|
Name |
Accession |
Description |
Interval |
E-value |
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1-524 |
0e+00 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 750.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 1 MSETETMNVNG-PQDF-YSDSPFCLEASFSSSDLLQNETKNVKRGNESVHMSSEDILSTEGSLLGDINLGNYPERIQNQP 78
Cdd:pfam15066 1 MSESDAMNVSGlSQDLtHSDSPLCMETSSTTSDLPQNEIKNVKRENESKFTLSEDIYSTLDNLLGDINIGSYSQNVLIQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 79 ANTRVSSSRQFEPICKFHWIDAFNDD-SSVPDLTRAFSYSEeKPELQSQVYNDPADASQKPDPLKEESLMESSTSENKDE 157
Cdd:pfam15066 81 VDTSISSLRQFEPICKFHWTEAFNDEmTTFQNLTEGFSYTE-KPELQSHVYNYAKDTNIKQDSFKEENPVETSISTNKDQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 158 LVHEPVRK-SRSLCLNHYRGKTRPLTETPLVRSVVVDVALNNNQPESFLGKENVCRNGENLSDSENCFDQLDLRAIYKAG 236
Cdd:pfam15066 160 LANECVRQsSRSPPLIHCSGETLPFTEKSLAKSTAKESALNPSQPQSFLYEENVPRNVEKPFYKENSFSLLDLRANYKTE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 237 KPEVSSKGIQNSGEFSDMSVGPQEEVTEDGLDSLAITSPWSPAGI-FKGRRSQDDFQMPDGELDFESLEPLEEDMALNEA 315
Cdd:pfam15066 240 ETEVSSKEIQNSGEIPEMSVSHQKEVTEEGVESPEIASTWSPAGIsWSSGASQENCKTPDTEQSFESLQPLEEDMALNEV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 316 LQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSKQHVLLDIINKLKVNVEELIDDKYNVILEKNDINKKLQDLQET 395
Cdd:pfam15066 320 LQKLKHTNRKQQMQIQDLQCSNLYLEKKVKELQMKITKQQVFVDIINKLKENVEELIEDKYNVILEKNDINKTLQNLQEI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 396 SANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQRLQRHKGELEKATSS 475
Cdd:pfam15066 400 LANTQKHLQESRKEKETLQLELKKIKVNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQQLKGELEKATTS 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 564391044 476 ALDLLKREKEIREQEFLSFQEEFQRREKENLKERRKLKSRVEKLVAQVK 524
Cdd:pfam15066 480 ALDLLKREKETREQEFLSLQEEFQKHEKENLEERQKLKSRLEKLVAQVK 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
307-564 |
2.91e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 307 EEDMALNEALQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSKQHVLLDIINKLKVNVEELIDDKYNVILEKNDIN 386
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 387 KKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERyIAEIQQKNRSVTQCL-----EIEKTLSKKDEELQR 461
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE-LEEAEEELEEAEAELaeaeeALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 462 LQRHKGELEKATSSALDLLKREKEIREQEflsfQEEFQRREkENLKERRKLKSRVEKLVAQVKSLLFTCESERAQTTALQ 541
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAE----EALLERLE-RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260
....*....|....*....|...
gi 564391044 542 QQVDALRLENLELRQQAAKREAQ 564
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAA 478
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
311-565 |
8.16e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 311 ALNEALQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSKQHV----LLDIINKLKVNVEELIDDKYNVILEKNDIN 386
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrreLEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 387 KKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQRLQRHK 466
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 467 GELEKATSSALDLLKREKEiREQEFLSFQEEFQRREKENLKERRKLKSRVEKLVAQVKSLLftcesERAQTTALQQQVDA 546
Cdd:COG1196 424 EELEEALAELEEEEEEEEE-ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL-----EELAEAAARLLLLL 497
|
250
....*....|....*....
gi 564391044 547 LRLENLELRQQAAKREAQA 565
Cdd:COG1196 498 EAEADYEGFLEGVKAALLL 516
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
381-563 |
5.78e-08 |
|
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: 55.93 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 381 EKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIkvhyvrlqERYIAEIQQKNRSVTQCL-EIEKTLSKKDEEL 459
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL--------ERRIAALARRIRALEQELaALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 460 QRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQR--REKENLKE-RRKLKSRVEKLVAQVKSLLFTCESERAQ 536
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELAALRAELEAE 172
|
170 180
....*....|....*....|....*..
gi 564391044 537 TTALQQQVDALRLENLELRQQAAKREA 563
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQK 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
298-559 |
1.93e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 298 LDFESLEplEEDMALNEALQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKV-SKQHVLLDI---INKLKVNVEELID 373
Cdd:TIGR02168 232 LRLEELR--EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeELQKELYALaneISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 374 ---------DKYNVILEKNDinKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTQ 444
Cdd:TIGR02168 310 rlanlerqlEELEAQLEELE--SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 445 CLEIEKTLSKKDEELQRLQRHKGELEKAtssaLDLLKREKEIREQEFLSFQ-EEFQRREKENLKERRKLKSRVEKLVAQV 523
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDR----RERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEAL 463
|
250 260 270
....*....|....*....|....*....|....*.
gi 564391044 524 KSLlftceseRAQTTALQQQVDALRLENLELRQQAA 559
Cdd:TIGR02168 464 EEL-------REELEEAEQALDAAERELAQLQARLD 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-581 |
3.02e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 283 KGRRSQDDFQMPDGELDFESLEPLEEDMALNEALQKLkqtnkkqelqiQDLHGRNLTLESRVQELQTKVSKQHvllDIIN 362
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-----------SDASRKIGEIEKEIEQLEQEEEKLK---ERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 363 KLKVNVEELIDDKYNVILEKNDINKKLQDLQETSANTKKHLQESKKDQ-----ESLQLQVKKIKVHYVRLQERyIAEIQQ 437
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEAR-LREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 438 KNRSVTQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKENLKERRKLKSRVE 517
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564391044 518 KLVAQVKSLLFTCESERAQTTALQQQVDALRLENLEL-RQQAAKREAQACTPSFEIIQPK-EKLEE 581
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAElQRVEE 965
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
361-565 |
7.11e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 7.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 361 INKLKVNVEELIDDKYNVILEKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERY---IAEIQQ 437
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 438 KNRSVTQcleIEKTLSKKD--EELQRLQRhkgeLEKATSSALDLLKREKEIREQeflsfQEEFQRREKENLKERRKLKSR 515
Cdd:COG3883 98 SGGSVSY---LDVLLGSESfsDFLDRLSA----LSKIADADADLLEELKADKAE-----LEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564391044 516 VEKLVAQVKSLLftcESERAQTTALQQQVDALRLENLELRQQAAKREAQA 565
Cdd:COG3883 166 LEAAKAELEAQQ---AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
296-589 |
1.09e-06 |
|
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: 52.75 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 296 GELDfESLEPLEEDMALNEALQKLKQ--TNKKQELQIQDLHGRNLTLESRVQELQTKVSKQHVLLDIINKLKVNVEELID 373
Cdd:TIGR02168 196 NELE-RQLKSLERQAEKAERYKELKAelRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 374 DKYNVILEKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQvkkikvhyvrlQERYIAEIQQKnrsvtqcleiEKTLS 453
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ-----------LEELEAQLEEL----------ESKLD 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 454 KKDEELQRLQRHKGELEKATSSALDLLKREKEIreqeflsfQEEFQRREKENLKERRKLKSRVEKLVAQVKSLLFTCESE 533
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAE--------LEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 564391044 534 RAQTTALQQQVDALRLENLELRQQAAKREAQACTPSF-EIIQPKEKLEEVVEPDVTQ 589
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELeELEEELEELQEELERLEEA 462
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
380-698 |
1.27e-06 |
|
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: 52.37 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 380 LEKNDIN-KKLQDLqetsantkkhLQESKKDQESLQLQVKK------------------IKVHYVRLQERYIAEIQQKNR 440
Cdd:TIGR02168 181 LERTRENlDRLEDI----------LNELERQLKSLERQAEKaerykelkaelrelelalLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 441 SVTQCLEIEKTLSKKDEELQRLQRHKGELEKATSSA---LDLLKREKEIREQEFLSFQEEFQRREKENLK---ERRKLKS 514
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELqkeLYALANEISRLEQQKQILRERLANLERQLEEleaQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 515 RVEKLVAQVKSLLFTCESERAQTTALQQQVDALRLENLELRQQAAKREAQACTPSFEIIQPKEKLEEVVEPDVTQDTKGT 594
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 595 HcnLFLNCSSCKENPELPSMKRTSPLTSRLHSLLALTIGLLTCQDLAIPDTELRQESKKandimlQRLKDCQLRKKDLDK 674
Cdd:TIGR02168 411 R--LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELR------EELEEAEQALDAAER 482
|
330 340
....*....|....*....|....
gi 564391044 675 ELLKHRNRIATLKELIANEKALQD 698
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
368-584 |
2.22e-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: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 368 VEELIDDKYNVILEKNDINKKLQDlqetsantkkhlqESKKDQESLQLQVKKIKVHYVRLqeryiaeIQQKNRSVTQCLE 447
Cdd:TIGR02169 182 VEENIERLDLIIDEKRQQLERLRR-------------EREKAERYQALLKEKREYEGYEL-------LKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 448 IEKTLSKKDEELQRLQRHKGELEKATSSALDLL----KREKEIREQEFLSFQEEF-----------------QRREKENL 506
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLeelnKKIKDLGEEEQLRVKEKIgeleaeiaslersiaekERELEDAE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564391044 507 KERRKLKSRVEKLVAQVKSLLFTCESERAQTTALQQQVDALRLENLELRQQAAKREAQACTPSFEIIQPKEKLEEVVE 584
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
304-565 |
4.94e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 304 EPLEEDMALNEALQKLKQT---NKKQEL--QIQDLHGRNLTLESRVQELQTKVSKQHVLLDIINKLKVNVEELIDDKYNV 378
Cdd:TIGR02169 208 EKAERYQALLKEKREYEGYellKEKEALerQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 379 ilEKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQ------ERYIAEIQQKNRSVTQCL-EIEKT 451
Cdd:TIGR02169 288 --EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLaeieelEREIEEERKRRDKLTEEYaELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 452 LSKKDEELQRLQRHKGELEKATSS---ALDLLKREKEIREQEFLSFQEEFQRREKENLKERRKLKS-------------- 514
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDyreKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGieakineleeeked 445
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564391044 515 ---RVEKLVAQVKSLLFTCESERAQTTALQQQVDALRLENLELRQQAAKREAQA 565
Cdd:TIGR02169 446 kalEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
285-527 |
1.06e-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: 49.28 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 285 RRSQDDFQMPDGELDFESLEPLEEDMALNEALQKLKQTN-----KKQELQIQDLHGRNL--TLESRVQELQTKVSKQHVL 357
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAneisrLEQQKQILRERLANLerQLEELEAQLEELESKLDEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 358 LDIINKLKVNVEELIDDKYNVILEKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERY--IAEI 435
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLerLEDR 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 436 QQKNRSVTQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKENLKERRK---- 511
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdsle 495
|
250
....*....|....*..
gi 564391044 512 -LKSRVEKLVAQVKSLL 527
Cdd:TIGR02168 496 rLQENLEGFSEGVKALL 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
297-581 |
1.09e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 297 ELDFESLEpLEEDMALNEALQKLKQTNKKQELQIQDLHGRNLT-----------LESRVQELQTKVSKQHVLLDIINKLK 365
Cdd:pfam02463 157 EIEEEAAG-SRLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkeqakkaLEYYQLKEKLELEEEYLLYLDYLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 366 VNVEELIDDKYNVILEKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQER-YIAEIQQKNRSVTQ 444
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSeLLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 445 CLEIEKTLSKKDEELQRLQRHKGELEKATSSAldLLKREKEIREQEFLSFQEEFQRREKENLKERRKLKSRVEKLVAQVK 524
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKEL--EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 564391044 525 SLLFTCESERAQTTALQQQVDALRLENLELRQQAAKREAQACTPSFEIIQPKEKLEE 581
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
383-565 |
1.12e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 48.54 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 383 NDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKikvhyvrlQERYIAEIQQKNRSVTQCLE-IEKTLSKKDEELQR 461
Cdd:PRK11637 43 SDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKK--------QEEAISQASRKLRETQNTLNqLNKQIDELNASIAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 462 LQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREK----------------ENLKERRK----LKSRVEKLVA 521
Cdd:PRK11637 115 LEQQQAAQERLLAAQLDAAFRQGEHTGLQLILSGEESQRGERilayfgylnqarqetiAELKQTREelaaQKAELEEKQS 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564391044 522 QVKSLLFT----------CESERAQT-TAL-------QQQVDALRLENLELRQQAAKREAQA 565
Cdd:PRK11637 195 QQKTLLYEqqaqqqkleqARNERKKTlTGLesslqkdQQQLSELRANESRLRDSIARAEREA 256
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
311-564 |
2.46e-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: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 311 ALNEALQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSKQHVLLDIINKLKVNVEELIDDKYNVILEKNDINKKLQ 390
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 391 DLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQRLQRHKGELE 470
Cdd:TIGR02168 786 ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 471 KATSSALDLLKREKEIREQEFLsfqeefqrrekenlkERRKLKSRVEKLVAQVKSLlftcESERaqtTALQQQVDALR-- 548
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEE---------------ALALLRSELEELSEELREL----ESKR---SELRRELEELRek 923
|
250
....*....|....*.
gi 564391044 549 LENLELRQQAAKREAQ 564
Cdd:TIGR02168 924 LAQLELRLEGLEVRID 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
297-526 |
4.10e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 297 ELDFESLEPLEEDMALNEALQKLKQTNKKQELQIQDLHGRNLTLESRVQELQtkvskqhvllDIINKLKVNVEELIDDKY 376
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR----------AELTLLNEEAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 377 NVILEKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNR-------SVTQCLEIE 449
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlrseleeLSEELRELE 907
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564391044 450 KTLSKKDEELQRLQRHKGELEKATSSALDLLKREKE-IREQEFLSFqEEFQRREKENLKERRKLKSRVEKLVAQVKSL 526
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErLSEEYSLTL-EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
341-548 |
4.13e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.06 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 341 ESRVQELQTKVSkqhVLLDIINKLKvNVEELIDDKYNVILEK--NDINKKLQDLQETSANTKKHLQES----KKDQESLQ 414
Cdd:pfam09731 254 SERIVFQQELVS---IFPDIIPVLK-EDNLLSNDDLNSLIAHahREIDQLSKKLAELKKREEKHIERAlekqKEELDKLA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 415 LQVKKIKVHYVRLQERYIAEIQQKnrsvtqclEIEKTLSKKDEELqrlqrhKGELEKATSSALDLLKREKEIREQEflsF 494
Cdd:pfam09731 330 EELSARLEEVRAADEAQLRLEFER--------EREEIRESYEEKL------RTELERQAEAHEEHLKDVLVEQEIE---L 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564391044 495 QEEFQRREKENL-KERRKLKSRVEKLVAQVKSL------LFTCESERAQTTALQQQVDALR 548
Cdd:pfam09731 393 QREFLQDIKEKVeEERAGRLLKLNELLANLKGLekatssHSEVEDENRKAQQLWLAVEALR 453
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
311-571 |
1.37e-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: 45.14 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 311 ALNEALQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSKQHVLLdiinklkvnveeliddkynvilekNDINKKLQ 390
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI------------------------RALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 391 DLQETSANTKKHLQESKKDQESLQLQVKK-IKVHYVRLQERYIA------EIQQKNRSvtqcLEIEKTLSKKD-EELQRL 462
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEELAElLRALYRLGRQPPLAlllspeDFLDAVRR----LQYLKYLAPARrEQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 463 QRHKGELEKatssaldlLKREKEIREQEflsfQEEFQRREKENLKERRKLKSRVEKLVAQVKSLLftcESERAQTTALQQ 542
Cdd:COG4942 156 RADLAELAA--------LRAELEAERAE----LEALLAELEEERAALEALKAERQKLLARLEKEL---AELAAELAELQQ 220
|
250 260
....*....|....*....|....*....
gi 564391044 543 QVDALRLENLELRQQAAKREAQACTPSFE 571
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
403-564 |
1.50e-04 |
|
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: 45.50 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 403 LQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQR--------LQRHKGELEKATS 474
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRkiqqqkveMEQIRAEQEEARQ 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 475 SALDLLKREKE-----IREQEF--------LSFQEEFQRREKENLKERRKLKSRVEKlvaQVKSLLFTCESERAQTTALQ 541
Cdd:pfam17380 435 REVRRLEEERAremerVRLEEQerqqqverLRQQEEERKRKKLELEKEKRDRKRAEE---QRRKILEKELEERKQAMIEE 511
|
170 180
....*....|....*....|...
gi 564391044 542 QQVDALRLENLELRQQAAKREAQ 564
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAIYEEER 534
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
339-575 |
1.76e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 339 TLESRVQELQTKVSK---QHVLLDIINKLKVNVEELiddkynvilekNDINKKLQDLQETSANTKKHLQESKKdqeslQL 415
Cdd:COG3206 186 ELRKELEEAEAALEEfrqKNGLVDLSEEAKLLLQQL-----------SELESQLAEARAELAEAEARLAALRA-----QL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 416 QVKKIKVHYVRLQERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQRLQRHKGELEKatssaldLLKREKEIREQEFLSFQ 495
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA-------QLQQEAQRILASLEAEL 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 496 EEFQRREKENLKERRKLKSRVEKLVAQvksllftceseRAQTTALQQQVDALR--LENLELRQQAAKREAQACTPSFEII 573
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPEL-----------EAELRRLEREVEVARelYESLLQRLEEARLAEALTVGNVRVI 391
|
..
gi 564391044 574 QP 575
Cdd:COG3206 392 DP 393
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
296-526 |
1.96e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 296 GELDFESLEPLEEDM-ALNEALQKLK--QTNKKQELQ-IQDLHGRNLTLESRVQELQTKVSKqhvLLDIINKLKVNVEEL 371
Cdd:PRK03918 513 KKYNLEELEKKAEEYeKLKEKLIKLKgeIKSLKKELEkLEELKKKLAELEKKLDELEEELAE---LLKELEELGFESVEE 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 372 IDDK-------YNVILEKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTq 444
Cdd:PRK03918 590 LEERlkelepfYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY- 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 445 cLEIEKTLSKKDEELQRLQRHKGELEKAtssaLDLLKREKEIREQeflsfqeefQRREKENLKerrKLKSRVEKLVAQVK 524
Cdd:PRK03918 669 -LELSRELAGLRAELEELEKRREEIKKT----LEKLKEELEEREK---------AKKELEKLE---KALERVEELREKVK 731
|
..
gi 564391044 525 SL 526
Cdd:PRK03918 732 KY 733
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
429-762 |
2.04e-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: 45.05 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 429 ERYIAEIQQKNRSVTQCLeieKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKENL-- 506
Cdd:TIGR02168 683 EEKIEELEEKIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTel 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 507 -KERRKLKSRVEK--------------LVAQVKSLLFTCESERAQTTALQQQVDALRLE--NLELRQQAAKREAQACTPS 569
Cdd:TIGR02168 760 eAEIEELEERLEEaeeelaeaeaeieeLEAQIEQLKEELKALREALDELRAELTLLNEEaaNLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 570 FEII-QPKEKLEEVVEpdvtqdtkgthcNLFLNCSSCKENPELPSMKRTSPLTSRLHSLLALTIGLLTCQDLaipDTELR 648
Cdd:TIGR02168 840 LEDLeEQIEELSEDIE------------SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL---SEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 649 QESKKANDiMLQRLKDCQLRKKDLDKELLKHRNRIATLKELIANE-KALQDHTMEITDFDTEEVKNASEAPVLLTVKLDK 727
Cdd:TIGR02168 905 ELESKRSE-LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 564391044 728 -----------YHSLNEELDFLITKLGDLLESKEDhYSRLIEENDK 762
Cdd:TIGR02168 984 lgpvnlaaieeYEELKERYDFLTAQKEDLTEAKET-LEEAIEEIDR 1028
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
316-550 |
3.89e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 316 LQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSK--------QHVLLDIINKLKVNVEELID-----DKYNVILEK 382
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEktteisntQTQLNQLKDEQNKIKKQLSEkqkelEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 383 -----NDINKKLQDL-----QETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTQCLEIEKTL 452
Cdd:TIGR04523 286 lekqlNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 453 SKKDEELQRLQR----HKGELEKATSSALDL------LKREKEIREQEFLSFQEEFQRREKE--NLKERR-KLKSRVEKL 519
Cdd:TIGR04523 366 EEKQNEIEKLKKenqsYKQEIKNLESQINDLeskiqnQEKLNQQKDEQIKKLQQEKELLEKEieRLKETIiKNNSEIKDL 445
|
250 260 270
....*....|....*....|....*....|.
gi 564391044 520 VAQVKSLLFTCESERAQTTALQQQVDALRLE 550
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
429-581 |
3.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 429 ERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQEflsfqeefqrREKENLKE 508
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE----------AELERLDA 682
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564391044 509 R----RKLKSRVEKLVAQVKSLlftcESERAQTTALQQQVDAlRLENLELRQQAAKREAQACtPSFEIIQPKEKLEE 581
Cdd:COG4913 683 SsddlAALEEQLEELEAELEEL----EEELDELKGEIGRLEK-ELEQAEEELDELQDRLEAA-EDLARLELRALLEE 753
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
313-519 |
4.13e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 313 NEALQKLKQTNKKQELQIQDLHGRNLTLEsrvQELQTKVSKqhvlldiINKLKVNVEELIDDKYNVILEKNDINKKLQDL 392
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQ---RELEEKQNE-------IEKLKKENQSYKQEIKNLESQINDLESKIQNQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 393 QETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERyIAEIQQKNRSVTqcLEIEKTLSKKDEELQRLQRHKGELEKA 472
Cdd:TIGR04523 404 EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE-IKDLTNQDSVKE--LIIKNLDNTRESLETQLKVLSRSINKI 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 564391044 473 TSSaLDLLKREKEIREQEFLSFQEEFQRREKEN---LKERRKLKSRVEKL 519
Cdd:TIGR04523 481 KQN-LEQKQKELKSKEKELKKLNEEKKELEEKVkdlTKKISSLKEKIEKL 529
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-806 |
4.22e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 301 ESLEPLEEDMALNEALQKLKQTNKKQELQIqdLHGRNLtLESRVQELQTKVSKQHVLLDIINKLKVNVEELIddkynviL 380
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEV--LREINE-ISSELPELREELEKLEKEVKELEELKEEIEELE-------K 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 381 EKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKvHYVRLQERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQ 460
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 461 RLQRHKGELEKATSSALDLLKREKEIREQ--EFLSFQEEFQR-----REKENLKERRKLKSrVEKLVAQVKSLlftcesE 533
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRleELEERHELYEEakakkEELERLKKRLTGLT-PEKLEKELEEL------E 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 534 RAQTTaLQQQVDALRLENLELRQQAAKReaqactpsfeiiqpKEKLEEvvepdvtqdtkgthcnlflncssckenpeLPS 613
Cdd:PRK03918 398 KAKEE-IEEEISKITARIGELKKEIKEL--------------KKAIEE-----------------------------LKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 614 MKRTSPLTSRlhsllaltiglltcqdlaipdtELRQESKKanDIM---LQRLKDCQLRKKDLDKELLKHRNRIATLKELI 690
Cdd:PRK03918 434 AKGKCPVCGR----------------------ELTEEHRK--ELLeeyTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 691 ANEKAL-QDHTM---------EITDFDTEEVKNASEapvlltvkldKYHSLNEELDFL---ITKLGDLLESKEDHYSRLI 757
Cdd:PRK03918 490 KKESELiKLKELaeqlkeleeKLKKYNLEELEKKAE----------EYEKLKEKLIKLkgeIKSLKKELEKLEELKKKLA 559
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 564391044 758 EendkyrrhvgsLINKVTSYEEIIKCADQRL-EISHSQIAHLEERNRHLE 806
Cdd:PRK03918 560 E-----------LEKKLDELEEELAELLKELeELGFESVEELEERLKELE 598
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
311-584 |
7.60e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 311 ALNEALQKLKQTNKKQELQIQDLhgrnltlesrVQELQTKVSKQHVLLDIINKLKVNVEEL---IDDKYNVILEKNDINK 387
Cdd:pfam05483 360 SLEELLRTEQQRLEKNEDQLKII----------TMELQKKSSELEEMTKFKNNKEVELEELkkiLAEDEKLLDEKKQFEK 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 388 KLQDLQETSANTKKHLQESKKDQESLQLQVKKIKV---HYVRLQERYIAEIQQ---KNRSVTQ-----CLEIEKTLSKKD 456
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTseeHYLKEVEDLKTELEKeklKNIELTAhcdklLLENKELTQEAS 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 457 EELQRLQRHKGELEKATSSALDLLKREKEIREQEfLSFQEEFQRREKENLKERRKLKSRVEK--------------LVAQ 522
Cdd:pfam05483 510 DMTLELKKHQEDIINCKKQEERMLKQIENLEEKE-MNLRDELESVREEFIQKGDEVKCKLDKseenarsieyevlkKEKQ 588
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564391044 523 VKSLLFTCESERAQTTALQQQVDALRLENLELRQQAAKR-------EAQACTPSFEIIQPKEKLEEVVE 584
Cdd:pfam05483 589 MKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEnkqlnayEIKVNKLELELASAKQKFEEIID 657
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
301-564 |
9.05e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 301 ESLEPLEEDMALNEALQKLKQTNKKQELQIQDlHGRNLTLESRVQELQT--KVSKQHVLLDIINKLKVNVEELIDDKYNV 378
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAE-EAKKADEAKKAEEKKKadELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 379 ILEKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQEryiaEIQQKNRSVTQCLEIEKtlsKKDEE 458
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE----EEKKKVEQLKKKEAEEK---KKAEE 1651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 459 LQrlqrhKGELEKATSSALDLLKREKEIREQEFLSFQEEFQRREKENLKERRKLKSRVEKLVAQVKSllftcESERAQTT 538
Cdd:PTZ00121 1652 LK-----KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE-----EKKKAEEL 1721
|
250 260
....*....|....*....|....*.
gi 564391044 539 ALQQQVDALRLENLELRQQAAKREAQ 564
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
301-490 |
9.63e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 301 ESLEPLEEDM-ALNEALQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSKQHVLL----DIINKLKV-----NVEE 370
Cdd:COG3883 37 AELDALQAELeELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsgGSVSYLDVllgseSFSD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 371 LID--DKYNVILEKN-DINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKvhyvrlqeryiAEIQQknrsvtQCLE 447
Cdd:COG3883 117 FLDrlSALSKIADADaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK-----------AELEA------QQAE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 564391044 448 IEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEIREQE 490
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
381-565 |
9.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 381 EKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQEryiaEIQQKNRSVTqclEIEKTLSKKDEEL- 459
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIA---EAEAEIEERREELg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 460 ---QRLQRHKGelekaTSSALDLLKREKEIreQEFLS---FQEEFQRREKENLKERRKLKSRVEKLVAQVKSLLFTCESE 533
Cdd:COG3883 90 eraRALYRSGG-----SVSYLDVLLGSESF--SDFLDrlsALSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190
....*....|....*....|....*....|..
gi 564391044 534 RAQTTALQQQVDALRLENLELRQQAAKREAQA 565
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
401-581 |
1.94e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 401 KHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRsvtQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLL 480
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE---EYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 481 KREKEIREQEFLSFQ-EEFQRR---EKENLKERRKLKSRVEKLVAQVKSLLFTCESERAQTT---------------ALQ 541
Cdd:COG4717 126 QLLPLYQELEALEAElAELPERleeLEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeelqdlaeeleELQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 564391044 542 QQVDALR--LENLELRQQAAKREAQACTPSFEIIQPKEKLEE 581
Cdd:COG4717 206 QRLAELEeeLEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
311-470 |
2.76e-03 |
|
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: 41.59 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 311 ALNEALQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSKqhvLLDIINKLKVNVEELIDDKYNVILEKNDINKKLQ 390
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK---LKREINELKRELDRLQEELQRLSEELADLNAAIA 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 391 DLQEtsantkkHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQRLQRHKGELE 470
Cdd:TIGR02169 431 GIEA-------KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE 503
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
310-587 |
3.26e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 310 MALNEALQKLKQTNKKQELQiqdlhgrnltlESRVQELQTKVSKQHVL----LDIINKLKVNVEELIDDKYNVILEKNDI 385
Cdd:pfam17380 344 MERERELERIRQEERKRELE-----------RIRQEEIAMEISRMRELerlqMERQQKNERVRQELEAARKVKILEEERQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 386 NKKLQDLQETSantkkhlQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQRLQRH 465
Cdd:pfam17380 413 RKIQQQKVEME-------QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 466 KGELE-----------KATSSALDLLKREKEIREQEFLSFQ----EEFQRREKEN-------LKERRKLKSRVEKLVaqv 523
Cdd:pfam17380 486 RKRAEeqrrkilekelEERKQAMIEEERKRKLLEKEMEERQkaiyEEERRREAEEerrkqqeMEERRRIQEQMRKAT--- 562
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564391044 524 ksllftceSERAQTTALQQQVDALRlenlELRQQAAKREAQACTPSFEIIQP--KEKLEEVVEPDV 587
Cdd:pfam17380 563 --------EERSRLEAMEREREMMR----QIVESEKARAEYEATTPITTIKPiyRPRISEYQPPDV 616
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
331-593 |
3.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 331 QDLHGRNLTLESRVQELQTKVSKqhvlldiINKLKVNVEELIDDKYNVILEKNDINKKLQDLQETSANTKKHLQESKKDQ 410
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 411 ESLQLQVKKIKVHYVRLQER---YIAEIQQKNRSVTQCLEIEKTLSKKDEELQR--------LQRHKGELEKATSSALDL 479
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEErddLLAEAGLDDADAEAVEARREELEDRDEELRDrleecrvaAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 480 LKREKEIREQeflsfQEEFQRREKENLKERRKLKSRVEKLVAQVKSLLFTCESERAQTTALQQQVDALRLENLELRQQAA 559
Cdd:PRK02224 355 EERAEELREE-----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270
....*....|....*....|....*....|....
gi 564391044 560 KREAQACTPSFEIIQPKEKLEEVVEPDVTQDTKG 593
Cdd:PRK02224 430 ELEATLRTARERVEEAEALLEAGKCPECGQPVEG 463
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-565 |
3.48e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 385 INKKLQDLQETSANTKKHlQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNRSVTQCLEIEKTLSKKDEELQRLQR 464
Cdd:COG1196 198 LERQLEPLERQAEKAERY-RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 465 HKGELEKATSSALDLLKREKEIREQEFLSFQEE----FQRREKENLKERRKLKSRVEKLVAQVKSLLFTCESERAQTTAL 540
Cdd:COG1196 277 EELELELEEAQAEEYELLAELARLEQDIARLEErrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180
....*....|....*....|....*
gi 564391044 541 QQQVDALRLENLELRQQAAKREAQA 565
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEEL 381
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
381-523 |
4.74e-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: 39.52 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 381 EKNDINKKLQDLQETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERyIAEIQQKNRSVT-----QCLEIEKTLSKK 455
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVRnnkeyEALQKEIESLKR 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 456 DEEL--QRLQRHKGELEKATSsALDLLKREKEIREQEFLSFQEEFQRREKENLKERRKLKSRVEKLVAQV 523
Cdd:COG1579 104 RISDleDEILELMERIEELEE-ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
380-508 |
6.03e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 380 LEKNDINKKLQDLQETSantKKHLQESKKDQESLQ----LQVKKiKVHyvRLQERYIAEIQQKNRSVTQ----CLEIEKT 451
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA---KRILEEAKKEAEAIKkealLEAKE-EIH--KLRNEFEKELRERRNELQKlekrLLQKEEN 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 564391044 452 LSKKDEELQRLQRhkgELEKATSSaldLLKREKEIREQEflsfqEEFQRREKENLKE 508
Cdd:PRK12704 98 LDRKLELLEKREE---ELEKKEKE---LEQKQQELEKKE-----EELEELIEEQLQE 143
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
306-761 |
6.18e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 306 LEEDMALNEALQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSKQHVLL----DIINKLKV-------NVEELIDD 374
Cdd:pfam05483 211 LEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLeesrDKANQLEEktklqdeNLKELIEK 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 375 KYNVILEKNDINKKLQ-----------DLQ-------ETSANTKKHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQ 436
Cdd:pfam05483 291 KDHLTKELEDIKMSLQrsmstqkaleeDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 437 QKNRSVTQCLEIEKTLSKKDEELQRLQRHKGELEKATSSALDLLKREKEI--REQEFLSFQEEFQRREKEN---LKERRK 511
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLldEKKQFEKIAEELKGKEQELiflLQAREK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 512 -----------LKSRVEKLVAQVKSLLFTCESERAQTTALQQQVDALRLENLELRQQAAKREAQACTPSFEIIQPKEKLE 580
Cdd:pfam05483 451 eihdleiqltaIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 581 EVV---------EPDVTQDTKGTHCNLFLNCSSCKENPELPSMKRTSPLTSRLHSLLALTIGLLTCQDLAipdtelRQES 651
Cdd:pfam05483 531 RMLkqienleekEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK------KQIE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 652 KKANDIMLQRLKDCQLRKKDLDKELLKHRNRIATLKELIANEKALQDHTMEITDFDTE-EVKNASEAPVLLTVK-----L 725
Cdd:pfam05483 605 NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEiEDKKISEEKLLEEVEkakaiA 684
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 564391044 726 DKYHSLNEELDFL----ITKLGDLLESKEDHYSRLIEEND 761
Cdd:pfam05483 685 DEAVKLQKEIDKRcqhkIAEMVALMEKHKHQYDKIIEERD 724
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
387-565 |
6.98e-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: 39.14 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 387 KKLQDLQETsantKKHLQESKKDQESLQLQVKKIKVHYVRLQERYIAEIQQKNrsvtqclEIEKTLSKKDEEL----QRL 462
Cdd:COG1579 7 RALLDLQEL----DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-------DLEKEIKRLELEIeeveARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 463 QRHKGELEKATSSaldllkrekeiREQEFLSFQEEFQRREKENLKER-RKLKSRVEKLVAQVKSLLFTCESERAQTTALQ 541
Cdd:COG1579 76 KKYEEQLGNVRNN-----------KEYEALQKEIESLKRRISDLEDEiLELMERIEELEEELAELEAELAELEAELEEKK 144
|
170 180
....*....|....*....|....*.
gi 564391044 542 QQVDAlRLENL--ELRQQAAKREAQA 565
Cdd:COG1579 145 AELDE-ELAELeaELEELEAEREELA 169
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
382-594 |
7.36e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 40.00 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 382 KNDINKKLQDLQeTSANTKKHLQESkkdqeSLQLQVKKIKVHYVR----LQERYIAEIQQKNRSvtqclEIEKTLSKKDE 457
Cdd:NF033838 64 ESHLEKILSEIQ-KSLDKRKHTQNV-----ALNKKLSDIKTEYLYelnvLKEKSEAELTSKTKK-----ELDAAFEQFKK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 458 ELQRLQRHKGELEKATSSALDLLKREKE------------IREQEFLSFQEEFQRREKENLKERRKlKSRVEKLVAQVKS 525
Cdd:NF033838 133 DTLEPGKKVAEATKKVEEAEKKAKDQKEedrrnyptntykTLELEIAESDVEVKKAELELVKEEAK-EPRDEEKIKQAKA 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564391044 526 llfTCESERAQTTalqqqvdalRLENLELRQQAAKREAQActpsfeiiQPKEKLEEVVEPDVTQDTKGT 594
Cdd:NF033838 212 ---KVESKKAEAT---------RLEKIKTDREKAEEEAKR--------RADAKLKEAVEKNVATSEQDK 260
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
316-565 |
8.75e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 316 LQKLKQTNKKQELQIQDLHGRNLTLESRVQELQTKVSKQHVLLDIINKLKVNVEELIDDKYNVILEKNDINKKLQDLQET 395
Cdd:pfam01576 105 IQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 396 SANTKKHLQESKKDQESLQLQVKKIKvhyvRLQERYIAEIQ-QKNRSVTQCLEIEKTLSKKDEELQRLQrhkGELEKATS 474
Cdd:pfam01576 185 HEAMISDLEERLKKEEKGRQELEKAK----RKLEGESTDLQeQIAELQAQIAELRAQLAKKEEELQAAL---ARLEEETA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564391044 475 SALDLLKREKEIrEQEFLSFQEEFQR----REKENlKERRKLKSRVEKLVAQVKSLLftceseraQTTALQQQVDALRLE 550
Cdd:pfam01576 258 QKNNALKKIREL-EAQISELQEDLESeraaRNKAE-KQRRDLGEELEALKTELEDTL--------DTTAAQQELRSKREQ 327
|
250
....*....|....*
gi 564391044 551 NLELRQQAAKREAQA 565
Cdd:pfam01576 328 EVTELKKALEEETRS 342
|
|
| |
