|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
286-614 |
5.76e-28 |
|
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: 120.28 E-value: 5.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 286 QLNARVIEAETRLKTEVTR------IKKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQATL 359
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQraqavaAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIL 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 360 DQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQELSVVASDYEEVSKEL 439
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNT 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 440 RISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGSKRIISKLEARIRDLELELEE 519
Cdd:pfam01576 906 ELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQ 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 520 EKRRHAETIKILRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQEGVSQQTTTRVRRFQRELEAAED 599
Cdd:pfam01576 986 ESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATE 1065
|
330
....*....|....*
gi 24661120 600 RADTAESSLNIIRAK 614
Cdd:pfam01576 1066 SNESMNREVSTLKSK 1080
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
335-617 |
2.51e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.80 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 335 KKQSLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTAnvsl 414
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 415 vsiKSKLEQELSVVASDYEEVSKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELN 494
Cdd:COG1196 297 ---LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 495 AVAGSKRIISKLEARIRDLELELEEEKRRhAETIKILRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLS 574
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24661120 575 EQEGVSQQTTTRVRRFQRELEAAEDRADTAESSLNIIRAKHRT 617
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
310-614 |
5.46e-09 |
|
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: 59.69 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 310 QIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRA 389
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 390 KRTVELQYEEAASRINELTTANVSLVSIKSKLEQ-------ELSVVASDYEEVSKELRISDERYQKVQVELKHVVEQVHE 462
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAqieqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 463 EQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGSKRIISKLEARiRDLELELEEEKRRHAETIKILRKKERTVKEvl 542
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER-ASLEEALALLRSELEELSEELRELESKRSE-- 912
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24661120 543 vqceedqknlilLQDALDKSTAKINIYRRQLSEQEGVSQQTTTRVR-RFQRELEAAEDRADTAESSLNIIRAK 614
Cdd:TIGR02168 913 ------------LRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
289-581 |
6.53e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 289 ARVIEAETRLKT--EVTRIKKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQATLDQYAVAQ 366
Cdd:COG1196 222 LKELEAELLLLKlrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 367 RRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQELSVVASDYEEVSKELRISDERY 446
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 447 QKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAgskriiskLEARIRDLELELEEEKRRHAE 526
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE--------LEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 24661120 527 TIKILRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQEGVSQ 581
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
343-617 |
7.81e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 7.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 343 ELQAHYEdvQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTAnvslvsikskle 422
Cdd:COG1196 217 ELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE------------ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 423 qelsvvasdYEEVSKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGSKRI 502
Cdd:COG1196 283 ---------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 503 ISKLEARIRDLELELEEEKRRHA--ETIKILRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQEGVS 580
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEaeEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270
....*....|....*....|....*....|....*..
gi 24661120 581 QQTTTRVRRFQRELEAAEDRADTAESSLNIIRAKHRT 617
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
283-581 |
5.88e-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: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 283 EIEQLNARVIEAETRLKTEVTRIKKkLQIQITELEMSLDVANKTNIDLQKVikkqslqLTELQAHYEDVQRQLQATLDQY 362
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEELQKE-------LYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 363 AVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINElttanvslvsikskLEQELSVVASDYEEVSKELRIS 442
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES--------------LEAELEELEAELEELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 443 DERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGSKRIISKLEARIRDLELELEEEKR 522
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 24661120 523 RHAETIKILRKKERTVKEVLVQCEEDQKNLILLQDALDkstakiNIYRRQLSEQEGVSQ 581
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLE------RLQENLEGFSEGVKA 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
335-616 |
1.07e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 335 KKQSLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAAS-RINELTTANVS 413
Cdd:TIGR02169 219 EKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 414 LVSIKSKLEQELSVVASDYEEVSKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVEl 493
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 494 navagskriisklearirdleleleeekRRHAETIKILRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQL 573
Cdd:TIGR02169 378 ----------------------------KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 24661120 574 SEQEGVSQQTTTRVRRFQRELEAAEDRADTAESSLNIIRAKHR 616
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-494 |
3.09e-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: 50.44 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 258 VKRQLSTLNQRTVEFYADSsKQTSIEIEQLNARVIEAETRLKTEVTRIKKkLQIQITELEMSLDVANKTNIDLQKVIKKQ 337
Cdd:TIGR02168 703 LRKELEELEEELEQLRKEL-EELSRQISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAEIEELEERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 338 SLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSI 417
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24661120 418 KSKLEQELSVVASDYEEVSKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELN 494
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
292-490 |
3.91e-06 |
|
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: 50.17 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 292 IEAETRLKTEVTRIKKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAG 371
Cdd:pfam01576 365 LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELES 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 372 LNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQELSVVASDYEEVSKELRISDERYQKVQV 451
Cdd:pfam01576 445 VSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA 524
|
170 180 190
....*....|....*....|....*....|....*....
gi 24661120 452 ELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEE 490
Cdd:pfam01576 525 QLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEE 563
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
254-504 |
9.61e-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: 48.91 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 254 SLHNVKRQLSTLNQrtvefyadSSKQTSIEIEQLNARVIEAETRLKTEVTRIKKK--------------LQIQITELEMS 319
Cdd:TIGR02169 238 QKEAIERQLASLEE--------ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkekigeLEAEIASLERS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 320 LDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQ-------ATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRT 392
Cdd:TIGR02169 310 IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 393 VELQYEEAASRINELTTANVSLVSIKSKLEQELS-------VVASDYEEVSKELRISDERYQKVQVELKHVVEQVHEEQE 465
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELAdlnaaiaGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
250 260 270
....*....|....*....|....*....|....*....
gi 24661120 466 RIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGSKRIIS 504
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
306-511 |
5.76e-05 |
|
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: 45.91 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 306 KKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDS 385
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 386 --ANRAKRTVELQYEEAASRINELTTANVSLVSIKS-----KLEQELSVVASDYEEVSKELRISDERYQKVQVELKHVVE 458
Cdd:COG4942 102 qkEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 24661120 459 QVHEEQERIVKLETIKKSLEVEVKNlSIRLEEVELNAVAGSKRIISKLEARIR 511
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEK-ELAELAAELAELQQEAEELEALIARLE 233
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
301-599 |
6.12e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.21 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 301 EVTRIKKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVR 380
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 381 SHLDSANRAKRTVELQYEEAASRINELTTAnvSLVSIKSKLEQELSVVASDYEEVSKELRISDERYQKVQVELKHVVEQV 460
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEAR--LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 461 HEEQERIVKLETIKKSLEVEVKNLSIRLEEVElnavagskRIISKLEARIRDLELELEEEKRRHAETIKILRKKERTVKE 540
Cdd:TIGR02169 836 QELQEQRIDLKEQIKSIEKEIENLNGKKEELE--------EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24661120 541 VLVQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQEGVSQQTTT------RVRRFQRELEAAED 599
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSledvqaELQRVEEEIRALEP 972
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
337-550 |
1.64e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 337 QSLQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVS 416
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 417 IKSKLEQELSVV--------ASDYEEV---SKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLS 485
Cdd:COG4942 98 ELEAQKEELAELlralyrlgRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24661120 486 IRLEEVElnavaGSKRIISKLEARIRDLELELEEEKRRHAETIKILRKKERTVKEVLVQCEEDQK 550
Cdd:COG4942 178 ALLAELE-----EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-466 |
2.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 283 EIEQLNARVIEAETRLKtEVTRIKKKLQIQITELEMSLDVANkTNIDLQKVIKkqslQLTELQAHYEdvqrQLQATLDQY 362
Cdd:COG4913 618 ELAELEEELAEAEERLE-ALEAELDALQERREALQRLAEYSW-DEIDVASAER----EIAELEAELE----RLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 363 AVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQElsvvasDYEEVSKELRIs 442
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA------LLEERFAAALG- 760
|
170 180
....*....|....*....|....
gi 24661120 443 DERYQKVQVELKHVVEQVHEEQER 466
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNR 784
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
273-541 |
5.52e-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: 43.09 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 273 YADSSKQTSIEIEQLNARVIEAETRLKTEVTRIKKK------LQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQA 346
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLqqekelLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 347 HYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQELS 426
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 427 vvasdyeEVSKELRISDERYQKVQVElkhvvEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGSKRI---I 503
Cdd:TIGR04523 542 -------DLEDELNKDDFELKKENLE-----KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIeekE 609
|
250 260 270
....*....|....*....|....*....|....*...
gi 24661120 504 SKLEARIRDLELELEEEKRRHAETIKILRKKERTVKEV 541
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
274-607 |
6.01e-04 |
|
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: 43.24 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 274 ADSSKQTSIEIEQLNARVIEAETRLKTE------VTRIKKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAH 347
Cdd:pfam01576 144 EDQNSKLSKERKLLEERISEFTSNLAEEeekaksLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 348 YEDVQRQ--------------LQATLD-------QYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINE 406
Cdd:pfam01576 224 IAELQAQiaelraqlakkeeeLQAALArleeetaQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 407 LTT-------ANVSLVSIKSKLEQELSVVASDYEEVSK--ELRISDERyQKVQVELKHVVEQVHEEQERIVKLETIKKSL 477
Cdd:pfam01576 304 LKTeledtldTTAAQQELRSKREQEVTELKKALEEETRshEAQLQEMR-QKHTQALEELTEQLEQAKRNKANLEKAKQAL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 478 EVEVKNLSIRLEEVElNAVAGSKRIISKLEARIRDLELELEEEKRRHAETIKILRKKERTVKEVLVQCEEDQKNLILLQD 557
Cdd:pfam01576 383 ESENAELQAELRTLQ-QAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSK 461
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 24661120 558 ALDKSTAKINIYRRQLSEQEGVSQQTTTRVRRFQRELEAAEDRADTAESS 607
Cdd:pfam01576 462 DVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEA 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
340-512 |
7.08e-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: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 340 QLTELQAHYE---------DVQRQLQATLDQYAvAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTA 410
Cdd:COG4913 253 LLEPIRELAEryaaarerlAELEYLRAALRLWF-AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 411 --NVSLVSIKSkLEQELSVVASDYEEVSKELRI--------------SDERYQKVQVELKHVVEQVHEEQERIVKLETik 474
Cdd:COG4913 332 irGNGGDRLEQ-LEREIERLERELEERERRRARleallaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALA-- 408
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 24661120 475 kSLEVEVKNLSIRLEEV--ELNAVAGSKRIISKLEARIRD 512
Cdd:COG4913 409 -EAEAALRDLRRELRELeaEIASLERRKSNIPARLLALRD 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
181-477 |
8.92e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 181 AQALLSESEKNIKTAKKEEEDYIAQTLVrssravsrarsrssspLDGQYRAHALHIELMDDRLVDKLD--HRVSSSLHNV 258
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAE----------------LEAELEELRLELEELELELEEAQAeeYELLAELARL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 259 KRQLSTLNQRTvEFYADSSKQTSIEIEQLNARVIEAETRLKTEVTRIKKkLQIQITELEMSLDVANKTNIDLQKVIKKQS 338
Cdd:COG1196 301 EQDIARLEERR-RELEERLEELEEELAELEEELEELEEELEELEEELEE-AEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 339 LQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIK 418
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24661120 419 SKLEQELSVVASDYEEVSKELRISDERYQ--KVQVELKHVVEQVHEEQERIVKLETIKKSL 477
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAeaAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
276-608 |
1.27e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 276 SSKQTSIEIEQLNARVIEAETRlKTEVTRIKKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEdvqrql 355
Cdd:PRK03918 378 KKRLTGLTPEKLEKELEELEKA-KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR------ 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 356 QATLDQYavaQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANvSLVSIKSKLEqelSVVASDYEEV 435
Cdd:PRK03918 451 KELLEEY---TAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKLK---KYNLEELEKK 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 436 SKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETI---KKSLEVEVKNLSIRLEEVELNAVAGSKRIISKLEARIRD 512
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELekkLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 513 LELELEEEKRrhaetikiLRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQE--GVSQQTTTRVRRF 590
Cdd:PRK03918 604 YLELKDAEKE--------LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeELREEYLELSREL 675
|
330 340
....*....|....*....|.
gi 24661120 591 QR---ELEAAEDRADTAESSL 608
Cdd:PRK03918 676 AGlraELEELEKRREEIKKTL 696
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
339-510 |
1.49e-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: 40.68 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 339 LQLTELQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVRSHLDSANRAKRTVELQYEEAASRINelttanvslvsik 418
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 419 sKLEQELSVVAS--DYEEVSKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEvelnAV 496
Cdd:COG1579 77 -KYEEQLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE----EL 151
|
170
....*....|....
gi 24661120 497 AGSKRIISKLEARI 510
Cdd:COG1579 152 AELEAELEELEAER 165
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
182-607 |
1.90e-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: 41.64 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 182 QALLSESEKNIKTAKKEEEDYIAQtLVRSSRAVSRARSRSSSPLDGQYRAHALHIELMDD--RLVDKLDHRVSSSLHNVK 259
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQDRIEQ-LISEHEVEITGLTEKASSARSQANSIQSQLEIIQEqaRNQNSMYMRQLSDLESTV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 260 RQLSTLNQRTVEFYADSSKQTSIEIEQLNARVIEAET---RLKTEVTRIKKKLQIQITEL-----EMSL----------- 320
Cdd:pfam15921 327 SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTerdQFSQESGNLDDQLQKLLADLhkrekELSLekeqnkrlwdr 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 321 DVANKTNID-LQKVIKKQSLQLTELQAHYEDVQRQLQATLDQYAVAqrrLAGLNGELEEVRSHLDSANRAKRTVELQYEE 399
Cdd:pfam15921 407 DTGNSITIDhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAA---IQGKNESLEKVSSLTAQLESTKEMLRKVVEE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 400 AASRINELTTANVSLVSIKSKLEQELSVVASDYEEVSK-------------ELRISDERYQKVQVELK----------HV 456
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlklqelqHLKNEGDHLRNVQTECEalklqmaekdKV 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 457 VEQVHEEQERIVKL-----------ETIKKSLEVEVKNLSIRLEEVELNAVAGSKRIiSKLEARIRDLELELEEEKRRHA 525
Cdd:pfam15921 564 IEILRQQIENMTQLvgqhgrtagamQVEKAQLEKEINDRRLELQEFKILKDKKDAKI-RELEARVSDLELEKVKLVNAGS 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 526 ETIKILRKKERTVKEVLVQCEEDQKNLILLQDalDKSTAKINiYRRQLSEQEGVSQQTTTRVRRFQRELEAAEDRADTAE 605
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELNSLSE--DYEVLKRN-FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
..
gi 24661120 606 SS 607
Cdd:pfam15921 720 GS 721
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-614 |
2.99e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 365 AQRRLAGLNGELEEVRSHLDSANRAKRTVELQyEEAASRINELttanvslvsiKSKLEQ-ELSVVASDYEEVSKELRisd 443
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQ-AEKAERYKEL----------KAELRElELALLVLRLEELREELE--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 444 eryqKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEV--ELNAVAGskrIISKLEARIRDLELELEEEK 521
Cdd:TIGR02168 243 ----ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELqkELYALAN---EISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 522 RRHAETIKILRKKERtvkevlvQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQEGVSQQTTTRVRRFQRELEAAEDRA 601
Cdd:TIGR02168 316 RQLEELEAQLEELES-------KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
250
....*....|...
gi 24661120 602 DTAESSLNIIRAK 614
Cdd:TIGR02168 389 AQLELQIASLNNE 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
344-608 |
4.70e-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: 39.88 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 344 LQAHYEDVQRQLQATLDQYAVAQRRLAGLNGELEevrshldsanRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQ 423
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYK----------RDREQWERQRRELESRVAELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 424 ELSVVASDYEEVSKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVE---------LN 494
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEaerkqlqakLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 495 AVAGSKRIISKLEARIRDLELELEEEKRRHAETIKILRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLS 574
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELS 261
|
250 260 270
....*....|....*....|....*....|....
gi 24661120 575 EQegVSQQTTTRVRRFQRELEAAEDRADTAESSL 608
Cdd:pfam07888 262 SM--AAQRDRTQAELHQARLQAAQLTLQLADASL 293
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
374-612 |
6.21e-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: 39.67 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 374 GELEEVRSHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQELSVVASDYEEVSKELRISDERYQKVQVEL 453
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 454 KHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGSKR----IISKLEARIRDLELELEEEKRRHAETIK 529
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSkleeEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 530 ILRKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQEGVSQQTTTRVRRFQRELEAAEDRADTAESSLN 609
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
...
gi 24661120 610 IIR 612
Cdd:TIGR02169 914 KKR 916
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
304-600 |
8.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 304 RIKKKLQIQITELEMSLdvanKTNIDLQKVIKKQSLQLTELQ---AHYEDVQRQLQATLDQYAVAQRRLAGLNGELEEVR 380
Cdd:PRK03918 169 EVIKEIKRRIERLEKFI----KRTENIEELIKEKEKELEEVLreiNEISSELPELREELEKLEKEVKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 381 SHLDSANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEqELSVVASDYEEVSKELRISDERYQKVQVELKHVVEQV 460
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 461 HEEQERIVKLETIK---KSLEVEVKNLSIRLEEVE-----LNAVAGSKRIISKLEARIRDLELELEEEKRRHAETIKI-L 531
Cdd:PRK03918 324 NGIEERIKELEEKEerlEELKKKLKELEKRLEELEerhelYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEeI 403
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24661120 532 RKKERTVKEVLVQCEEDQKNLILLQDALDKSTAKINIYRRQLSEQE--GVSQQTTTRVRRFQRELEAAEDR 600
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHrkELLEEYTAELKRIEKELKEIEEK 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
358-602 |
8.75e-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: 39.27 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 358 TLDQYAVAQRRLAGLNGELEEVRSHLDS----ANRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQELSVVASDYE 433
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSlerqAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 434 EVSKELRISDERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNavagskriISKLEARIRDL 513
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ--------LEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 514 ELELEEEKRRHAEtikiLRKKERTVKEVLVQCEEDQKNLILLQ----DALDKSTAKINIYRRQLSEQEGVSQQTTTRVRR 589
Cdd:TIGR02168 329 ESKLDELAEELAE----LEEKLEELKEELESLEAELEELEAELeeleSRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250
....*....|...
gi 24661120 590 FQRELEAAEDRAD 602
Cdd:TIGR02168 405 LEARLERLEDRRE 417
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
284-595 |
9.14e-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: 39.23 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 284 IEQLNARVIEAETRLKTEvTRIKKKLQIQITELEMSLDVANKTNIDLQKVIKKQSLQLTELQAHYEDVQRQLQATLDQYA 363
Cdd:TIGR04523 98 INKLNSDLSKINSEIKND-KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 364 VAQRRLAGLNGELEEVRSHLdsanRAKRTVELQYEEAASRINELTTANVSLVSIKSKLEQELSVVASDYEEVSKELRISD 443
Cdd:TIGR04523 177 LLEKEKLNIQKNIDKIKNKL----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 444 ERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVELNAVAGS----KRIISKLEARIRDLELELEE 519
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWnkelKSELKNQEKKLEEIQNQISQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 520 EKRRHAE---TIKILRK----KERTVKEVLVQCEEDQKNLILLQ-------DALDKSTAKINIYRRQLSEQEGVSQQTTT 585
Cdd:TIGR04523 333 NNKIISQlneQISQLKKeltnSESENSEKQRELEEKQNEIEKLKkenqsykQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
330
....*....|
gi 24661120 586 RVRRFQRELE 595
Cdd:TIGR04523 413 QIKKLQQEKE 422
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
443-561 |
9.36e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.07 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24661120 443 DERYQKVQVELKHVVEQVHEEQERIVKLETIKKSLEVEVKNLSIRLEEVElnavagskRIISKLEARIRDLELELEEEKR 522
Cdd:COG2433 391 PEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKD--------ERIERLERELSEARSEERREIR 462
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 24661120 523 RHAE------TIKILRKKERTVKEVLvqcEEDQKNLILLQDALDK 561
Cdd:COG2433 463 KDREisrldrEIERLERELEEERERI---EELKRKLERLKELWKL 504
|
|
| |
