|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
345-669 |
1.96e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 345 KALAGQAELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEE 424
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 425 GLRHGLEAQVKELQLKLKHSQSpdsGKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEvASHDQEV 504
Cdd:COG1196 316 ERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL-AEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 505 EHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEETGhwqsmfQKNKEELRATKQELLQLRME 584
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE------EAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 585 KEEMEEELGEKMEVLQRDLEQARASTRDTHQVEELKKELRRTQGELKELQAEQQNQEVTGRHQNQVLEKQLAALREEADR 664
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALA 545
|
....*
gi 568924020 665 GRELE 669
Cdd:COG1196 546 AALQN 550
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
324-664 |
2.08e-12 |
|
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: 70.86 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 324 RKVSLVLEQMQPLGMVSPASTKALAGQAELTRKMEELQKKLDEevkkrqkLEPSRVGLERQLEEKAEECHRLQELLERRK 403
Cdd:TIGR02168 646 RIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEE-------LEEKIAELEKALAELRKELEELEEELEQLR 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 404 GEVQQSSKELQNMKLLLGQEEGLRHGLEAQVKELQLKLKHSQSPdsgKESLLKDLLDTRELLEELLEGKQRVEEQLRLRE 483
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE---IEELEERLEEAEEELAEAEAEIEELEAQIEQLK 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 484 RELTALK---GALKEEVASHDQEVEHVRL---QYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEET 557
Cdd:TIGR02168 796 EELKALRealDELRAELTLLNEEAANLRErleSLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 558 GHWQSMFQKNKEELRATKQELLQLRMEKEEMEEELGEkmevLQRDLEQARASTRDTH-QVEELKKELRRTQGELKELQae 636
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELRELESKRSE----LRRELEELREKLAQLElRLEGLEVRIDNLQERLSEEY-- 949
|
330 340
....*....|....*....|....*...
gi 568924020 637 QQNQEVTGRHQNQVlEKQLAALREEADR 664
Cdd:TIGR02168 950 SLTLEEAEALENKI-EDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
381-700 |
1.00e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 381 LERQLE------EKAEECHRLQELLERRKGEVQQSSKELQNMKL--LLGQEEGLRHGLEAQVKELQLKLKHSQSPDSGKE 452
Cdd:COG1196 198 LERQLEplerqaEKAERYRELKEELKELEAELLLLKLRELEAELeeLEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 453 SLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEvashDQEVEHVRLQYQRDTEQLRRSMQDATQDHAAL 532
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 533 EAERQKMSSLVRELQRELEETSEETGHWQsmfQKNKEELRATKQELLQLRMEKEEMEEELGEKMEVLQRDLEQARASTRD 612
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 613 ThQVEELKKELRRTQGELKELQAEQQNQEVTGRHQNQVLEKQLAALREEADRGRELEQQNLQLQKTLQQLRQDCEEASKA 692
Cdd:COG1196 431 A-ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
....*...
gi 568924020 693 RLRWHQRQ 700
Cdd:COG1196 510 VKAALLLA 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-654 |
1.82e-10 |
|
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: 64.69 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 353 LTRKMEELQKKLDEEVKKRQKlepsrvgLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGLEA 432
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKE-------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 433 QVKELQLKLKHSQSPdsgKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEVASHdQEVEHVRLQYQ 512
Cdd:TIGR02168 303 QKQILRERLANLERQ---LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL-EELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 513 RDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEET-GHWQSMFQKNKEELRATKQELLQLRMEKEEMEEE 591
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568924020 592 LGEKMEVLQRDLEQARAstrdthQVEELKKELRRTQGELKELQAEQQNQEVTGRHQNQVLEKQ 654
Cdd:TIGR02168 459 LEEALEELREELEEAEQ------ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
473-701 |
5.88e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 473 QRVEEQLRLRERELTALKG-ALKEEVASHDQEVEHVRLQYQRDTEQLRR---SMQDATQDHAALEAERQKMSSLVRELQR 548
Cdd:COG1196 216 RELKEELKELEAELLLLKLrELEAELEELEAELEELEAELEELEAELAEleaELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 549 ELEETSEETGHWQSMFQKNKEELRATKQELLQLRMEKEEMEEELGEKMEVLQRDLEQARASTRDTHQVEELKKELRRTQG 628
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568924020 629 ELKELQAEQQNQEVTGRHQNQVLEKQLAALREEADRGRELEQQNLQLQKTLQQLRQDCEEASKARLRWHQRQR 701
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
357-663 |
5.94e-10 |
|
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: 62.89 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 357 MEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHG------- 429
Cdd:pfam01576 189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNalkkire 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 430 LEAQVKELQLKLKHSQSPDSGKESLLKDL---LDTRELLEELLEGKQRVEEQLRL-RERELTALKGALKEEVASHDQEVE 505
Cdd:pfam01576 269 LEAQISELQEDLESERAARNKAEKQRRDLgeeLEALKTELEDTLDTTAAQQELRSkREQEVTELKKALEEETRSHEAQLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 506 HVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSE---ETGHWQSMFQKNKEELRATKQELLQLR 582
Cdd:pfam01576 349 EMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQakqDSEHKRKKLEGQLQELQARLSESERQR 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 583 MEKEEMEEELGEKMEVLQRDLEQARA-STRDTHQVEELKKELRRTQgelkELQAEQQNQEVTGRHQNQVLEKQLAALREE 661
Cdd:pfam01576 429 AELAEKLSKLQSELESVSSLLNEAEGkNIKLSKDVSSLESQLQDTQ----ELLQEETRQKLNLSTRLRQLEDERNSLQEQ 504
|
..
gi 568924020 662 AD 663
Cdd:pfam01576 505 LE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
342-581 |
2.37e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 342 ASTKALAGQAELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLG 421
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 422 QEEGLRHGLEAQVKELQLKLkhsqspdsgkESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEVASHD 501
Cdd:COG1196 362 EAEEALLEAEAELAEAEEEL----------EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 502 QEvehvrlqyQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEETGhwqsmfQKNKEELRATKQELLQL 581
Cdd:COG1196 432 EL--------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA------ELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
455-701 |
3.22e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 455 LKDLLDTRELLEELLEGKQRVEEQLRLRER--ELTALKGALKEEVASHDQEVEHVRLQYQRDTEQL---RRSMQDATQDH 529
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAEleELEAELEELEAELAELEAELEELRLELEELELELeeaQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 530 AALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQELLQLRMEKEEMEEELGEKMEVLQRDLEQARAS 609
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 610 TRDTHQVEELKKELRRTQGELKELQAEQQNQEVTGRHQNQVLEKQLAALREEADRGRELEQQNLQLQKTLQQLRQDCEEA 689
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250
....*....|..
gi 568924020 690 SKARLRWHQRQR 701
Cdd:COG1196 458 EEALLELLAELL 469
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-667 |
1.02e-08 |
|
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: 58.93 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 345 KALAGQAELTRKMEELQKKLDEEVKKRQKLEPSRvglerqleEKAEECHRLQELLERRKGevqqsskelqnmKLLLGQEE 424
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEKRQQLERLRRER--------EKAERYQALLKEKREYEG------------YELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 425 GLRHGLEAQVKELqlklkhsqspdSGKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKG-ALKEEVASHDQE 503
Cdd:TIGR02169 234 ALERQKEAIERQL-----------ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 504 VEhvrlQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQELLQLRM 583
Cdd:TIGR02169 303 IA----SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 584 EKEEMEEELGEkmevLQRDLEQArastrdTHQVEELKKELRRTQGELKELQAEQQNQevtgRHQNQVLEKQLAALREEAD 663
Cdd:TIGR02169 379 EFAETRDELKD----YREKLEKL------KREINELKRELDRLQEELQRLSEELADL----NAAIAGIEAKINELEEEKE 444
|
....
gi 568924020 664 RGRE 667
Cdd:TIGR02169 445 DKAL 448
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
350-692 |
1.54e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 350 QAELTRKMEELQKKLDEEVKK---RQKLEPSRVGLErqLEEKAEECHRLQELlERRKGEVQQSSKELQNMKLLLGQEEGL 426
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAeeaKKKAEEAKKADE--AKKKAEEAKKADEA-KKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 427 RHGLEAQVKELQLKLKHSQSPDSGKESLLKDLLDT--RELLEELLEGKQRVEEQLRLRERELTALKgalKEEVASHDQEV 504
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALR---KAEEAKKAEEA 1592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 505 EHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQELLQLRME 584
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 585 KEEMEEELGEKMEVLQRDLEQARASTRDTHQVEELKKELRRTQGELKELQAEQQNQEVtgrhqnqvleKQLAALREEADR 664
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI----------KAEEAKKEAEED 1742
|
330 340
....*....|....*....|....*...
gi 568924020 665 GRELEQQNLQLQKTLQQLRQDCEEASKA 692
Cdd:PTZ00121 1743 KKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
350-669 |
5.25e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.69 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 350 QAELTRKMEELQKKLDEEVKK----RQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEg 425
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKadeaKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE- 1556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 426 LRHGLEAQVKELQLKLKHSQSPDSGKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGalkEEVASHDQEVE 505
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA---EELKKAEEEKK 1633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 506 HVRLQYQRDTEQLRRSMQ--DATQDHAALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATkQELLQLRM 583
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-EELKKKEA 1712
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 584 EKEEMEEELGEKMEVLQRDLEQA-RASTRDTHQVEELKKElrrtQGELKELQAEQQNQEVTGRHQNQVLEKQLAALREEA 662
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAkKEAEEDKKKAEEAKKD----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
....*..
gi 568924020 663 DRGRELE 669
Cdd:PTZ00121 1789 DEKRRME 1795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-660 |
6.06e-08 |
|
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: 56.22 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 351 AELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNmklllgQEEGLRhGL 430
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA------LREALD-EL 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 431 EAQVKELQLKLkhsQSPDSGKESLLKDLLDTRELLeellegkQRVEEQLRLRERELTALKGALKEEVASHDQ-EVEHVRL 509
Cdd:TIGR02168 809 RAELTLLNEEA---ANLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAAEIEELEELIEElESELEAL 878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 510 QYQRDteQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETseetghwQSMFQKNKEELRATKQELLQLRMEKEEME 589
Cdd:TIGR02168 879 LNERA--SLEEALALLRSELEELSEELRELESKRSELRRELEEL-------REKLAQLELRLEGLEVRIDNLQERLSEEY 949
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568924020 590 EELGEKMEVLQRDLEQarastrdthQVEELKKELRRTQGELKE-----LQAEQQNQEVTGRHQNqvLEKQLAALRE 660
Cdd:TIGR02168 950 SLTLEEAEALENKIED---------DEEEARRRLKRLENKIKElgpvnLAAIEEYEELKERYDF--LTAQKEDLTE 1014
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
338-580 |
6.08e-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: 55.54 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 338 MVSPASTKALAGQAELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNmk 417
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 418 lLLGQEEGLRHGLEAQVKELQLKLKHSQSpdSGKESLLKDLLDTRELLEELLEGkQRVEEQLRLRERELTALKGALkeev 497
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYR--LGRQPPLALLLSPEDFLDAVRRL-QYLKYLAPARREQAEELRADL---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 498 ashdQEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEETghwqSMFQKNKEELRATKQE 577
Cdd:COG4942 160 ----AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL----AELQQEAEELEALIAR 231
|
...
gi 568924020 578 LLQ 580
Cdd:COG4942 232 LEA 234
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
346-679 |
1.45e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 346 ALAGQAELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEG 425
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 426 LRHGLEAQVKELQLKLKHSQ-SPDSGKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEVASHDQEV 504
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAvAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 505 EHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETseetghWQSMFQKNKEELRATKQELLQLRME 584
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA------ALRRAVTLAGRLREVTLEGEGGSAG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 585 KEEMEEELGEKMEVLQRDLEQARASTRDTHQVEELKKELRRTQGELKELQAEQQNQEVTGRHQNQVLEKQLAALREEADR 664
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
330
....*....|....*
gi 568924020 665 GRELEQQNLQLQKTL 679
Cdd:COG1196 740 ELLEEEELLEEEALE 754
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
324-669 |
5.78e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 324 RKVSLVLEQMQPLGMVSPASTKALAGQAELTRKMEELQKKLDEEvkkrQKLEPSRVGLERQLEEKAEECHRLQELLERRK 403
Cdd:TIGR02169 640 RMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERL----EGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 404 GEVQQSSKELQnmkLLLGQEEGLRhgleAQVKELQLKLKHSQSPDSGKESLLKDLldtrelleellegkqrvEEQLRLRE 483
Cdd:TIGR02169 716 RKIGEIEKEIE---QLEQEEEKLK----ERLEELEEDLSSLEQEIENVKSELKEL-----------------EARIEELE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 484 RELTALKGALKEEVASHDQE-VEHVRLQYQRDTEQLRR---SMQDATQDHAALEAERQKMSSLVRELQRELEETSEEtgh 559
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ--- 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 560 wQSMFQKNKEELRATKQELlqlrmekeemeeelgekmevlQRDLEQARASTRD-THQVEELKKELRRTQGELKELQAEQQ 638
Cdd:TIGR02169 849 -IKSIEKEIENLNGKKEEL---------------------EEELEELEAALRDlESRLGDLKKERDELEAQLRELERKIE 906
|
330 340 350
....*....|....*....|....*....|.
gi 568924020 639 NQEVTGRHQNQVLEKQLAALREEADRGRELE 669
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
471-695 |
7.93e-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: 52.75 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 471 GKQRVEEQLRLRERELTALKGALKEEVASHDqEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQREL 550
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 551 EETSEETGHWQSMFQKNKEELRATKQELLQLRMEKEEMEEELGEKMEVLQrDLEQARASTRDthQVEELKKELRRTQGEL 630
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE-ELESRLEELEE--QLETLRSKVAQLELQI 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568924020 631 KELQAEQQNQEVTGRHQNQVLEKQLAALREEADRGRELEQQNLQLQKTLQQLRQDCEEASKARLR 695
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
350-691 |
1.33e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 350 QAELTRKMEELQKKLDEEVKKRQKLEPSrvgleRQLEEKAEECHRLQELL----ERRKGE-VQQSSKELQNMKLLLGQEE 424
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEKKKA-----DEAKKKAEEAKKADEAKkkaeEAKKAEeAKKKAEEAKKADEAKKKAE 1480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 425 GLRHGLEAQVKELQLKLKHSQ----SPDSGKESLLKDLLDTRELLEELLEGKQRVEEQLRLRE--RELTALKGALKEEVA 498
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEakkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEekKKADELKKAEELKKA 1560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 499 SHDQEVEHVRLQYQRDTEQLRRSmQDATQDHAALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQEL 578
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 579 LQLRMEKEEMEEELGEKMEVLQRDLEQARASTRDTHQVEELKKElrrtqGELKELQAEQQNQEVTGRHQNQVLEKQLAal 658
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA-----EEDEKKAAEALKKEAEEAKKAEELKKKEA-- 1712
|
330 340 350
....*....|....*....|....*....|...
gi 568924020 659 rEEADRGRELEQQNLQLQKTLQQLRQDCEEASK 691
Cdd:PTZ00121 1713 -EEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
353-580 |
1.09e-05 |
|
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: 48.74 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 353 LTRKMEELQKKLdEEVKKRQKlepsrvGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGLEA 432
Cdd:pfam07888 141 LTQRVLERETEL-ERMKERAK------KAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 433 QVKELQLKLKHSQSPDSGKESLLKDLLDTRELLEELLEGKQRVEEQL-----------------RLRERELTA----LKG 491
Cdd:pfam07888 214 TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELssmaaqrdrtqaelhqaRLQAAQLTLqladASL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 492 ALKEEVASHDQEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRE-------LEETSEETGHWQS-- 562
Cdd:pfam07888 294 ALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREkdcnrvqLSESRRELQELKAsl 373
|
250
....*....|....*....
gi 568924020 563 -MFQKNKEELRATKQELLQ 580
Cdd:pfam07888 374 rVAQKEKEQLQAEKQELLE 392
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
352-635 |
1.23e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 352 ELTRKMEELQKKL--DEEVKKRQKlepsrvGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLR-- 427
Cdd:PRK03918 173 EIKRRIERLEKFIkrTENIEELIK------EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEke 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 428 -HGLEAQVKELQLKLKHSQSPDSGKESLLKDLldtrelleellegKQRVEEQLRLRERELTALK-GALKEEVASHDQEVE 505
Cdd:PRK03918 247 lESLEGSKRKLEEKIRELEERIEELKKEIEEL-------------EEKVKELKELKEKAEEYIKlSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 506 HVRLQYQRDTEQLRRSMQDATQDhaalEAERQKMSSLVRELQRELEETSEetghwqsmFQKNKEELRATKQELLQLRMEK 585
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEK----EERLEELKKKLKELEKRLEELEE--------RHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 568924020 586 EEMEEELgekmevLQRDLEQA-RASTRDTHQVEELKKELRRTQGELKELQA 635
Cdd:PRK03918 382 TGLTPEK------LEKELEELeKAKEEIEEEISKITARIGELKKEIKELKK 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
350-552 |
2.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 350 QAELTRKMEELQKKLDEEVKKRQKLEPSRVGL-----ERQLEEKAEECHRLQELLERRKGEVQQSSKELQnmklllgqee 424
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAELERLEARLD---------- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 425 glrhglEAQVKELQLKLKHSQSPDSGKESLLKDLldtrelleellegkQRVEEQLRLRERELTALKGA---LKEEVASHD 501
Cdd:COG4913 320 ------ALREELDELEAQIRGNGGDRLEQLEREI--------------ERLERELEERERRRARLEALlaaLGLPLPASA 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568924020 502 QEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEE 552
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
352-663 |
2.89e-05 |
|
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: 47.81 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 352 ELTRKMEELQKKLDEEVKKRQKLEPSRVG-------LERQLEEKAEECHRLQELL-----------ERRKGEVQQSSKEL 413
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLWDRDTGnsitidhLRRELDDRNMEVQRLEALLkamksecqgqmERQMAAIQGKNESL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 414 QNMKLLLGQEEGLRHGLEAQVKELQLKLKHSQSPDSGKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKG-- 491
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNeg 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 492 -----------ALKEEVASHDQEVEHVRLQYQRDTE-----------------QLRRSMQDATQDHAALEAERQKMSSLV 543
Cdd:pfam15921 541 dhlrnvqteceALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagamqvekaQLEKEINDRRLELQEFKILKDKKDAKI 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 544 RELQRELEETSEETghwQSMFQKNKEELRATKqELLQLRMEKEEMEEELGEKMEVLQRDLEQARASTRDTHQVEE----- 618
Cdd:pfam15921 621 RELEARVSDLELEK---VKLVNAGSERLRAVK-DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMEtttnk 696
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 568924020 619 LKKELRRTQGELKELQAEQQNQEVTGRHQNQV---LEKQLAALREEAD 663
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVamgMQKQITAKRGQID 744
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
351-663 |
2.90e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 351 AELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQEL------LERRKGEVQQSSKELQNMKLLLGQEE 424
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELkekaeeYIKLSEFYEEYLDELREIEKRLSRLE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 425 GLRHGLEAQVKELQLKLKHSQSPDSGKESLLKDLLDTRELLEELLEGKQRVEEQLRLREReltaLKGALKEEVASHDQEV 504
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKR----LTGLTPEKLEKELEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 505 EHVRLQYQRDTEQLRRSMQDATQDHA-------ALEAERQKMSSLVRELQRE-----LEETSEETGHWQSMFQKNKEELR 572
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKelkkaieELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 573 ATKQELLQLRMEKEEMEEELGEKMEVLQ-RDLEQaRASTRDTHQVEELKKELRRTQGELKELQAEQQNQEVTGRHQNQvL 651
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQlKELEE-KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE-L 554
|
330
....*....|..
gi 568924020 652 EKQLAALREEAD 663
Cdd:PRK03918 555 KKKLAELEKKLD 566
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
475-669 |
4.56e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 475 VEEQLRLRERELTALKGALKEEVASHDQEVEHVRLQYQR------------DTEQLRRSMQDATQDHAALEAERQKMSSL 542
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlseEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 543 VRELQRELEETSEETGhwqsmFQKNKEELRATKQELLQLrmekeemeeelgekmevlQRDLEQARASTRDTH-QVEELKK 621
Cdd:COG3206 242 LAALRAQLGSGPDALP-----ELLQSPVIQQLRAQLAEL------------------EAELAELSARYTPNHpDVIALRA 298
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 568924020 622 ELRRTQGELKE----LQAEQQNQEVTGRHQNQVLEKQLAALREEADRGRELE 669
Cdd:COG3206 299 QIAALRAQLQQeaqrILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-582 |
5.89e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 352 ELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGLE 431
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 432 AQVKELQLKLkhsqspdsgkESLLKDLLDTRELleellegkqrvEEQLRLRERELTALKGALKEEVASHDQEVEhvrlqy 511
Cdd:TIGR02168 372 SRLEELEEQL----------ETLRSKVAQLELQ-----------IASLNNEIERLEARLERLEDRRERLQQEIE------ 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568924020 512 QRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEEtghwqsmFQKNKEELRATKQELLQLR 582
Cdd:TIGR02168 425 ELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE-------LEEAEQALDAAERELAQLQ 488
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
385-627 |
6.02e-05 |
|
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: 46.43 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 385 LEEKAEECHR-LQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGLEAQVKELQLKLKHSQSPDSGKESLLKDLLDTRE 463
Cdd:pfam07888 32 LQNRLEECLQeRAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 464 LLEELLEGKQRVEEQLRLRERELTALKGALKEEVASHDQEVEHVRLQYQRDTEQLRRSmqdatqdhaalEAERqkmsslv 543
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-----------EAER------- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 544 RELQRELEETSEETGHWQSMFQKNKEELRATKQELLQLRMEKEEmeeelgekmevLQRDLEQARastRDTHQVEELKKEL 623
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT-----------LTQKLTTAH---RKEAENEALLEEL 239
|
....
gi 568924020 624 RRTQ 627
Cdd:pfam07888 240 RSLQ 243
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
381-581 |
6.22e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 381 LERQLEEKAEECHRLQ----ELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGLEAQVKELQLKLKHSQSpdsgKESLLK 456
Cdd:COG4717 47 LLERLEKEADELFKPQgrkpELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE----ELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 457 DLLDTRELLEELLEGKQRVE------EQLRLRERELTALKGALKEEVASHDQEVEHVRLQYQRDTEQLRRSMQDATQDHA 530
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 568924020 531 ALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQELLQL 581
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
348-692 |
8.15e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 348 AGQAELTRKMEELQKKldEEVKKRQklEPSRVGLERQLEE--KAEECHRLQEL-----LERRKGEVQQSSKELQNMKLLL 420
Cdd:PTZ00121 1181 ARKAEEVRKAEELRKA--EDARKAE--AARKAEEERKAEEarKAEDAKKAEAVkkaeeAKKDAEEAKKAEEERNNEEIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 421 GQEEGLRHGLEAQVKELQLKLKHSQSPDSGKESLLKDLLDTRELLEELLEGKQRVEE-----QLRLRERELTALKGALKE 495
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakkadEAKKKAEEAKKKADAAKK 1336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 496 EVASHDQEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQR-----ELEETSEETGHWQSMFQKNKEE 570
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadEAKKKAEEDKKKADELKKAAAA 1416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 571 LRatKQELLQLRMEKEEMEEELGEKMEVlQRDLEQARASTRDTHQVEELKK--ELRRTQGELKElQAEQQNQEVTGRHQN 648
Cdd:PTZ00121 1417 KK--KADEAKKKAEEKKKADEAKKKAEE-AKKADEAKKKAEEAKKAEEAKKkaEEAKKADEAKK-KAEEAKKADEAKKKA 1492
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 568924020 649 QVLEKQLAALREEADRGRELEQQNLQLQKTLQQLRQDCEEASKA 692
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA 1536
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
348-664 |
1.48e-04 |
|
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: 45.35 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 348 AGQAELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEEchrlqellERRKGEVQQSSKELQNMKLLLGQEEGLR 427
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ--------AKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 428 HgLEAQVKELQLKLKHSQSpdsgKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEVAShdqEVEHV 507
Cdd:pfam02463 234 L-NEERIDLLQELLRDEQE----EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS---ELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 508 RLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQrELEETSEETGHWQSMFQKNKEELRATKQELLQLRMEKEE 587
Cdd:pfam02463 306 ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 588 MEEELGEKM--------EVLQRDLEQARASTRDTHQVEELKKELRRTQGELKELQAEQQNQEVTGRHQNQVLEKQLAALR 659
Cdd:pfam02463 385 RLSSAAKLKeeelelksEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
....*
gi 568924020 660 EEADR 664
Cdd:pfam02463 465 LELKK 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-580 |
2.07e-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: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 351 AELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGL 430
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 431 EAQVKELQLKLKHSQSPDSGKESLLKDLLDTRelleellegKQRVEEQLRLRERELTALKGALKEEVASHDQEVEHVRLQ 510
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRR---------ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 511 YQRDTEQLRRsmqdatqdhaaLEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQELLQ 580
Cdd:TIGR02168 456 LERLEEALEE-----------LREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
317-661 |
2.16e-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: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 317 ESEASVRRKVSLVLEQMQPLGMVSPASTKALAGQAELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQL----EEKAEEC 392
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvvedDEVAAAA 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 393 hrLQELLERRKGEV------QQSSKELQNMKLLLGQEEGLRHGLEAQVKELQLKLKhsqspDSGKESLLKDLLDTRELLE 466
Cdd:COG1196 563 --IEYLKAAKAGRAtflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYY-----VLGDTLLGRTLVAARLEAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 467 ELLEGKQRVEEQLRLRERELTALKGALKEEVASHDQEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVREL 546
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 547 QRELEETSEEtghwqsmfQKNKEELRATKQELLQLRMEKEemeeelgekmevlqrDLEQARASTRDTHQVEELKKELRRT 626
Cdd:COG1196 716 RLEEELEEEA--------LEEQLEAEREELLEELLEEEEL---------------LEEEALEELPEPPDLEELERELERL 772
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 568924020 627 QGELKEL-----QAEQQNQEVTGRHQNqvLEKQLAALREE 661
Cdd:COG1196 773 EREIEALgpvnlLAIEEYEELEERYDF--LSEQREDLEEA 810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
297-573 |
2.76e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 297 PGSADHVKATIYGILREGSSESEASVRRKVSLVLEQMQPLGMVSPASTKALAGQAELTRKMEELQKKLDEEVKKRQKLEP 376
Cdd:TIGR02169 662 PRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 377 SRV---GLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQE------------EGLRHGLEAQVKELQLKL 441
Cdd:TIGR02169 742 LEEdlsSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiqaelsklEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 442 KHSQSPDSGKESLLKDLLDTRELLEELLEGKQRVEEQLRLR--------------ERELTALKGALKEEVASHDQEVEHV 507
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeeleeleaaLRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568924020 508 RLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEET--GHWQSMFQKNKEELRA 573
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
474-669 |
3.37e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 474 RVEEQLRLRERELTALKGALKEeVASHDQEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEET 553
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 554 SEETGHWQSMFQKNKEELRATKQELLQLRMekeemeeelgekmevlqrdleqarastrdthQVEELKKELRRTQGELKEL 633
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEA-------------------------------QIEQLKEELKALREALDEL 808
|
170 180 190
....*....|....*....|....*....|....*.
gi 568924020 634 QAEQQNQEVTGRHQNQVLEKQLAALREEADRGRELE 669
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
343-642 |
3.71e-04 |
|
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: 43.79 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 343 STKALAGQAELTRKMEELQKKLDEEVKK-RQKLEPS--RVGLERQLEEKAEECHRLQEL--LERRKGEVQQSSKELQnMK 417
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENtKEKIAEYtkSIDIKKATESLEEQLAAAEAEqeLEESKRETETGIQNLT-AE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 418 LLLGQeEGLRHGLEAQVKELQLKLKHSQSPDSGKEslLKDLLDTRELLeellegKQRVEEQLRLRERELTALKGALKEEV 497
Cdd:COG5185 345 IEQGQ-ESLTENLEAIKEEIENIVGEVELSKSSEE--LDSFKDTIEST------KESLDEIPQNQRGYAQEILATLEDTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 498 ASHDQEVEHVrlqyQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRElqrelEETSEETGHWQSMFQKNKEELRATKQE 577
Cdd:COG5185 416 KAADRQIEEL----QRQIEQATSSNEEVSKLLNELISELNKVMREADE-----ESQSRLEEAYDEINRSVRSKKEDLNEE 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568924020 578 LLQLRMEKEEMEEELGEKMEVLQRDLEQARAStrdTHQVEELKKELRRTQGELKELQAEQQNQEV 642
Cdd:COG5185 487 LTQIESRVSTLKATLEKLRAKLERQLEGVRSK---LDQVAESLKDFMRARGYAHILALENLIPAS 548
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
330-664 |
4.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 330 LEQMQPLGMVSPASTKALAGQAELTRKMEELQKkLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQEL--------LER 401
Cdd:COG4717 118 LEKLEKLLQLLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQlslateeeLQD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 402 RKGEVQQSSKELQNMKLLLGQEEGLRHGLEAQVKELQLKLKHSQSPDSGKE----------------------------- 452
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEarlllliaaallallglggsllsliltia 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 453 --------SLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEVASHDQEVEHVRLQYQR--DTEQLRRSM 522
Cdd:COG4717 277 gvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieELQELLREA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 523 QDATQDhAALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQELLQLRMEKEEMEEELGEKMevLQRD 602
Cdd:COG4717 357 EELEEE-LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEE 433
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568924020 603 LEQARASTRDTH-QVEELKKELRRTQGELKELQAEQQNQEVtgRHQNQVLEKQLAALREEADR 664
Cdd:COG4717 434 LEELEEELEELEeELEELREELAELEAELEQLEEDGELAEL--LQELEELKAELRELAEEWAA 494
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
403-704 |
6.72e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 403 KGEVQQSSKELQNMKLLLGQEEGLRHG----LEAQVKELQLKLKHSQSPDSGKESLLKdLLDTRELLEELLEGKQRVEEQ 478
Cdd:TIGR00618 193 HGKAELLTLRSQLLTLCTPCMPDTYHErkqvLEKELKHLREALQQTQQSHAYLTQKRE-AQEEQLKKQQLLKQLRARIEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 479 LRLRERELTALKGAL-----KEEVASHDQEVEHVRLQYQRDTEQLRRSMQDATQ------DHAALEAERQKMSSLVRELQ 547
Cdd:TIGR00618 272 LRAQEAVLEETQERInrarkAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKllmkraAHVKQQSSIEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 548 RELEETSEETGHwQSMFQKNKEELRATKQELLQLRMEKEEMEEELGEKMEVL-QRDLEQARASTRDTHQ-VEELKKELRR 625
Cdd:TIGR00618 352 SQEIHIRDAHEV-ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELdILQREQATIDTRTSAFrDLQGQLAHAK 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568924020 626 TQGELKELQAEQQNQEVTGRHQNQVLEKqlAALREEADRGRELEQQNLQLQKTLQQLRQDCEEASKARLRWHQRQRPWC 704
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKLEK--IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLC 507
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
396-641 |
7.15e-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: 42.44 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 396 QELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGLEAQVKELQLKLKHSQspdsgkesllKDLLDTRELLEELLEGKQRV 475
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA----------RRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 476 EEQLRLRERELTALKGALKEEVASHDQEVEHVRLQY---QRDTEQLRRSMQdatqdhaALEAERQKMSSLVRELQRELEE 552
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQ-------YLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 553 TSEEtghwQSMFQKNKEELRATKQELLQLRMEKEEMEEELGEKMEVLQRDLEQARAstrdthQVEELKKELRRTQGELKE 632
Cdd:COG4942 162 LAAL----RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA------ELAELQQEAEELEALIAR 231
|
....*....
gi 568924020 633 LQAEQQNQE 641
Cdd:COG4942 232 LEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
474-661 |
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 568924020 474 RVEEQLRLRERELTALKG---------ALKEEVASHDQEVEHVRLQ--------YQRDTEQLRRSMQDATQDHAALEAER 536
Cdd:COG4913 239 RAHEALEDAREQIELLEPirelaeryaAARERLAELEYLRAALRLWfaqrrlelLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 537 QKMSSLVRELQRELEETS-EETGHWQSMFQKNKEELRATKQELLQLRMekeemeeelgekmevLQRDLEQARASTRDthQ 615
Cdd:COG4913 319 DALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEA---------------LLAALGLPLPASAE--E 381
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568924020 616 VEELKKELRRTQGELKELQAEQQNQEVTGRHQNQVLEKQLAALREE 661
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
352-661 |
1.39e-03 |
|
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: 41.93 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 352 ELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGLE 431
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 432 AQVKELQ---LKLKHSQSPDSGKEslLKDLLdtrelleellegkQRVEEQLRLRERELTALKGA---LKEEVASHDQEVE 505
Cdd:TIGR04523 288 KQLNQLKseiSDLNNQKEQDWNKE--LKSEL-------------KNQEKKLEEIQNQISQNNKIisqLNEQISQLKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 506 HVRLQYQRDTEQLR---RSMQDATQDHAALEAERQKMSSLVRELQRELEETSEETGHWQS---MFQKNKEELRATKQELL 579
Cdd:TIGR04523 353 NSESENSEKQRELEekqNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEqikKLQQEKELLEKEIERLK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 580 QLRMEKEEMEEELGEKMEVLQRDLEQARASTRDTH-QVEELKKELRRTQGELKELQAE--QQNQEVTG-RHQNQVLEKQL 655
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLEtQLKVLSRSINKIKQNLEQKQKElkSKEKELKKlNEEKKELEEKV 512
|
....*.
gi 568924020 656 AALREE 661
Cdd:TIGR04523 513 KDLTKK 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
345-632 |
1.68e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 345 KALAGQAELT--RKMEELQKKLDEEVKKrqklepsrVGLErQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLlgq 422
Cdd:PRK03918 487 KVLKKESELIklKELAEQLKELEEKLKK--------YNLE-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL--- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 423 eEGLRHGLEAQVKELQLKLK--HSQSPDSGKESL------LKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALK 494
Cdd:PRK03918 555 -KKKLAELEKKLDELEEELAelLKELEELGFESVeeleerLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 495 E------EVASHDQEVEHVRLQYQRDT-EQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEEtghwqsmfqkn 567
Cdd:PRK03918 634 ElaetekRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE----------- 702
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568924020 568 KEELRATKQELlqlrmekeemeeelgekmevlqRDLEQARAstrdthQVEELKKELRRTQGELKE 632
Cdd:PRK03918 703 LEEREKAKKEL----------------------EKLEKALE------RVEELREKVKKYKALLKE 739
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-543 |
1.71e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 351 AELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGL 430
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 431 EAQVKELQLKLKHSQspdsgKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGAL---KEEVASHDQEVEHV 507
Cdd:TIGR02168 420 QQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALdaaERELAQLQARLDSL 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 568924020 508 rlqyqrdtEQLRRSMQDATQDHAALEAERQKMSSLV 543
Cdd:TIGR02168 495 --------ERLQENLEGFSEGVKALLKNQSGLSGIL 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
352-695 |
1.86e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 352 ELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKA-------EECHRLQELLERRKGEVQQSSKELQNMKLLLGQEE 424
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKrltgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 425 G-LRHGLEAqvkelqLKLKHSQSPDSGKE------------------SLLKDLLDTRELLEELLEGKQRVEEQLrLRERE 485
Cdd:PRK03918 422 KeLKKAIEE------LKKAKGKCPVCGRElteehrkelleeytaelkRIEKELKEIEEKERKLRKELRELEKVL-KKESE 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 486 LTALKG------ALKEEVASHD-QEVEHVRLQYQRDTEQLR------RSMQDATQDHAALEAERQKMSSLVRELQRELEE 552
Cdd:PRK03918 495 LIKLKElaeqlkELEEKLKKYNlEELEKKAEEYEKLKEKLIklkgeiKSLKKELEKLEELKKKLAELEKKLDELEEELAE 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 553 TSEETGhwqSMFQKNKEELRATKQEL-------LQLRMEKEEMEEELGEKMEvLQRDLEQARAstrdthQVEELKKELRR 625
Cdd:PRK03918 575 LLKELE---ELGFESVEELEERLKELepfyneyLELKDAEKELEREEKELKK-LEEELDKAFE------ELAETEKRLEE 644
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568924020 626 TQGELKELQ---AEQQNQEVTGRHQNqvLEKQLAALREEADrgrELEQQNLQLQKTLQQLRQDCEEASKARLR 695
Cdd:PRK03918 645 LRKELEELEkkySEEEYEELREEYLE--LSRELAGLRAELE---ELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
351-508 |
2.04e-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: 40.29 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 351 AELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHgL 430
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE-Y 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568924020 431 EAQVKELQ-LKLKHSQSpdsgkESLLKDLLDTRELLEELlegKQRVEEQLRLRERELTALKGALKEEVASHDQEVEHVR 508
Cdd:COG1579 92 EALQKEIEsLKRRISDL-----EDEILELMERIEELEEE---LAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
348-692 |
2.57e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 348 AGQAELTRKMEELQK----KLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELlerRKGEVQQSSKELQNMKLLLGQE 423
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKaeaaRKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEA---RKAEDAKKAEAVKKAEEAKKDA 1239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 424 EGLRHGLEAQVKELQLKLKHSQSPDSGKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEVASHDQE 503
Cdd:PTZ00121 1240 EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 504 VEHVRLQYQRDTEQLRRSMQDATQdhaALEAERQKMSSLVRELQRElEETSEETGHWQSMFQKNKEELRATKQELLQLRM 583
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKK---AAEAAKAEAEAAADEAEAA-EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 584 EKEEMEEELGEKMEVLQRDLEQARAstrdthqvEELKK---ELRRTQGELKELQAEQQNQEVTGRHQNQVLEKQLAALRE 660
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKA--------DEAKKkaeEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
|
330 340 350
....*....|....*....|....*....|..
gi 568924020 661 EADRGRELEQQNLQLQKTLQQLRQDCEEASKA 692
Cdd:PTZ00121 1468 EAKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1499
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
350-555 |
2.72e-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: 41.31 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 350 QAELTRkmEELQKKLDEEVKKRQKLEPSRVGLE---RQLEEKAEECHRLQELLERR----KGEVQQSSKELQNMKLLLGQ 422
Cdd:pfam01576 858 QAQQER--DELADEIASGASGKSALQDEKRRLEariAQLEEELEEEQSNTELLNDRlrksTLQVEQLTTELAAERSTSQK 935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 423 EEGLRHGLEAQVKELQLKLKHSQSPDSGKESLLKDLLDTRELLEELLEGKQRVEEQ-----LRLRERELTALKGALKEEV 497
Cdd:pfam01576 936 SESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQaanklVRRTEKKLKEVLLQVEDER 1015
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568924020 498 ASHDQEVEHVRLQYQRdTEQLRRSMQDAtqdhaalEAERQKMSSLVRELQRELEETSE 555
Cdd:pfam01576 1016 RHADQYKDQAEKGNSR-MKQLKRQLEEA-------EEEASRANAARRKLQRELDDATE 1065
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
472-696 |
3.16e-03 |
|
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: 40.52 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 472 KQRVEEQLRLRERELTALKGALKEEVASHDqEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELE 551
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEK-ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 552 ETSEETGHWQSMFQKNKeelRATKQELLQLRMEKEEMEEELGEKMEVLQRDLEQARASTRDTHQVEELKKELRRTQGELK 631
Cdd:COG4942 101 AQKEELAELLRALYRLG---RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 632 ELQAEQQNQEVTGRHQNQ-------VLEKQLAALREEADR--------GRELEQQNLQLQKTLQQLRQDCEEASKARLRW 696
Cdd:COG4942 178 ALLAELEEERAALEALKAerqkllaRLEKELAELAAELAElqqeaeelEALIARLEAEAAAAAERTPAAGFAALKGKLPW 257
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
330-669 |
3.62e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 330 LEQMQPLGMVSPASTKALAGQAELTRKMEELQKKLDEEVK-----KRQKLEpsrvGLERQLEEKAEECHRLQELLERRKG 404
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPdtyheRKQVLE----KELKHLREALQQTQQSHAYLTQKRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 405 EVQQSSKELQNMKLLLGQEEGLRhGLEAQVKELQLKLKHSQSpdsgKESLLKDLLDTRELLEELLEGKQRVEEQLRLRER 484
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELR-AQEAVLEETQERINRARK----AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 485 ELTALKGALKEevashdqevehvrlqyQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETsEETGHWQSMF 564
Cdd:TIGR00618 326 LLMKRAAHVKQ----------------QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT-QHIHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 565 QKNKEELRATKQELLQLRMEKEEMEEELGEKM-------------EVLQRDLEQARASTRDTHQVEELKK-ELRRTQGEL 630
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQREQATIDTRTSAFRdlqgqlahakkqqELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSL 468
|
330 340 350
....*....|....*....|....*....|....*....
gi 568924020 631 KELQAEQQNQEVTGRHQNQVLEKQLAALREEADRGRELE 669
Cdd:TIGR00618 469 KEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLC 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
351-556 |
4.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 351 AELTRKMEELQKKLDEEVKKRQKLEpsrvGLERQLEEKAEECHRLQELLERRKgEVQQSSKELQNmklllgqeeglrhgL 430
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALE----AELDALQERREALQRLAEYSWDEI-DVASAEREIAE--------------L 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 431 EAQVKELQLklkhsqspDSGKESLLKDLLDTRelleellegkQRVEEQLRLRERELTALKGALKEEVASHDQEVEHVRLQ 510
Cdd:COG4913 674 EAELERLDA--------SSDDLAALEEQLEEL----------EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 568924020 511 YQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEE 556
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRAR 781
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
352-668 |
4.05e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 352 ELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAeecHRLQELLERRKGEVQQSSKELQNMKLLLGQEEGLRHGLE 431
Cdd:pfam15921 114 DLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV---HELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 432 AQVKELQlklkhsqsPDSGKESLLKDLLDTRELLEELLEgkqrVEEQLRLRERELTALKGAL------KEEVASHDQ-EV 504
Cdd:pfam15921 191 SILVDFE--------EASGKKIYEHDSMSTMHFRSLGSA----ISKILRELDTEISYLKGRIfpvedqLEALKSESQnKI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 505 EHVRLQYQRDTEQLrrsMQDATQDHAALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQEllqlrme 584
Cdd:pfam15921 259 ELLLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQ------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 585 keemeeelgekmevLQRDLEQARASTRDthQVEELKKELRRTQGELKELQAEQ-QNQEVTGRHQNQvLEKQLAALREead 663
Cdd:pfam15921 329 --------------LRSELREAKRMYED--KIEELEKQLVLANSELTEARTERdQFSQESGNLDDQ-LQKLLADLHK--- 388
|
....*
gi 568924020 664 RGREL 668
Cdd:pfam15921 389 REKEL 393
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
352-667 |
4.17e-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: 40.48 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 352 ELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKlllgqeeGLRHGLE 431
Cdd:pfam05483 332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT-------KFKNNKE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 432 AQVKELQLKLKHSQSpdsgkesllkdLLDTRELLeellegkQRVEEQLRLRERELTALKGALKEEVasHDQEVEhvrlqy 511
Cdd:pfam05483 405 VELEELKKILAEDEK-----------LLDEKKQF-------EKIAEELKGKEQELIFLLQAREKEI--HDLEIQ------ 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 512 qrdteqlrRSMQDATQDHAALEAERQKMsslvrELQRELEETSEETGHWQSMFQKNKEELRATKQELLQLRMEKEEMEEE 591
Cdd:pfam05483 459 --------LTAIKTSEEHYLKEVEDLKT-----ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINC 525
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568924020 592 LGEKMEVLQR--DLEQARASTRDthQVEELKKELRRTQGELKELQAEQQNQEVTGRHQNQVLEKQLAALREEADRGRE 667
Cdd:pfam05483 526 KKQEERMLKQieNLEEKEMNLRD--ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKK 601
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
345-436 |
5.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 345 KALAGQAELTRKMEELQKKLDEEVKKRQKL---EPSRVGLERQLEEKAEECHRLQELLERRKGE---VQQSSKELQNmkl 418
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELkkaEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEkkkIAHLKKEEEK--- 1768
|
90
....*....|....*...
gi 568924020 419 llgQEEGLRHGLEAQVKE 436
Cdd:PTZ00121 1769 ---KAEEIRKEKEAVIEE 1783
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
476-666 |
6.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 476 EEQLRLRERELTALKgalkEEVASHDQEVEHVRLQYQRDTEQLRrsmqdATQDHAALEAERQKmsslVRELQRELEETSE 555
Cdd:COG4913 609 RAKLAALEAELAELE----EELAEAEERLEALEAELDALQERRE-----ALQRLAEYSWDEID----VASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 556 EtghwqsmfqknKEELRATKQELLQLRMEKEEMEEElgekmevlQRDLEQARASTRDthQVEELKKELRRTQGELKELQA 635
Cdd:COG4913 676 E-----------LERLDASSDDLAALEEQLEELEAE--------LEELEEELDELKG--EIGRLEKELEQAEEELDELQD 734
|
170 180 190
....*....|....*....|....*....|..
gi 568924020 636 EQQNQEVTGR-HQNQVLEKQLAALREEADRGR 666
Cdd:COG4913 735 RLEAAEDLARlELRALLEERFAAALGDAVERE 766
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
350-667 |
8.09e-03 |
|
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: 39.62 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 350 QAELTRKMEELQKKLDEEVKKRQ---KLEPSRVGLERQLEEKAEECHRLQELLERRKGEVQQSSKELQNMKlllgqeeGL 426
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQeikNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK-------ET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 427 RHGLEAQVKELQLKlkhsqspDSGKESLLKDLLDTRELLeellegkqrvEEQLRLRERELTALKGALKE---EVASHDQE 503
Cdd:TIGR04523 435 IIKNNSEIKDLTNQ-------DSVKELIIKNLDNTRESL----------ETQLKVLSRSINKIKQNLEQkqkELKSKEKE 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 504 VehvrLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEETghwQSM-FQKNKEELRATKQELLQLR 582
Cdd:TIGR04523 498 L----KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL---NKDdFELKKENLEKEIDEKNKEI 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 583 MEKEEMEEELGEKMEVLQRDLEQARASTRD--------THQVEELKKELRRTQGELKELQAEQQNQEvtgrHQNQVLEKQ 654
Cdd:TIGR04523 571 EELKQTQKSLKKKQEEKQELIDQKEKEKKDlikeieekEKKISSLEKELEKAKKENEKLSSIIKNIK----SKKNKLKQE 646
|
330
....*....|...
gi 568924020 655 LAALREEADRGRE 667
Cdd:TIGR04523 647 VKQIKETIKEIRN 659
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
351-638 |
8.69e-03 |
|
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: 39.49 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 351 AELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQ-----------LEEKAEECHRLQELLERRKGEVQQS---SKELQNM 416
Cdd:pfam07888 76 RELESRVAELKEELRQSREKHEELEEKYKELSASseelseekdalLAQRAAHEARIRELEEDIKTLTQRVlerETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 417 KLLLGQEEGLRHGLEAQVKELQLKLKHSQSPdsgKESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEE 496
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEE---LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 497 VASHDQ--EVEHVRLQYQRDTEQLRRSMQD--ATQDHAALEAERQKMSSlvRELQRELEETS----EETGHW-------Q 561
Cdd:pfam07888 233 EALLEElrSLQERLNASERKVEGLGEELSSmaAQRDRTQAELHQARLQA--AQLTLQLADASlalrEGRARWaqeretlQ 310
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568924020 562 SMFQKNKEELRATKQELLQLRMEKEEMEEELGEKMEVLQRDLEQARASTRDT-HQVEELKKELRRTQGELKELQAEQQ 638
Cdd:pfam07888 311 QSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESrRELQELKASLRVAQKEKEQLQAEKQ 388
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
352-663 |
8.72e-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: 39.34 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 352 ELTRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQElLERRKGEVQQSSKELQNMKLLLgqeeglrhgle 431
Cdd:pfam05557 129 STNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKE-LEFEIQSQEQDSEIVKNSKSEL----------- 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 432 AQVKELqlklkhsqspdsgkESLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGAlKEEVASHDQEVEHVRLQY 511
Cdd:pfam05557 197 ARIPEL--------------EKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKY-REEAATLELEKEKLEQEL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 512 Q-------------RDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEETGHWQSMFQKNKEELRATKQEL 578
Cdd:pfam05557 262 QswvklaqdtglnlRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALV 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 579 LQLRMEKEEMEEELGEKMEVLQ---RDLEQARASTRDTHQVEELKKELRRTQGELKEL--QAEQQNQEVTG-RHQNQVLE 652
Cdd:pfam05557 342 RRLQRRVLLLTKERDGYRAILEsydKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMeaQLSVAEEELGGyKQQAQTLE 421
|
330
....*....|.
gi 568924020 653 KQLAALREEAD 663
Cdd:pfam05557 422 RELQALRQQES 432
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
354-556 |
8.80e-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: 39.39 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 354 TRKMEELQKKLDEEVKKRQKLEPSRVGLERQLEEKAEECHRLQEllerRKGEVQQSSK----ELQNMKLLLGQEEGLRHG 429
Cdd:pfam01576 355 TQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ----AKQDSEHKRKklegQLQELQARLSESERQRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 430 LEAQVKELQLKLK---------HSQSPDSGKE--SLLKDLLDTRELLEELLEGKQRVEEQLRLRERELTALKGALKEEVA 498
Cdd:pfam01576 431 LAEKLSKLQSELEsvssllneaEGKNIKLSKDvsSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEE 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568924020 499 SHdQEVEHVRLQYQRDTEQLRRSMQDATQDHAALEAERQKMSSLVRELQRELEETSEE 556
Cdd:pfam01576 511 AK-RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
345-438 |
8.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924020 345 KALAGQAELTRKMEELQKK--LDEEVK-KRQKLEPsrvgLERQLEEKAEECHRLQELLERRKGEVQQSSKEL-QNMKLLL 420
Cdd:PRK12704 52 EAIKKEALLEAKEEIHKLRneFEKELReRRNELQK----LEKRLLQKEENLDRKLELLEKREEELEKKEKELeQKQQELE 127
|
90
....*....|....*...
gi 568924020 421 GQEEGLRHGLEAQVKELQ 438
Cdd:PRK12704 128 KKEEELEELIEEQLQELE 145
|
|
| |
