL-DFKSLKENLErcwTVTESekitFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEdkGTS 384
Cdd:pfam15921 652 KQERDQLLnEVKTSRNELN---SLSED----YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME--GSD 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 385 TQLVRENQVLKQYLEVEKQKTDS------FL--------REREMLLEEARMLKRDLEREQLTAMALRAELEQFipgQAQS 450
Cdd:pfam15921 723 GHAMKVAMGMQKQITAKRGQIDAlqskiqFLeeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL---RSQE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 451 RAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSdlwerlyVEAKDQHGKQETDGRKRGSRGSHRAKSKSKETFLGTVK 530
Cdd:pfam15921 800 RRLKEKVANMEVALDKASLQFAECQDIIQRQEQES-------VRLKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRT 872
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 531 ETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKG--------SKRFRAPKEAATEK 602
Cdd:pfam15921 873 HSNVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGrapslgalDDRVRDCIIESSLR 952
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907200551 603 TRTAYSYSSYSQQEAPNQNQNC-RRPSAQRDGGREKPS 639
Cdd:pfam15921 953 SDICHSSSNSLQTEGSKSSETCsREPVLLHAGELEDPS 990
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
294-487 |
3.54e-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: 44.12 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 294 ELDGVKGYLSQRKQEQESFLDfkSLKENLERCwtvtesekitfETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 373
Cdd:pfam07888 133 ELEEDIKTLTQRVLERETELE--RMKERAKKA-----------GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRN 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 374 qirLLEDKGTSTQLVREN-QVLKQYLEVEKQKTdsflREREMLLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRA 452
Cdd:pfam07888 200 ---SLAQRDTQVLQLQDTiTTLTQKLTTAHRKE----AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQA 272
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907200551 453 E--SPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDL 487
Cdd:pfam07888 273 ElhQARLQAAQLTLQLADASLALREGRARWAQERETL 309
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
343-442 |
5.86e-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: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 343 LAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLED-----KGTSTQLVRENQVLKQYLEVEKQKTDSFLRER---EM 414
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeveelEAELEEKDERIERLERELSEARSEERREIRKDreiSR 469
|
90 100
....*....|....*....|....*...
gi 1907200551 415 LLEEARMLKRDLEREQLTAMALRAELEQ 442
Cdd:COG2433 470 LDREIERLERELEEERERIEELKRKLER 497
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-491 |
8.29e-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: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 361 LSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMlkRDLEREQLTAMALRAEL 440
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERL 314
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907200551 441 EQFIpGQAQSRAESPSVQTEE---KEVGLLQQRLAELEQKLifeQQRSDLWERL 491
Cdd:COG4913 315 EARL-DALREELDELEAQIRGnggDRLEQLEREIERLEREL---EERERRRARL 364
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
294-496 |
9.10e-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: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 294 ELDGVKGYLSQRKQEQEsflDFKSLKENLERCWTVTESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLRE 373
Cdd:TIGR02168 352 ELESLEAELEELEAELE---ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 374 QIRLLEDKGTSTQLVRENQVLKqylevEKQKTDSFLRERemlLEEARMLKRDLEREQLtamALRAELEqfipgQAQSRAE 453
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELE-----ELQEELERLEEA---LEELREELEEAEQALD---AAERELA-----QLQARLD 492
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907200551 454 SPSVQTEEKEvGLLQQRLAELEQKLIFEQQRSDLWERLYVEAK 496
Cdd:TIGR02168 493 SLERLQENLE-GFSEGVKALLKNQSGLSGILGVLSELISVDEG 534
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
350-494 |
1.84e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 350 LRISLEKEEQALSSLQ--------EELRQLREQIRLLEDK-GTSTQLVRENQVLKQYLEvEKQKTDSFLREREMLLEEAR 420
Cdd:COG4717 47 LLERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKeEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200551 421 MLKRDLEREQltamALRAELEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVE 494
Cdd:COG4717 126 QLLPLYQELE----ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
529-586 |
1.95e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.41 E-value: 1.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907200551 529 VKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 586
Cdd:COG4980 36 LKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
331-482 |
2.21e-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: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 331 SEKITFETQKKNLAAENQYLRISLEKEEqalSSLQEELRQLREQIRLLEDKgtstqlvrenqvlkqyLEVEKQKTDSFLR 410
Cdd:pfam09787 54 QERDLLREEIQKLRGQIQQLRTELQELE---AQQQEEAESSREQLQELEEQ----------------LATERSARREAEA 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200551 411 EREMLLEEARMLKRDLEREQLTAMALRAELEQFI---PGQAQSRAESPSVQTEekevglLQQRLAELEQKLIFEQ 482
Cdd:pfam09787 115 ELERLQEELRYLEEELRRSKATLQSRIKDREAEIeklRNQLTSKSQSSSSQSE------LENRLHQLTETLIQKQ 183
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
351-478 |
2.36e-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: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 351 RISLEKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQ 430
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL 741
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907200551 431 LTAMALRAELEQFIPGQAQSRAEspsvqteekevglLQQRLAELEQKL 478
Cdd:COG1196 742 LEEEELLEEEALEELPEPPDLEE-------------LERELERLEREI 776
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
330-491 |
3.74e-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: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 330 ESEKITFETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLE-DKGTSTQLVRENQvlKQYLEVEKQKT-DS 407
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLElEIEEVEARIKKYE--EQLGNVRNNKEyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 408 FLREremlLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSRAESPSVQTEEKEVglLQQRLAELEQKL-IFEQQRSD 486
Cdd:COG1579 94 LQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE--LDEELAELEAELeELEAEREE 167
|
....*
gi 1907200551 487 LWERL 491
Cdd:COG1579 168 LAAKI 172
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
281-593 |
3.79e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 281 QIQKQLVRKthEDELDGVKGYLSQRKQE-QESFLDFKSLKENLERcwtvTESEKITFETQKKNLAAENQYLRISLEKEEQ 359
Cdd:COG4372 63 QLEEELEQA--RSELEQLEEELEELNEQlQAAQAELAQAQEELES----LQEEAEELQEELEELQKERQDLEQQRKQLEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 360 ALSSLQEELRQLREQIRLLEDKGTSTQlvreNQVLKQYLEVEKQKTDSFLREREMLLEEARmlkRDLEREQLTAMALRAE 439
Cdd:COG4372 137 QIAELQSEIAEREEELKELEEQLESLQ----EELAALEQELQALSEAEAEQALDELLKEAN---RNAEKEEELAEAEKLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 440 LEQFIPGQAQSRAESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETDGRKRGSRGSHRAKS 519
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907200551 520 KSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKGSKRFR 593
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
329-487 |
4.05e-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: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 329 TESEKITFETQKKNLAAENQYlrislEKEEQALSSLQEELRQLREqiRLLEDKGTSTQLVRENQVLKQYLEVEKQKtdsf 408
Cdd:pfam05557 23 LEHKRARIELEKKASALKRQL-----DRESDRNQELQKRIRLLEK--REAEAEEALREQAELNRLKKKYLEALNKK---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 409 LREREMLLEEARMLKRDLERE--QLTAMALRAELEqfipgqaqsraespsVQTEEKEVGLLQQRLAELEQKLI-FEQQRS 485
Cdd:pfam05557 92 LNEKESQLADAREVISCLKNElsELRRQIQRAELE---------------LQSTNSELEELQERLDLLKAKASeAEQLRQ 156
|
..
gi 1907200551 486 DL 487
Cdd:pfam05557 157 NL 158
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
355-575 |
5.60e-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: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 355 EKEEQALSSLQEELRQLREQIRLLEDKGTSTQLVReNQVLKQYLEVEKQKTDSFLREREM--LLEEARMLKRDLEREQLT 432
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKAL-AELRKELEELEEELEQLRKELEELsrQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 433 AMALRAELEQFIPGQAQSRAESPS-VQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETDGRKRGS 511
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEErLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907200551 512 R-GSHRAKSKSKETFLGTVKETFDAMKNSTkEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRH 575
Cdd:TIGR02168 825 RlESLERRIAATERRLEDLEEQIEELSEDI-ESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
|
| DUF6627 |
pfam20332 |
Family of unknown function (DUF6627); This family of proteins is functionally uncharacterized. ... |
396-474 |
7.56e-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: 7.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907200551 396 QYLEVEKQKTDsflreREMLLEearMLKRDLEREQLTAMALRaeleqfiPGQAQSRAESPSVQteekEVGLLQQRLAEL 474
Cdd:pfam20332 29 QVIASEQAQVD-----RAQLLS---TLDRDDVQQQLTAMGVD-------PAQAAERVNRMTDQ----EVAQLNERLEDL 88
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
337-422 |
8.30e-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: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 337 ETQKKNLAAENQYLRISLEKEEQALSSLQEELRQLREQIRLLEDKGTS-TQLVRENQVLKQYLEVEKQKTDSfLREREML 415
Cdd:COG2433 419 EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREiSRLDREIERLERELEEERERIEE-LKRKLER 497
|
....*..
gi 1907200551 416 LEEARML 422
Cdd:COG2433 498 LKELWKL 504
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
269-626 |
8.58e-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: 39.56 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 269 GKNEGNKGKGTIQIQKQLVRKTHEDELDGVKGYLSqRKQEQESFLDFKSLKENLERcwTVTESEKITFETQKKNLAAENQ 348
Cdd:COG5185 196 KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIIN-IEEALKGFQDPESELEDLAQ--TSDKLEKLVEQNTDLRLEKLGE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 349 YLRISLEKEEQAlSSLQEELRQLREQIRLLEDKGTSTQLVRENQVLKQYLEVEKQKTDSfLREREMLLEEarmLKRDLER 428
Cdd:COG5185 273 NAESSKRLNENA-NNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEES-KRETETGIQN---LTAEIEQ 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 429 EQLTAM----ALRAELEQFIPGQAQSR----AESPSVQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKdqhg 500
Cdd:COG5185 348 GQESLTenleAIKEEIENIVGEVELSKsseeLDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIE---- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 501 kqETDGRKRGSRGSHRAKSKSKETFLGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTT 580
Cdd:COG5185 424 --ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATL 501
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907200551 581 KNIFDeKGSKRFRAPKEAATEKTRTAYSYSSYSQQEAPNQNQNCRR 626
Cdd:COG5185 502 EKLRA-KLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIP 546
|
|
| YtxH |
pfam12732 |
YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are ... |
517-570 |
9.16e-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: 9.16e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1907200551 517 AKSKSKETFlGTVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVK 570
Cdd:pfam12732 19 APKSGKETR-KDLKDKAEDLKDKAKDLAEEAKEKAEDLKEKVKEKADELKEKVK 71
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
298-623 |
9.92e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 39.68 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 298 VKGYLSQRKQEQESFLDFKSLKENLERCWTvtESEKITFETQKKNLAAENQYLRisLEKEEQALSSLQEELRQLREQIRL 377
Cdd:COG5022 812 YRSYLACIIKLQKTIKREKKLRETEEVEFS--LKAEVLIQKFGRSLKAKKRFSL--LKKETIYLQSAQRVELAERQLQEL 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 378 LEDKGTSTQLVREN-QVLKQYLEVEKQKTDSFLREREMLLEEARMLKRDLEREQLTAMALRAELEQFIPGQAQSraESPS 456
Cdd:COG5022 888 KIDVKSISSLKLVNlELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHE--VESK 965
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 457 VQTEEKEVGLLQQRLAELEQKLIFEQQRSDLWERLYVEAKDQHGKQETD-------GRKRGSRGSHRAKSKSKETFLGTV 529
Cdd:COG5022 966 LKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQEStkqlkelPVEVAELQSASKIISSESTELSIL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907200551 530 KETFDAMKNSTKEFVRHHKE----KIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDEKGSKrfrapKEAATEKTRT 605
Cdd:COG5022 1046 KPLQKLKGLLLLENNQLQARykalKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVK-----PANVLQFIVA 1120
|
330
....*....|....*...
gi 1907200551 606 AYSYSSYSQQEAPNQNQN 623
Cdd:COG5022 1121 QMIKLNLLQEISKFLSQL 1138
|
|
| |
