|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
240-514 |
1.85e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 240 KDGLEKQQSPLDLYNEESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELS 319
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 320 ELKErfQLELSDEHIADLmdntsngegmDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQER 399
Cdd:COG1196 299 RLEQ--DIARLEERRREL----------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 400 AESrrprpvstADTDTRQLQHEILVRNMVLLEVKQYQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELA 479
Cdd:COG1196 367 LLE--------AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270
....*....|....*....|....*....|....*
gi 801375512 480 AAQDEVDAATNNVRKLQRTNEDLVEQLESANVQLE 514
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
289-519 |
3.75e-11 |
|
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: 65.97 E-value: 3.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 289 TVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFQLELSDEHiADLMDNTSNGEGMDRRLTELRTELEKLQVENAAE 368
Cdd:pfam01576 851 ASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLE-EELEEEQSNTELLNDRLRKSTLQVEQLTTELAAE 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 369 WSKRERLETEKNSLERENKLLRLKLYELQERAESRRPRPVSTADTDTR----QLQHEILVRNMVLLEVKQYQASLKQSLA 444
Cdd:pfam01576 930 RSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAqleeQLEQESRERQAANKLVRRTEKKLKEVLL 1009
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 801375512 445 EKTTELSHAmrrsEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESANVQLEHFRNR 519
Cdd:pfam01576 1010 QVEDERRHA----DQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
280-510 |
4.14e-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: 59.30 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 280 REENNSLHRT---VEKLKAEVRQLREQCEELSE--SKAEAMRELSELKERFQLELSDehiadlmdntsngegmdRRLTEL 354
Cdd:TIGR02168 175 KETERKLERTrenLDRLEDILNELERQLKSLERqaEKAERYKELKAELRELELALLV-----------------LRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 355 RTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESrrprpvstADTDTRQLQHEILVRNMVLLEVKQ 434
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE--------LQKELYALANEISRLEQQKQILRE 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 801375512 435 YQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESAN 510
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
255-509 |
4.40e-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: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 255 EESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKErfQLELSDEHI 334
Cdd:COG1196 255 LEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE--ELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 335 ADLMDNTSNGEgmdRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESRRPRpVSTADTD 414
Cdd:COG1196 333 EELEEELEELE---EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 415 TRQLQHEILVRNMVLLEVKQYQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRK 494
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
250
....*....|....*
gi 801375512 495 LQRTNEDLVEQLESA 509
Cdd:COG1196 489 AAARLLLLLEAEADY 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
264-510 |
7.77e-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: 58.53 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 264 ELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFQ-LELSDEHIADLMDNTS 342
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 343 -NGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAesrrprpvstadTDTRQLQHE 421
Cdd:TIGR02168 754 kELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEL------------TLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 422 ILVRNMVLLEVKQYQASLKQSLAEKTTELSHAMrrsEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNED 501
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDI---ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
....*....
gi 801375512 502 LVEQLESAN 510
Cdd:TIGR02168 899 LSEELRELE 907
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
280-508 |
1.28e-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: 57.77 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 280 REENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFQLELSdEHIADLMDNTSNGEGMDRRLTELRTELE 359
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGY-ELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 360 KLQVEnaaewskRERLETEKNSLERENKLLRLKLYELQERaesrrprpvstadtDTRQLQHEILvrnmvllEVKQYQASL 439
Cdd:TIGR02169 255 KLTEE-------ISELEKRLEEIEQLLEELNKKIKDLGEE--------------EQLRVKEKIG-------ELEAEIASL 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 801375512 440 KQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLES 508
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
297-519 |
2.43e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 297 VRQLREQCEELSE--SKAEAMRELSELKERFQLELSDEHIADLmdnTSNGEGMDRRLTELRTELEKLQVENAAEWSKRER 374
Cdd:COG1196 195 LGELERQLEPLERqaEKAERYRELKEELKELEAELLLLKLREL---EAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 375 LETEKNSLERENKLLRLKLYELQERAESRRPRpVSTADTDTRQLQHEILVRNMVLLEVKQYQASLKQSLAEKTTELSHAM 454
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQD-IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 801375512 455 RRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESANVQLEHFRNR 519
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-480 |
3.16e-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: 56.60 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 256 ESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKER-----FQLELS 330
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERlesleRRIAAT 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 331 DEHIADLMDNTsngEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESRRPRpVST 410
Cdd:TIGR02168 837 ERRLEDLEEQI---EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK-RSE 912
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801375512 411 ADTDTRQLQHEILVRNMVLLEVKQYQASLKQSLAEK-TTELSHAMRRSEQYEAEVKRVRARVEELKKELAA 480
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
243-519 |
9.59e-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: 55.06 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 243 LEKQQSPLDLynEESLTQKMSELQIKLEEATKTISVER--EENNSLHRTVEKLKAEVRQLREQCEELSESKAE------A 314
Cdd:TIGR02168 198 LERQLKSLER--QAEKAERYKELKAELRELELALLVLRleELREELEELQEELKEAEEELEELTAELQELEEKleelrlE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 315 MRELSELKERFQLELsDEHIADLMDNTSNGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLY 394
Cdd:TIGR02168 276 VSELEEEIEELQKEL-YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 395 ELQER-AESRRPRPVSTADTDTRQLQHEILVRNMVLLEVKQYQASLKQSLAEKttelshamrRSEQYEAEVKRVRARVEE 473
Cdd:TIGR02168 355 SLEAElEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA---------RLERLEDRRERLQQEIEE 425
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 801375512 474 LKKELAAAqdEVDAATNNVRKLQRTNEDLVEQLESANVQLEHFRNR 519
Cdd:TIGR02168 426 LLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
256-477 |
2.98e-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: 53.52 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 256 ESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFQLELS--DEH 333
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAelEEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 334 IADLMDNTSNGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESRRPRPVSTADT 413
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 801375512 414 DTRQLQHEILVRnmvLLEVKQYQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKE 477
Cdd:TIGR02168 444 ELEEELEELQEE---LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
292-519 |
1.85e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 292 KLKAEVRQLREQCEELSESKAEAMRELSELK-ERFQL--ELSDEH--IADLMDNTSNGEG----MDRRLTELRTELEKLQ 362
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEnRLDELsqELSDASrkIGEIEKEIEQLEQeeekLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 363 VENAAEWSKRERLETEKNSLERENKLLRLKLYELqERAESRRPRPVSTADTDTRQLQHEILVRNMVLLEVKQYQASLKQS 442
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDL-EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 801375512 443 LAEKttELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESANVQLEHFRNR 519
Cdd:TIGR02169 830 YLEK--EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
294-514 |
4.94e-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: 49.28 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 294 KAEVRQLREQCEELSESKAEAMRELSELKERFQlelsdehiadlmDNTSNGEGMDRRLTELRTELEKLQVENAAEWSKRE 373
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELE------------ELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 374 RLETEKNSLERENKLLRLKLYELQERAESRRPRpvstadtdtrqlqheilvrnmvLLEVKQYQASLKQSLAEkttelshA 453
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEE----------------------LAEAEAEIEELEAQIEQ-------L 794
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801375512 454 MRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESANVQLE 514
Cdd:TIGR02168 795 KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
258-493 |
9.81e-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: 48.53 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 258 LTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFQlELSDEhiadL 337
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-ELKEE----L 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 338 MDNTSNGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESRRPRpVSTADTDTRQ 417
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK-INELEEEKED 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 801375512 418 LQheilvrnmvlLEVKQYQASLKQSLAEKTTELSHAMRRSEQYEaevkRVRARVEELKKELAAAQDEVDAATNNVR 493
Cdd:TIGR02169 446 KA----------LEIKKQEWKLEQLAADLSKYEQELYDLKEEYD----RVEKELSKLQRELAEAEAQARASEERVR 507
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
284-508 |
1.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 284 NSLHRTVEKLKAEVRQL---REQCEELSESKAEAmRELSELKERFQLELSDehiadlmdntsngegmdRRLTELRTELEK 360
Cdd:COG4913 238 ERAHEALEDAREQIELLepiRELAERYAAARERL-AELEYLRAALRLWFAQ-----------------RRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 361 LQVEnaaewskRERLETEKNSLERENKLLRLKLYELQERAESRRPRPVSTADTDTRQLQHEILVRNMVLLEVKQYQASLK 440
Cdd:COG4913 300 LRAE-------LARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 801375512 441 QSLAEKttelshamrrSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLES 508
Cdd:COG4913 373 LPLPAS----------AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
255-391 |
2.35e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 255 EESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFQLEL-SDEH 333
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIrKDRE 466
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 801375512 334 IADLmdntsngegmDRRLTELRTELEKLqvenaaewskRERLETEKNSLERENKLLRL 391
Cdd:COG2433 467 ISRL----------DREIERLERELEEE----------RERIEELKRKLERLKELWKL 504
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
278-509 |
4.99e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 278 VEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFqlelsDEHiadlmdntsngEGMDRRLTELRTE 357
Cdd:PRK02224 196 IEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL-----EEH-----------EERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 358 LEKLQvenaaewSKRERLETEKNSLERENKLLRLKLYELQERAESRRPR-PVSTADTDTRQLQHEilvrnmvllEVKQYQ 436
Cdd:PRK02224 260 IEDLR-------ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEaGLDDADAEAVEARRE---------ELEDRD 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 801375512 437 ASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESA 509
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEEL 396
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-403 |
8.10e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 38 RQRELEEARARAAQMEKTMRWWSDCTANWREKWSKVRNERNAARDEAKALRAKLEIAVKDANTFKHESQELELQNEQLKK 117
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 118 EMEKIHMILLKHAGQFdQQIFTILESDPQLRATfgLDEQLEfynnvDASDALGAQRDMLSCKNShEVANVASGGHNILPE 197
Cdd:TIGR02168 755 ELTELEAEIEELEERL-EEAEEELAEAEAEIEE--LEAQIE-----QLKEELKALREALDELRA-ELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 198 RDIEEYVLqGAVPKHAVELYKESPSNSLD-KSITKLVTDSNVKKDGLEKQ-QSPLDLYneESLTQKMSELQIKLEEATKT 275
Cdd:TIGR02168 826 LESLERRI-AATERRLEDLEEQIEELSEDiESLAAEIEELEELIEELESElEALLNER--ASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 276 ISVEREENNSLHRTVEKLKAEVRQLREQCEELsesKAEAMRELSELKERFQLELsDEHIADLMDNTSNGEGMDRRLTELR 355
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLELRLEGL---EVRIDNLQERLSEEYSLTL-EEAEALENKIEDDEEEARRRLKRLE 978
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 801375512 356 TELEKLQVEN-------AAEWSKRERLETEKNSLERENKLLRLKLYELQERAESR 403
Cdd:TIGR02168 979 NKIKELGPVNlaaieeyEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
291-514 |
8.92e-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: 44.75 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 291 EKLKAEVRQLREQCEELSESKAEAMRELSELKErfQLELSDEHIADLmdntsngegmDRRLTELRTELEKLQVENAAews 370
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLK--QLAALERRIAAL----------ARRIRALEQELAALEAELAE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 371 KRERLETEKNSLERENKLLRLKLYELQERAESRRPRPVSTADTdtrqlQHEILVRNMVLLEVKQYQASLKQSLAEKTTEL 450
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 801375512 451 SHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESANVQLE 514
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
349-494 |
1.46e-04 |
|
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: 43.37 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 349 RRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESRRPRPVSTADT-DTRQLQHEIlvrnm 427
Cdd:COG1579 24 HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkEYEALQKEI----- 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 801375512 428 vllevkqyqASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRK 494
Cdd:COG1579 99 ---------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
241-511 |
2.38e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 241 DGLEKQQSPLDLYNEESLTQKMSELQIKLEEATKTISVEREENNSLHRtVEKLKAEVRQLREQCEELSESKAEAMRELSE 320
Cdd:PRK04863 875 SALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQ-LEPIVSVLQSDPEQFEQLKQDYQQAQQTQRD 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 321 LKERFqlelsdehiadlmdntsngegmdRRLTELRteleklQVENAAEWSKRERLETEKNSLereNKLLRLKLyelqERA 400
Cdd:PRK04863 954 AKQQA-----------------------FALTEVV------QRRAHFSYEDAAEMLAKNSDL---NEKLRQRL----EQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 401 ESRRprpvSTADTDTRQLQHEILVRNMVLLEVKQYQASLKQSLAEKTTELS------------HAMRRSEQYEAEVKRVR 468
Cdd:PRK04863 998 EQER----TRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpadsgaeeRARARRDELHARLSANR 1073
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 801375512 469 ARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESANV 511
Cdd:PRK04863 1074 SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKA 1116
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
223-514 |
5.43e-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: 42.70 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 223 NSLDKSITKLVTDSNVKKDGLEKQQSPLDLYNE--ESLTQKMSELQIKLEEATKtiSVEREENNSLHRTVEKLKAEVRQL 300
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkiKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 301 REQCEELSESKAEAMRELSELKErfqlelsdehiaDLMDNTSNGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKN 380
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQISQLKK------------ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIN 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 381 SLERE-------NKLLRLKLYELQERAEsrrprpvsTADTDTRQLQHEILVRNMVLLEVKQYQASLKQSLAEKTTELSHA 453
Cdd:TIGR04523 395 DLESKiqnqeklNQQKDEQIKKLQQEKE--------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801375512 454 MRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESANVQLE 514
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
283-519 |
6.38e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 283 NNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERfqlelsdehiADLMDNTSNGEGMDRRLTELRTELEKLQ 362
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK----------NGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 363 VENAAEWSKRERLETEKNS----------------LERENKLLRLKLYELQERAESRRPrpvstadtDTRQLQHEIlvrn 426
Cdd:COG3206 233 AELAEAEARLAALRAQLGSgpdalpellqspviqqLRAQLAELEAELAELSARYTPNHP--------DVIALRAQI---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 427 mvllevkqyqASLKQSLAEKTTelshamRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRtnedLVEQL 506
Cdd:COG3206 301 ----------AALRAQLQQEAQ------RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREV 360
|
250
....*....|...
gi 801375512 507 ESANVQLEHFRNR 519
Cdd:COG3206 361 EVARELYESLLQR 373
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-479 |
9.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 260 QKMSELQIKLEEATKTIS---VEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERF-QLELSDEHIA 335
Cdd:COG4913 654 AEYSWDEIDVASAEREIAeleAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELeQAEEELDELQ 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 336 DLMDNTSNGEGMDRRLtELRTELEKLQVENAAEwSKRERLETEKNSLERENKLLRLKLYELQERAESRRPRPVSTADTDT 415
Cdd:COG4913 734 DRLEAAEDLARLELRA-LLEERFAAALGDAVER-ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADL 811
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 801375512 416 ----------RQLQHEILVRnmvllevkqYQASLKQSLAEKTTE----LSHAMRRseqyeaEVKRVRARVEELKKELA 479
Cdd:COG4913 812 eslpeylallDRLEEDGLPE---------YEERFKELLNENSIEfvadLLSKLRR------AIREIKERIDPLNDSLK 874
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
254-519 |
1.00e-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: 42.03 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 254 NEESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLRE----QCEELSESKAEAMRELSELKERFQLEL 329
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSmymrQLSDLESTVSQLRSELREAKRMYEDKI 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 330 SDEHIADLMDNTsngegmdrRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLlrlklyelqERAESRRPRPVS 409
Cdd:pfam15921 345 EELEKQLVLANS--------ELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSL---------EKEQNKRLWDRD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 410 TADTDT-RQLQHEILVRNMvllEVKQYQASLKQSLAEKTTELSHAMR----RSEQYEaEVKRVRARVEELKKELAAAQDE 484
Cdd:pfam15921 408 TGNSITiDHLRRELDDRNM---EVQRLEALLKAMKSECQGQMERQMAaiqgKNESLE-KVSSLTAQLESTKEMLRKVVEE 483
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 801375512 485 VDAATNNVRKLQRTNEDLVEQL-------ESANVQLEHFRNR 519
Cdd:pfam15921 484 LTAKKMTLESSERTVSDLTASLqekeraiEATNAEITKLRSR 525
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
255-490 |
1.02e-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: 41.29 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 255 EESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFQLELsdehi 334
Cdd:COG4942 50 EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 335 adlMDNTSNGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERaesrrprpvstadtd 414
Cdd:COG4942 125 ---LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE--------------- 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 801375512 415 trqlqheilvrnmvllevkqyQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATN 490
Cdd:COG4942 187 ---------------------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
243-513 |
1.15e-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: 41.63 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 243 LEKQQSPLDLYNEEsLTQKMSELQiKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKaeamRELSELK 322
Cdd:pfam05483 372 LEKNEDQLKIITME-LQKKSSELE-EMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKE----QELIFLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 323 ERFQLELSDEHIaDLMDNTSNGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAES 402
Cdd:pfam05483 446 QAREKEIHDLEI-QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 403 RRPRPVSTADTDTRQLQHEILVRNmvllEVKQYQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQ 482
Cdd:pfam05483 525 CKKQEERMLKQIENLEEKEMNLRD----ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK 600
|
250 260 270
....*....|....*....|....*....|.
gi 801375512 483 DEVDAATNNVRKLQRTNEDLVEQLESANVQL 513
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENKQL 631
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
369-519 |
1.74e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 369 WSKRERLETeknsLERENKLLRLKLYELQERAEsrrprpvstadtDTRQLQHEILVRNMVLLEVKQYQASLK--QSLAEK 446
Cdd:COG4913 606 FDNRAKLAA----LEAELAELEEELAEAEERLE------------ALEAELDALQERREALQRLAEYSWDEIdvASAERE 669
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 801375512 447 TTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLVEQLESANVQLEHFRNR 519
Cdd:COG4913 670 IAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
243-518 |
1.83e-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: 41.26 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 243 LEKQQSPLDLYNEEslTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELK 322
Cdd:pfam15921 446 MERQMAAIQGKNES--LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 323 ERFQLELSD-EHIADLMDNTSNGE-----------GMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLR 390
Cdd:pfam15921 524 SRVDLKLQElQHLKNEGDHLRNVQtecealklqmaEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 391 LKLYELQERAESRrprpvstaDTDTRQLqhEILVRNMVLLEVKQYQASlkqslAEKTTELSHAMRRSEQYEAEVKRVRAR 470
Cdd:pfam15921 604 LELQEFKILKDKK--------DAKIREL--EARVSDLELEKVKLVNAG-----SERLRAVKDIKQERDQLLNEVKTSRNE 668
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 801375512 471 VEELKKELAAAQDEVdaaTNNVRKLQRTNEDLVEQLESANVQLEHFRN 518
Cdd:pfam15921 669 LNSLSEDYEVLKRNF---RNKSEEMETTTNKLKMQLKSAQSELEQTRN 713
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
227-334 |
1.95e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.10 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 227 KSITKLVTDSNVKKDGLEKQQSPLDLYNE-ESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCE 305
Cdd:COG4026 122 KSLQNIPEYNELREELLELKEKIDEIAKEkEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFE 201
|
90 100 110
....*....|....*....|....*....|
gi 801375512 306 ELSESKAEAMRELSEL-KERFQLELSDEHI 334
Cdd:COG4026 202 ELLKKRLLEVFSLEELwKELFPEELPEEDF 231
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
263-506 |
2.38e-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: 40.82 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 263 SELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFQLELSdehiADLMDNTS 342
Cdd:TIGR02169 226 YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVK----EKIGELEA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 343 NGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESRrprpvstadtdtrqlqhei 422
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL------------------- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 423 lvrnmvllevKQYQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDAATNNVRKLQRTNEDL 502
Cdd:TIGR02169 363 ----------KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
....
gi 801375512 503 VEQL 506
Cdd:TIGR02169 433 EAKI 436
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
268-509 |
2.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 268 KLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERfqlelsdehIADLMDNTSNGEGM 347
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE---------LPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 348 DRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERA-ESRRPRPVSTADTDTRQLQHEILVRN 426
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVkELKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 427 MVLLEVKQYQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKElAAAQDEVDAATNNVRKLQ-----RTNED 501
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKkrltgLTPEK 388
|
....*...
gi 801375512 502 LVEQLESA 509
Cdd:PRK03918 389 LEKELEEL 396
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
268-474 |
2.74e-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: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 268 KLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESK---------AEAMRELSELKERfqlelsdehIADLM 338
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvASAEREIAELEAE---------LERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 339 DNTSNGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLEREnkllrlkLYELQERAESRRPRPVSTADTDTRQL 418
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE-------LDELQDRLEAAEDLARLELRALLEER 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 419 QHEILVRNMVLLEVKQYQASLKQS---LAEKTTELSHAMRR-SEQYEAEVKRVRARVEEL 474
Cdd:COG4913 755 FAAALGDAVERELRENLEERIDALrarLNRAEEELERAMRAfNREWPAETADLDADLESL 814
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
223-518 |
3.48e-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: 40.00 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 223 NSLDKSITKLVTDSNVKKDGLEKQQSPLDLYNEE---------SLTQKMSELQIKLEEATKT-------ISVEREENNSL 286
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELEEKQNEIEKLKKEnqsykqeikNLESQINDLESKIQNQEKLnqqkdeqIKKLQQEKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 287 HRTVEKLKAEVRQLREQCEELSESKAE---AMRELSELKERFQLELS-------------DEHIADLMDNTSNGEGMDRR 350
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVkelIIKNLDNTRESLETQLKvlsrsinkikqnlEQKQKELKSKEKELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 351 LTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQEraesrrprpvstaDTDTRQLQHEILVRNMVLL 430
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF-------------ELKKENLEKEIDEKNKEIE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 431 EVKQYQASLKQSLAEKTTELshamrrsEQYEAEVKRVR-------ARVEELKKELAAAQDEVDAATNNVRKLQRTNEDLV 503
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELI-------DQKEKEKKDLIkeieekeKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
330
....*....|....*
gi 801375512 504 EQLESANVQLEHFRN 518
Cdd:TIGR04523 645 QEVKQIKETIKEIRN 659
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
256-474 |
3.69e-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: 40.05 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 256 ESLTQKMSELQIKLEEATKTISVEREENNSL-----HRTVEKLKAEVRQLREQCEELSESKAEAMRELSELK-ERFQLEL 329
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTlEKEYLEK 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 330 SDEHIADLMDNTSNGEGMDR-RLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESrrprpV 408
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEkEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-----L 908
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 801375512 409 STADTDTRQLQHEILVRNMVLL-EVKQYQASLKQSLAEKTTELShamrrSEQYEAEVKRVRARVEEL 474
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEeELSEIEDPKGEDEEIPEEELS-----LEDVQAELQRVEEEIRAL 970
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
269-507 |
4.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 269 LEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEElsESKAEAMRELSELKERFQLELSDEHIADLMDNTSNGEGMD 348
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK--ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 349 RRLTELRTELEKLqvenAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESRRPRPVSTADTDTRQLQhEILVRNMV 428
Cdd:PRK03918 532 EKLIKLKGEIKSL----KKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLE 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 429 LLEVKQYQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKK-------------------ELAAAQDEVDAAT 489
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseeeyeelreeylelsrELAGLRAELEELE 686
|
250
....*....|....*...
gi 801375512 490 NNVRKLQRTNEDLVEQLE 507
Cdd:PRK03918 687 KRREEIKKTLEKLKEELE 704
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
256-406 |
5.76e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.67 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 256 ESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKErfQLELSDEHIA 335
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA--AIAGIEAKIN 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 801375512 336 DLMDNTsngEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESRRPR 406
Cdd:TIGR02169 438 ELEEEK---EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
231-519 |
5.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 231 KLVTDSNVKKDGLEKQQSPLDLYNEESLTQKMSELQIKLEEATKTISVEREENNSLhrtveklKAEVRQLREQCEELSES 310
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL-------KKEIKELKKAIEELKKA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 311 KAEAMRELSELKERFQLELSDEHIADLMDNTSNGEGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNSLERENKLLR 390
Cdd:PRK03918 435 KGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKK 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 391 LKLYELQERAESRRprpvsTADTDTRQLQHEILVRNMVLLEVKQYQ---ASLKQSLAEKTTELSHAMRRSEQYEAE-VKR 466
Cdd:PRK03918 515 YNLEELEKKAEEYE-----KLKEKLIKLKGEIKSLKKELEKLEELKkklAELEKKLDELEEELAELLKELEELGFEsVEE 589
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 801375512 467 VRARVEELKK------ELAAAQDEVDAATNNVRKLQRTNEDLVEQLESANVQLEHFRNR 519
Cdd:PRK03918 590 LEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
280-485 |
5.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 280 REENNSLHRTVEKLKAEVRQLREQCEELSESKAEAMRELSELKERFQlelsdehiadlmdntSNGegmDRRLTELRTELE 359
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIR---------------GNG---GDRLEQLEREIE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 360 KLQVENAAEWSKRERLETEKNSLERENKLLRLKLYELQERAESRRPRpVSTADTDTRQLQHEILVRnmvllevkqyQASL 439
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA-LEEELEALEEALAEAEAA----------LRDL 417
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 801375512 440 KQSLAEKTTELSHAMRRSEQYEAEVKRVRarvEELKKELAAAQDEV 485
Cdd:COG4913 418 RRELRELEAEIASLERRKSNIPARLLALR---DALAEALGLDEAEL 460
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
265-513 |
6.03e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 265 LQIKLEEATKTIsvereennslhrtveklkaevRQLREQCEELSESKAEAMRELSELKERfqlelsdehiADLMDNTSNG 344
Cdd:COG3206 166 LELRREEARKAL---------------------EFLEEQLPELRKELEEAEAALEEFRQK----------NGLVDLSEEA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 345 EGMDRRLTELRTELEKLQVENAAEWSKRERLETEKNS----------------LERENKLLRLKLYELQERAESRRPrpv 408
Cdd:COG3206 215 KLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellqspviqqLRAQLAELEAELAELSARYTPNHP--- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 409 stadtDTRQLQHEILVRNmvllevKQYQASLKQSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKK---ELAAAQDEV 485
Cdd:COG3206 292 -----DVIALRAQIAALR------AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEleaELRRLEREV 360
|
250 260 270
....*....|....*....|....*....|
gi 801375512 486 DAATNNVRK-LQRTNE-DLVEQLESANVQL 513
Cdd:COG3206 361 EVARELYESlLQRLEEaRLAEALTVGNVRV 390
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
256-516 |
7.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 256 ESLTQKMSELQIKLEEATKTISVEREENNSLHRTVEKLKAEVRQLREQCEELsESKAEAMR---------------ELSE 320
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL-ESELEEAReavedrreeieeleeEIEE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 321 LKERF-----QLELSDEHIADLMDNTSNGEGmdrRLTELRTELEKLQ---------------------------VENAAE 368
Cdd:PRK02224 396 LRERFgdapvDLGNAEDFLEELREERDELRE---REAELEATLRTARerveeaealleagkcpecgqpvegsphVETIEE 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 801375512 369 W-SKRERLETEKNSLE-----RENKLLRLK-LYELQERAESRRprpvstadtDTRQLQHEILVRNMVLLEVKQYQA-SLK 440
Cdd:PRK02224 473 DrERVEELEAELEDLEeeveeVEERLERAEdLVEAEDRIERLE---------ERREDLEELIAERRETIEEKRERAeELR 543
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 801375512 441 QSLAEKTTELSHAMRRSEQYEAEVKRVRARVEELKKELAAAQDEVDaATNNVRKLQRTNEDLVEQLESANVQLEHF 516
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTLLAAIADAEDEIERLREKREAL 618
|
|
| |
