|
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 ... |
2-511 |
7.60e-58 |
|
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: 207.72 E-value: 7.60e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLD 81
Cdd:pfam01576 571 LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALE 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 82 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID 161
Cdd:pfam01576 651 AKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFE 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 162 RKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDT 241
Cdd:pfam01576 731 RDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 242 QLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETD 321
Cdd:pfam01576 811 QRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEAR 890
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 322 ISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQ 401
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIA 970
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 402 KLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNL 481
Cdd:pfam01576 971 ALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050
|
490 500 510
....*....|....*....|....*....|
gi 9581821 482 AKFRKIQHELEEAEERADIAESQVNKLRVK 511
Cdd:pfam01576 1051 AARRKLQRELDDATESNESMNREVSTLKSK 1080
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
210-511 |
5.86e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 210 LNEMEIQLNHANRQAAEAIRnLRNTQGMLKDTQLHLddALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRV 289
Cdd:COG1196 195 LGELERQLEPLERQAEKAER-YRELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 290 AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLER 369
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 370 MKKNMEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNV 449
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEA-ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9581821 450 LRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVK 511
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
29-504 |
1.18e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 29 ALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGG 108
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 109 KHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQST 188
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 189 LDAEIRSRNDALRIKKKmEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANL 268
Cdd:COG1196 396 AELAAQLEELEEAEEAL-LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 269 MQAEIEELRASLEQTERSRRVAEQELLDASERVQLlhTQNTSLINTKKKLETDISQIQG-----EMEDIVQEARNAEEKA 343
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEG--VKAALLLAGLRGLAGAVAVLIGveaayEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 344 KKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVEN--EQKRN 421
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 422 IEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIA 501
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
...
gi 9581821 502 ESQ 504
Cdd:COG1196 713 EEE 715
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-497 |
2.21e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLD 81
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 82 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID 161
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 162 RKIAEKDEEIDQLKRnhlrvvesmqstLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAiRNLRNTQGMLKDT 241
Cdd:COG1196 460 ALLELLAELLEEAAL------------LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA-LLLAGLRGLAGAV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 242 QLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINtkkkLETD 321
Cdd:COG1196 527 AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG----AAVD 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 322 ISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQ 401
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 402 KLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNL 481
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
490
....*....|....*.
gi 9581821 482 AKFRKIQHELEEAEER 497
Cdd:COG1196 763 EELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-304 |
2.64e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.70 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQnEVEDLMIDVER--------SNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVK 73
Cdd:TIGR02168 181 LERTRENLD-RLEDILNELERqlkslerqAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 74 NAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLEL 153
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 154 NQVKSEIDRKIAEKDEEIDQLK--RNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDL-NEMEIQLNHANRQAAEAIRN 230
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEelEAELEELESRLEELEEQLETLRSKVAQLELQIASLnNEIERLEARLERLEDRRERL 419
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9581821 231 LRNTQGMLKDTQLHLDDALRGQ-DDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLL 304
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
41-382 |
3.28e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 41 LAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQ 120
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 121 IDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRvVESMQSTLDAEIRSRNDAL 200
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 201 RIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASL 280
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 281 EQTERSRRVAEQELLDASERVQLLHTQNTSLINTKK-KLETDISQIQGEMEDIvqearnaeEKAKKAITDAAMMA-EELK 358
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALEnKIEDDEEEARRRLKRL--------ENKIKELGPVNLAAiEEYE 996
|
330 340
....*....|....*....|....
gi 9581821 359 KEQDTSAHLERMKKNMEQTVKDLQ 382
Cdd:TIGR02168 997 ELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-519 |
4.25e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLD 81
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 82 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLE--------L 153
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEelqeelerL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 154 NQVKSEIDRKIAEKDEEIDQLKRNH------LRVVESMQSTLDAEIRSRNDALRIKKKMEGDLN--------------EM 213
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELaqlqarLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlselisvdegyeaAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 214 EIQL----------------------------------------NHANRQAAEAIRNLRNTQGMLKD-----TQLH---- 244
Cdd:TIGR02168 540 EAALggrlqavvvenlnaakkaiaflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFLGVAKDlvkfdPKLRkals 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 245 -----------LDDALRGQDDLKEQLAMV-----------------ERRANLMQA---EIEELRASLEQTERSRRVAEQE 293
Cdd:TIGR02168 620 yllggvlvvddLDNALELAKKLRPGYRIVtldgdlvrpggvitggsAKTNSSILErrrEIEELEEKIEELEEKIAELEKA 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 294 LLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKN 373
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 374 MEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQ 453
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9581821 454 DLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKV 519
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
46-344 |
2.61e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 46 QKYEETQAELEASQKESRSLstELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEK 125
Cdd:COG1196 213 ERYRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 126 SELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESmQSTLDAEIRSRNDALRIKKK 205
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 206 MEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTER 285
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 9581821 286 SRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAK 344
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
133-488 |
7.13e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 133 EEAEASLEHEEGKILRIQLELNQVKSEIDR--KIAEKDEEIDQLKRnhlrvvesmqstlDAEIRSRNDALRIKKKMEGDL 210
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERQLEPleRQAEKAERYRELKE-------------ELKELEAELLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 211 NEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVA 290
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 291 EQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERM 370
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 371 KKNMEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVL 450
Cdd:COG1196 402 LEELEEAEEALLERLERLEE-ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350
....*....|....*....|....*....|....*...
gi 9581821 451 RLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQ 488
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
30-499 |
1.15e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.39 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 30 LDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELfkvkNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGK 109
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEA----EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 110 HIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKilriqlelnqvKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTL 189
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK-----------KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK 1464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 190 DAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQgmlKDTQLHLDDALRGQDDLKEqlAMVERRAN-L 268
Cdd:PTZ00121 1465 KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEAKKADEAKK--AEEAKKADeA 1539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 269 MQAEIEELRASLEQTERSRRVAEQELLDASERVQllHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAiT 348
Cdd:PTZ00121 1540 KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAE--EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA-E 1616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 349 DAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQH-RLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKG 427
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK 1696
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9581821 428 LRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAE---EQSNVNLAKFRKIQHELEEAEERAD 499
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKkkaEEAKKDEEEKKKIAHLKKEEEKKAE 1771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
210-515 |
1.28e-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: 61.23 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 210 LNEMEIQLNHANRQAAEAIRnLRNTQGMLKDTQLHL-----DDALRGQDDLKEQLAMVE-------RRANLMQAEIEELR 277
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAER-YKELKAELRELELALlvlrlEELREELEELQEELKEAEeeleeltAELQELEEKLEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 278 ASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEEL 357
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 358 KKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKE 437
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRS-KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9581821 438 LtyQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREV 515
Cdd:TIGR02168 433 A--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-509 |
4.35e-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: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 225 AEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLL 304
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 305 HTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHR 384
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 385 LDEAEQLA------LKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDK 458
Cdd:TIGR02168 840 LEDLEEQIeelsedIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 9581821 459 LQTKVKAYKRQAEEAEEQSNVNLAKFR-KIQHELEEAEERADIAESQVNKLR 509
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEAR 971
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
158-476 |
8.50e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 158 SEIDRKIAEKDEEIDQLKRNHLR---VVESMQSTLDAEIRSRNDALR------IKKKMEG-----DLNEMEIQLNHANRQ 223
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERyqallkEKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 224 AAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQL-AMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQ 302
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 303 LLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSA----HLERMKKNMEQTV 378
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 379 KDLQHRLDEAEQLALKGG--KKQIQKLEARVRELENEVENEQKRnieavkgLRKHERRVKELTYQTEEDRKNVLRLQDLV 456
Cdd:TIGR02169 406 RELDRLQEELQRLSEELAdlNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340
....*....|....*....|
gi 9581821 457 DKLQTKVKAYKRQAEEAEEQ 476
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQ 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
255-518 |
4.96e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 255 LKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQ 334
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 335 EARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMkknmeqtvkDLQHRLDEAEQLALKGgKKQIQKLEARVRELENEV 414
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEAR---------LSHSRIPEIQAELSKL-EEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 415 ENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEA 494
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260
....*....|....*....|....
gi 9581821 495 EERADIAESQVNKLRVKSREVHTK 518
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAK 925
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2-511 |
9.93e-07 |
|
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: 51.66 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQNEVEDLMIDVERSNAacaaLDKKQRNF-DKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESL 80
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNE----LHEKQKFYlRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 81 DQLETLKRENKNLQQEISDLTEQIaeggkhiHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLElnQVKSEI 160
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQL-------RKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFR--SLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 161 DRKIAEKDEEIDQLKrNHLRVVESMQSTLDAEIRSRNDAL--RIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGML 238
Cdd:pfam15921 223 SKILRELDTEISYLK-GRIFPVEDQLEALKSESQNKIELLlqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 239 KDTQlhlddalrgqDDLKEQLAMVERRANLMQAEIEELRASLEQterSRRVAEQELLDASERVQLLHTQntslintkkkl 318
Cdd:pfam15921 302 EIIQ----------EQARNQNSMYMRQLSDLESTVSQLRSELRE---AKRMYEDKIEELEKQLVLANSE----------- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 319 etdISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlalkggkk 398
Cdd:pfam15921 358 ---LTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNM-------- 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 399 QIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKnvlRLQDLVDKLQTkvkayKRQAEEAEEQSN 478
Cdd:pfam15921 427 EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE---MLRKVVEELTA-----KKMTLESSERTV 498
|
490 500 510
....*....|....*....|....*....|...
gi 9581821 479 VNLAKfrkiqhELEEAEERADIAESQVNKLRVK 511
Cdd:pfam15921 499 SDLTA------SLQEKERAIEATNAEITKLRSR 525
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
160-503 |
1.30e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.44 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 160 IDRKIAEKDEEIDQLKRNHLRVVESM--QSTLDAEIRSRNDALRIKKKMEGDLnemEIQLNHANRQAAEAIRnLRNTQGM 237
Cdd:PLN02939 61 SNSKLQSNTDENGQLENTSLRTVMELpqKSTSSDDDHNRASMQRDEAIAAIDN---EQQTNSKDGEQLSDFQ-LEDLVGM 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 238 LKDTQ---LHLDDA-LRGQDDLKEQLAmvERRAnlMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLIN 313
Cdd:PLN02939 137 IQNAEkniLLLNQArLQALEDLEKILT--EKEA--LQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 314 TKKKLETDISQIQGEMEDIVQEarNAEEKAkkaitDAAMMAEELKKEQDTS---AHLERMKKNMEQTVKDLQHRLDEAEQ 390
Cdd:PLN02939 213 RGATEGLCVHSLSKELDVLKEE--NMLLKD-----DIQFLKAELIEVAETEervFKLEKERSLLDASLRELESKFIVAQE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 391 LALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKH---ERRVKELTYQTEEdrKNVLRLQ-DLVDKLQTKVKAY 466
Cdd:PLN02939 286 DVSKLSPLQYDCWWEKVENLQDLLDRATNQVEKAALVLDQNqdlRDKVDKLEASLKE--ANVSKFSsYKVELLQQKLKLL 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 9581821 467 KR--QAEEAEEQSNVNL-----AKFRKIQHELEEAEERADIAES 503
Cdd:PLN02939 364 EErlQASDHEIHSYIQLyqesiKEFQDTLSKLKEESKKRSLEHP 407
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
11-506 |
1.66e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 11 NEVEDLMIDVERSNAACAALDKKQRNFDKVLAEW-KQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRE 89
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLaELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 90 NKNLQQEISDLTEQIAEGG--------KHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID 161
Cdd:COG4913 318 LDALREELDELEAQIRGNGgdrleqleREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 162 RKIAEKDEEIDQLKRNH-------------LRVVESMQSTLDAEIRSRNDALRIK-KKMEGDL----NEMEIQLNHAN-R 222
Cdd:COG4913 398 EELEALEEALAEAEAALrdlrrelreleaeIASLERRKSNIPARLLALRDALAEAlGLDEAELpfvgELIEVRPEEERwR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 223 QAAE-AIRNLRNTqgMLKDTQlHLDDALRGQDDLKeqlamverranlmqaeieeLRASLeQTERSRRVAEQELLDASERV 301
Cdd:COG4913 478 GAIErVLGGFALT--LLVPPE-HYAAALRWVNRLH-------------------LRGRL-VYERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 302 QLLHtqntslintkkKLETDISQIQGEMEDIVQEARNAE--------EKAKKAITDAAMMAeelkkeQDTSAHlermkkn 373
Cdd:COG4913 535 SLAG-----------KLDFKPHPFRAWLEAELGRRFDYVcvdspeelRRHPRAITRAGQVK------GNGTRH------- 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 374 meqtVKDLQHRLDE--------AEQLALKggKKQIQKLEARVRELENEVE---------NEQKRNIEAVKGLRKHERRVK 436
Cdd:COG4913 591 ----EKDDRRRIRSryvlgfdnRAKLAAL--EAELAELEEELAEAEERLEaleaeldalQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9581821 437 ELTY---QTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVN 506
Cdd:COG4913 665 SAEReiaELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
94-304 |
1.67e-06 |
|
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: 50.15 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 94 QQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQ 173
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 174 LKRNHLRVVESMQStldAEIRSRNDALRIKKKMEG--DLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRG 251
Cdd:COG4942 99 LEAQKEELAELLRA---LYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9581821 252 QDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLL 304
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
68-508 |
2.32e-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: 50.56 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 68 ELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKIL 147
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 148 RIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVV--ESMQSTLDAEI----RSRNDALRIKKKMEGDLNEMEIQLNHAN 221
Cdd:pfam01576 93 QLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVttEAKIKKLEEDIllleDQNSKLSKERKLLEERISEFTSNLAEEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 222 RQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERV 301
Cdd:pfam01576 173 EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 302 QLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDL 381
Cdd:pfam01576 253 EEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTEL 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 382 QHRLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQT 461
Cdd:pfam01576 333 KKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 9581821 462 KVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKL 508
Cdd:pfam01576 413 QLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL 459
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-176 |
2.69e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 1 SLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEwkQKYEETQAELEASQKESRSLSTELFKVKNAYEESL 80
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 81 DQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEI 160
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
|
170
....*....|....*.
gi 9581821 161 DRKIAEKDEEIDQLKR 176
Cdd:TIGR02169 906 EELEAQIEKKRKRLSE 921
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
20-294 |
3.64e-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: 50.07 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 20 VERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISD 99
Cdd:TIGR02169 676 LQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 100 LTEQIAEGGKHIHELEkikkqidQEKSELQASLEEAEASLEHEEGKILRIQL-ELNQVKSEIDRKIAEKDEEIDQLKRNH 178
Cdd:TIGR02169 756 VKSELKELEARIEELE-------EDLHKLEEALNDLEARLSHSRIPEIQAELsKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 179 LRVVESMQstldaEIRSRNDALRIKKKMEGDlnemeiQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQ 258
Cdd:TIGR02169 829 EYLEKEIQ-----ELQEQRIDLKEQIKSIEK------EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270
....*....|....*....|....*....|....*.
gi 9581821 259 LAMVERRANLMQAEIEELRASLEQTERSRRVAEQEL 294
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
46-266 |
4.28e-06 |
|
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: 48.99 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 46 QKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEK 125
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 126 SELQASLEEAEASLeHEEGKILRIQLELNQVKSEidrKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKK 205
Cdd:COG4942 100 EAQKEELAELLRAL-YRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9581821 206 MEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRA 266
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-330 |
4.84e-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: 49.67 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLD 81
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 82 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQ-------EKSELQASLEEAEASLEHEEGKILRIQLELN 154
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieslaaEIEELEELIEELESELEALLNERASLEEALA 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 155 QVKSEIDRKIAEkdeeidqlkrnhLRVVESMQSTLDAEIRSRNDALrikKKMEGDLNEMEIQLNHANRQAAEairnlrnt 234
Cdd:TIGR02168 891 LLRSELEELSEE------------LRELESKRSELRRELEELREKL---AQLELRLEGLEVRIDNLQERLSE-------- 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 235 qgmlkDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEEL-RASLEqtersrrvAEQELLDASERVQLLHTQNTSLIN 313
Cdd:TIGR02168 948 -----EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgPVNLA--------AIEEYEELKERYDFLTAQKEDLTE 1014
|
330
....*....|....*..
gi 9581821 314 TKKKLETDISQIQGEME 330
Cdd:TIGR02168 1015 AKETLEEAIEEIDREAR 1031
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
86-342 |
8.01e-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: 8.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 86 LKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHE-EGKILRIQLELNQVKSEI---D 161
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIaslE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 162 RKIAEKDEEIDQLKrNHLRVVESMQSTLDAEIRSRNDALRIKK----KMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGM 237
Cdd:TIGR02169 308 RSIAEKERELEDAE-ERLAKLEAEIDKLLAEIEELEREIEEERkrrdKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 238 LKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKK 317
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260
....*....|....*....|....*
gi 9581821 318 LETDISQIQGEMEDIVQEARNAEEK 342
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRE 491
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1-177 |
1.07e-05 |
|
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: 48.09 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 1 SLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESL 80
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 81 DQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHE--EGKILRIQLELNQVKS 158
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQ 575
|
170 180
....*....|....*....|..
gi 9581821 159 EID---RKIAEKDEEIDQLKRN 177
Cdd:TIGR04523 576 TQKslkKKQEEKQELIDQKEKE 597
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
256-519 |
1.17e-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: 48.14 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 256 KEQLAMVERRANLMQAEIEELRASLEQTERSRRVAE--QELLDASERVQLlhtqnTSLINTKKKLETDISQIQGEMEDIV 333
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryQALLKEKREYEG-----YELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 334 QEArnaeEKAKKAITDAAMMAEELKKEQDTSAhlERMKKNMEQTVKDLQHRLDEAEqlalkggkKQIQKLEARVRELENE 413
Cdd:TIGR02169 251 EEL----EKLTEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELE--------AEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 414 VENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEE 493
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260
....*....|....*....|....*.
gi 9581821 494 AEERADIAESQVNKLRVKSREVHTKV 519
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEEL 422
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
81-414 |
1.27e-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: 48.14 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 81 DQLETLKRENKNLQQE-------ISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLEL 153
Cdd:TIGR02169 681 ERLEGLKRELSSLQSElrrienrLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 154 NQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRikkKMEGDLNEMEIQLNHANRQAAEAIRNLRN 233
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 234 TQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLIN 313
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 314 TKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAhLERMKKNMEQTVKDLQHRLDE--AEQL 391
Cdd:TIGR02169 918 RLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA-LEPVNMLAIQEYEEVLKRLDElkEKRA 996
|
330 340
....*....|....*....|...
gi 9581821 392 ALKGGKKQIQKLEARVRELENEV 414
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
315-478 |
1.51e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 315 KKKLETDISQIQGEMEDIVQEARN-AEEKAKKAITDAAMMAEELKKEQDTSAHLERMK-KNMEQTVKDLQHRLDEAEQLA 392
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeAEAIKKEALLEAKEEIHKLRNEFEKELRERRNElQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 393 lkggKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLrLQDLVDKLQTKVKAYKRQAE- 471
Cdd:PRK12704 106 ----EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEIL-LEKVEEEARHEAAVLIKEIEe 180
|
....*..
gi 9581821 472 EAEEQSN 478
Cdd:PRK12704 181 EAKEEAD 187
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1-390 |
1.56e-05 |
|
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: 47.86 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 1 SLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESL 80
Cdd:pfam01576 177 SLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEET 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 81 DQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEI 160
Cdd:pfam01576 257 AQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKAL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 161 DRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKD 240
Cdd:pfam01576 337 EEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 241 TQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLET 320
Cdd:pfam01576 417 LQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLED 496
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 321 DISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQ 390
Cdd:pfam01576 497 ERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAA 566
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
257-477 |
1.73e-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: 47.07 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 257 EQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEA 336
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 337 RNAEEKAKKAITDAAMMAE----ELKKEQDTSAHLERMKKNMEQTVKDLQHRLDE--AEQLALKGGKKQIQKLEARVREL 410
Cdd:COG4942 100 EAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEElrADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9581821 411 ENEVENEQKRNIEAVKglrKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQS 477
Cdd:COG4942 180 LAELEEERAALEALKA---ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2-508 |
3.62e-05 |
|
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: 46.71 E-value: 3.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLD 81
Cdd:pfam01576 66 LAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 82 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID 161
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 162 RKIAEKDEEIDQLKRNHlRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDT 241
Cdd:pfam01576 226 ELQAQIAELRAQLAKKE-EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEAL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 242 QLHLDDALRGQDDLKEQLAMVERR-ANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLET 320
Cdd:pfam01576 305 KTELEDTLDTTAAQQELRSKREQEvTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALES 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 321 DISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGkKQI 400
Cdd:pfam01576 385 ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS-KDV 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 401 QKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVN 480
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEAL 543
|
490 500
....*....|....*....|....*...
gi 9581821 481 LAKFRKIQHELEEAEERADIAESQVNKL 508
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDKL 571
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
77-280 |
3.66e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 77 EESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKikkqidqEKSELQASLEEAEASLEHEEGKILRIQLELNQv 156
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA-------EVEELEAELEEKDERIERLERELSEARSEERR- 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 157 KSEIDRKIAEKDEEIDQLKRNhLRVVESMQSTLDAEIRsrndalRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQG 236
Cdd:COG2433 460 EIRKDREISRLDREIERLERE-LEEERERIEELKRKLE------RLKELWKLEHSGELVPVKVVEKFTKEAIRRLEEEYG 532
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 9581821 237 MLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASL 280
Cdd:COG2433 533 LKEGDVVYLRDASGAGRSTAELLAEAGPRAVIVPGELSEAADEV 576
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-175 |
3.81e-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: 46.60 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLD 81
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 82 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID 161
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
170
....*....|....*..
gi 9581821 162 R---KIAEKDEEIDQLK 175
Cdd:TIGR02169 480 RvekELSKLQRELAEAE 496
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
125-518 |
4.21e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 125 KSELQASLEEAEASLEHEEGKILRIQL-ELNQVKSEIDRKIAEKDEEIDQLKRNhlrvVESMQSTLDAEIRSRNDALRIK 203
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLnGLESELAELDEEIERYEEQREQARET----RDEADEVLEEHEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 204 KKMEgDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKD------TQLHLDDAlrGQDDLKEQLAMVERRANLMQAEIEELR 277
Cdd:PRK02224 258 AEIE-DLRETIAETEREREELAEEVRDLRERLEELEEerddllAEAGLDDA--DAEAVEARREELEDRDEELRDRLEECR 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 278 ASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEEL 357
Cdd:PRK02224 335 VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 358 KKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQL--------------------ALKGGKKQIQKLEARVRELENEVENE 417
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARERVEEAEALleagkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 418 QKRnIEAVKGLRKHERRVKELtyqtEEDRKNVlrlQDLVDKLQTKVKAYKRQAEEAEEQSNvnlakfrKIQHELEEAEER 497
Cdd:PRK02224 495 EER-LERAEDLVEAEDRIERL----EERREDL---EELIAERRETIEEKRERAEELRERAA-------ELEAEAEEKREA 559
|
410 420
....*....|....*....|.
gi 9581821 498 ADIAESQVNKLRVKSREVHTK 518
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSK 580
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-230 |
5.51e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVlaewkQKYEETQAELEASQKESRSLSTELfkvkNAYEESLD 81
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWDEIDVASAEREIAELEAEL----ERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 82 QLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHE--------------EGKIL 147
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElralleerfaaalgDAVER 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 148 RIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGD------------LNEMEI 215
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyeerfkelLNENSI 845
|
250
....*....|....*....
gi 9581821 216 Q----LNHANRQAAEAIRN 230
Cdd:COG4913 846 EfvadLLSKLRRAIREIKE 864
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1-349 |
9.41e-05 |
|
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: 45.01 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 1 SLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESL 80
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 81 DQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQ---LELNQVK 157
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEkelKKLNEEK 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 158 SEIDRKIAEKDEEIDQLKRNhLRVVESMQSTLDAEIRSRNDALrIKKKMEGDLNEMEIQLNHANRQaaeaIRNLRNTQGM 237
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEK-IEKLESEKKEKESKISDLEDEL-NKDDFELKKENLEKEIDEKNKE----IEELKQTQKS 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 238 LKDTQLHLDDalrgqddlkeqlamverRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKK 317
Cdd:TIGR04523 580 LKKKQEEKQE-----------------LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK 642
|
330 340 350
....*....|....*....|....*....|..
gi 9581821 318 LETDISQIQGEMEDIVQEARNAEEKAKKAITD 349
Cdd:TIGR04523 643 LKQEVKQIKETIKEIRNKWPEIIKKIKESKTK 674
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
252-488 |
1.96e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 252 QDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRV--AEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEM 329
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 330 EDIvQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMK----------KNMEQTVKDLQHRLDEAEQLALKGGKKQ 399
Cdd:COG3206 243 AAL-RAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSarytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 400 IQKLEARVRELENEVENEQKRnieaVKGLRKHERRVKELTYQTEEDRKNvlrLQDLVDKLQtkvkaykrqaeEAEEQSNV 479
Cdd:COG3206 322 LEALQAREASLQAQLAQLEAR----LAELPELEAELRRLEREVEVAREL---YESLLQRLE-----------EARLAEAL 383
|
....*....
gi 9581821 480 NLAKFRKIQ 488
Cdd:COG3206 384 TVGNVRVID 392
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
49-315 |
1.97e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 49 EETQAELEASQKeSRSLSTELFKVKNAYEESLDQL---ETLKRENKNLQQEISDLTEQIAEGGKhihELEKIKKQIDQEK 125
Cdd:PRK11281 39 ADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLdkiDRQKEETEQLKQQLAQAPAKLRQAQA---ELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 126 SE--LQASLEEAEASLEHEEGKILRIQLELNQVKSEIdrkIAEKdeeiDQLKRNHLRVVESMQSTLdaEIRSRNDALRIK 203
Cdd:PRK11281 115 REtlSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQL---VSLQ----TQPERAQAALYANSQRLQ--QIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 204 KKmegDLNEMEIQLNHANRQAAEAiRNLRNTQGMLKDTQLHldDALRGQ-DDLKEQLAMVERRANLMQAEIEELRasLEQ 282
Cdd:PRK11281 186 GK---ALRPSQRVLLQAEQALLNA-QNDLQRKSLEGNTQLQ--DLLQKQrDYLTARIQRLEHQLQLLQEAINSKR--LTL 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 9581821 283 TERSrrVAEQELLDASERVQ---LLHTQntSLINTK 315
Cdd:PRK11281 258 SEKT--VQEAQSQDEAARIQanpLVAQE--LEINLQ 289
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
41-346 |
2.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 41 LAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQ 120
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 121 IDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDR-KIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDA 199
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAlSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 200 LRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRAS 279
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9581821 280 LEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKA 346
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
159-509 |
2.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 159 EIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGML 238
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 239 KDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKL 318
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 319 ETDISQIQGEMEDIvqEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKK 398
Cdd:COG4372 163 QEELAALEQELQAL--SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 399 QIQKLEARVRELENEVENEQKRNIEA-VKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQS 477
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAiLVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350
....*....|....*....|....*....|..
gi 9581821 478 NVNLAKFRKIQHELEEAEERADIAESQVNKLR 509
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
32-509 |
3.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 32 KKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKV----------KNAYEESLDQLETLKRENKNLQQEISDLT 101
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLekevkeleelKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 102 EQIAEGGKHIHELEKIKKQID--QEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAE---KDEEIDQLK- 175
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEleeKEERLEELKk 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 176 -----RNHLRVVESMQSTLDAEIRSRNDALRIKKKMEG----DLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLD 246
Cdd:PRK03918 346 klkelEKRLEELEERHELYEEAKAKKEELERLKKRLTGltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 247 DAL------RGQDDLKEQLAMVERRANLMQ---AEIEELRASLEQTERSRRVAEQEL------LDASERVQLLHTQNTSL 311
Cdd:PRK03918 426 KAIeelkkaKGKCPVCGRELTEEHRKELLEeytAELKRIEKELKEIEEKERKLRKELrelekvLKKESELIKLKELAEQL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 312 INTKKKLEtdiSQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDtsahLERMKKNMEQTVKDLQHRLDEAEQL 391
Cdd:PRK03918 506 KELEEKLK---KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE----LKKKLAELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 392 ALKGGKKQIQKLEARVRELEnEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQ-- 469
Cdd:PRK03918 579 LEELGFESVEELEERLKELE-PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKys 657
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 9581821 470 AEEAEEQSNVNLAKFRKI---QHELEEAEERADIAESQVNKLR 509
Cdd:PRK03918 658 EEEYEELREEYLELSRELaglRAELEELEKRREEIKKTLEKLK 700
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
30-509 |
3.90e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 30 LDKKQRNFDKVLAEWKQKYE----ETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIA 105
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEkdlhERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 106 EGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHeegkiLRIQLELNQVKSE-IDRKIAEKDEEIDQLKRNHLRVVES 184
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDD-----LLAEAGLDDADAEaVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 185 MQSTLDAEIRSRNDALRIKKKMEgDLNEMEIQLNHANRQAAEAIRNLRNTQGML----KDTQLHLDDALRGQDDLKEQLA 260
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAE-ELREEAAELESELEEAREAVEDRREEIEELeeeiEELRERFGDAPVDLGNAEDFLE 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 261 MVERRANLMQAEIEELRASLeQTERSRRVAEQELLDAS---ERVQLLhtQNTSLINTKKKLETDISQIQGEMEDIVQEAR 337
Cdd:PRK02224 416 ELREERDELREREAELEATL-RTARERVEEAEALLEAGkcpECGQPV--EGSPHVETIEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 338 NAEEKAKKaitdaammAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEaEQLALKGGKKQIQKLEARVRELENEVENE 417
Cdd:PRK02224 493 EVEERLER--------AEDLVEAEDRIERLEERREDLEELIAERRETIEE-KRERAEELRERAAELEAEAEEKREAAAEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 418 QKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAE--EQSNVNLAKFRKIQHELEEAE 495
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAElnDERRERLAEKRERKRELEAEF 643
|
490
....*....|....
gi 9581821 496 ERADIAESQVNKLR 509
Cdd:PRK02224 644 DEARIEEAREDKER 657
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
29-334 |
3.99e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.13 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 29 ALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKV-KNAYEESLDQLETLKRENKNLQQEISDLTEQIAEG 107
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 108 GKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEID---RKIAEKDEEIDQLKRNHlrvvES 184
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlrAELEEVDKEFAETRDEL----KD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 185 MQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVER 264
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 265 ranlmqaEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQ 334
Cdd:TIGR02169 470 -------ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS 532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1-497 |
6.28e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 1 SLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVknayeesL 80
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL-------Q 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 81 DQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEI 160
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 161 DRKIAEKD-------------------------------------------------------------EEIDQLKR--- 176
Cdd:TIGR02169 493 AEAEAQARaseervrggraveevlkasiqgvhgtvaqlgsvgeryataievaagnrlnnvvveddavakEAIELLKRrka 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 177 --------NHLR----------------------------------------VVESMQS-----------TLDAEI---- 193
Cdd:TIGR02169 573 gratflplNKMRderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlVVEDIEAarrlmgkyrmvTLEGELfeks 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 194 -------RSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRA 266
Cdd:TIGR02169 653 gamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 267 NLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISqiQGEMEDIVQEARNAEEKAKKA 346
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRI 810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 347 ITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDE--AEQLALKGGKK----QIQKLEARVRELENEVENEQKR 420
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSieKEIENLNGKKEeleeELEELEAALRDLESRLGDLKKE 890
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9581821 421 NIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNvNLAKFRKIQHELEEAEER 497
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEE 966
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2-389 |
6.44e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 2 LEKTKQRLQNEVEDLM---IDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEE 78
Cdd:pfam15921 470 LESTKEMLRKVVEELTakkMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 79 SLDQLETLKRENKN---LQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQ----- 150
Cdd:pfam15921 550 CEALKLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEarvsd 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 151 LELNQVK-----SEIDRKIAEKDEEIDQLkrnhLRVVESMQSTLDAeirSRNDALRIKKKMEGDLNEMEIQLNHANRQAA 225
Cdd:pfam15921 630 LELEKVKlvnagSERLRAVKDIKQERDQL----LNEVKTSRNELNS---LSEDYEVLKRNFRNKSEEMETTTNKLKMQLK 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 226 EAIRNLRNTQGMLKdtqlhlddALRGQDDLKEQLAMVerranlMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLH 305
Cdd:pfam15921 703 SAQSELEQTRNTLK--------SMEGSDGHAMKVAMG------MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLK 768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 306 TQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERmkknmEQTVKDLQHRL 385
Cdd:pfam15921 769 EEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ-----ESVRLKLQHTL 843
|
....
gi 9581821 386 DEAE 389
Cdd:pfam15921 844 DVKE 847
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
3-205 |
7.72e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 3 EKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNfdkvlaewkqkyEETQAELEASQKESRSLSTELFKVKnayeESLDQ 82
Cdd:NF012221 1568 EADRQRLEQEKQQQLAAISGSQSQLESTDQNALE------------TNGQAQRDAILEESRAVTKELTTLA----QGLDA 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 83 LETLKRENKNLQQE---------ISDLTEQIAEGGKHIHE-LEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLE 152
Cdd:NF012221 1632 LDSQATYAGESGDQwrnpfagglLDRVQEQLDDAKKISGKqLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQD 1711
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9581821 153 LNQVKSEIDRKiaeKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKK 205
Cdd:NF012221 1712 IDDAKADAEKR---KDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENK 1761
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
3-508 |
8.59e-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: 41.93 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 3 EKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVK---NAYEES 79
Cdd:TIGR04523 137 KKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKkkiQKNKSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 80 LDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSE 159
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 160 IDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALrikKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLK 239
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKII---SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 240 DTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLE 319
Cdd:TIGR04523 374 KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 320 TDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQlALKGGKKQ 399
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE-KIEKLESE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 400 IQKLEARVRELENEVE--NEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQS 477
Cdd:TIGR04523 533 KKEKESKISDLEDELNkdDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
490 500 510
....*....|....*....|....*....|.
gi 9581821 478 NVNLAKFRKIQHELEEAEERADIAESQVNKL 508
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIKSKKNKL 643
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
334-502 |
1.17e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 334 QEARNAEEKAKKAITDAAMMAEELKKEQdtsahlermkknmEQTVKDLQHRLdeaeqlalkggkkqIQKLEARVRELENE 413
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKEA-------------LLEAKEEIHKL--------------RNEFEKELRERRNE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 414 VENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKV-KAYKRQAEEAEEQSNVNLAKFRKIQHELE 492
Cdd:PRK12704 84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELeELIEEQLQELERISGLTAEEAKEILLEKV 163
|
170
....*....|
gi 9581821 493 EAEERADIAE 502
Cdd:PRK12704 164 EEEARHEAAV 173
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
324-523 |
1.24e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 324 QIQGEMEDIVQEARNAEEKAKKAItdAAMMAEELKKEQDTsahLERMKKNMEQTVKDLQHRLDEAEQlalkggkkQIQKL 403
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELAL--LVLRLEELREELEE---LQEELKEAEEELEELTAELQELEE--------KLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 404 EARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAK 483
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9581821 484 FRKIQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE 523
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
38-177 |
1.40e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 38 DKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEG---------- 107
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreelgerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 108 --------------------GKHIHELEKIKKQIDQEKSEL------QASLEEAEASLEHEEGKILRIQLELNQVKSEID 161
Cdd:COG3883 95 lyrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170
....*....|....*.
gi 9581821 162 RKIAEKDEEIDQLKRN 177
Cdd:COG3883 175 AQQAEQEALLAQLSAE 190
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
47-509 |
1.51e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 47 KYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAE------------------GG 108
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEkrdelngelsaadaavakDR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 109 KHIHELEKIKKQIDQEKSE-----------LQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRN 177
Cdd:pfam12128 322 SELEALEDQHGAFLDADIEtaaadqeqlpsWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 178 hlrvvesmqstldaeirSRNDALRIKKKMEGDLNEMEIQLNHanrQAAEAIRNLRNTQGMLK----DTQLHLDDALrGQD 253
Cdd:pfam12128 402 -----------------IREARDRQLAVAEDDLQALESELRE---QLEAGKLEFNEEEYRLKsrlgELKLRLNQAT-ATP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 254 DLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEM-EDI 332
Cdd:pfam12128 461 ELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlHFL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 333 VQEARNAEEKAKKAITDAAMMAEELKKEQDTSA------------HLERMKKN----MEQTvkdLQHRLDEAEQlALKGG 396
Cdd:pfam12128 541 RKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSvggelnlygvklDLKRIDVPewaaSEEE---LRERLDKAEE-ALQSA 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 397 KKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQteedrknvlrLQDLVDKLQTKVKAYKRQAEEA--- 473
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE----------KQSEKDKKNKALAERKDSANERlns 686
|
490 500 510
....*....|....*....|....*....|....*..
gi 9581821 474 -EEQSNVNLakfRKIQHELEEAEERADIAESQVNKLR 509
Cdd:pfam12128 687 lEAQLKQLD---KKHQAWLEEQKEQKREARTEKQAYW 720
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-473 |
1.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 4 KTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQaELEASQKESRSLSTELFKVKNAYEESLDQL 83
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 84 ETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKqidqEKSELQASLEEAEASLEHEEgKILRIQLELNQVKSEI-DR 162
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELEEKEERLEELKK----KLKELEKRLEELEERHELYE-EAKAKKEELERLKKRLtGL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 163 KIAEKDEEIDQLKRNHLRV------VESMQSTLDAEIRSRNDALRIKKKMEGD----------------LNEMEIQLNHA 220
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIeeeiskITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehrkelLEEYTAELKRI 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 221 NRQAAEAIRNLRNTQGMLK--DTQLHLDDALRGQDDLKEQLAMVERRanLMQAEIEELRASLEQTERSRRVAEQ------ 292
Cdd:PRK03918 465 EKELKEIEEKERKLRKELRelEKVLKKESELIKLKELAEQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKlkgeik 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 293 ELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDI-----------VQEARNAEEKAKKAITDAAMMAEELKKEQ 361
Cdd:PRK03918 543 SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesveeleerLKELEPFYNEYLELKDAEKELEREEKELK 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 362 DTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQ 441
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
490 500 510
....*....|....*....|....*....|....*...
gi 9581821 442 TEEDRKNVLRLQDL------VDKLQTKVKAYKRQAEEA 473
Cdd:PRK03918 703 LEEREKAKKELEKLekalerVEELREKVKKYKALLKER 740
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
55-502 |
1.59e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 55 LEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEe 134
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 135 aeasleheegkilriQLELNQVKSEIDRKIAEKDEEIDQLKRnhlrvvesmqstldaEIRSRNDALRIKKKMEGDLNEME 214
Cdd:COG4717 127 ---------------LLPLYQELEALEAELAELPERLEELEE---------------RLEELRELEEELEELEAELAELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 215 IQLNHANRQAAEAIRNLrntqgmLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQEL 294
Cdd:COG4717 177 EELEELLEQLSLATEEE------LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 295 LDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELK--KEQDTSAHLERMKK 372
Cdd:COG4717 251 LLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEelEEEELEELLAALGL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 373 NMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKRN-----------IEAVKGLRKHERRVKELTYQ 441
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAgvedeeelraaLEQAEEYQELKEELEELEEQ 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9581821 442 TEEDRKNVLRLQDLVDK--LQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAE 502
Cdd:COG4717 411 LEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
28-448 |
1.93e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 28 AALDKKQRNFDKVLAEWKQKYEETQAELEaSQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEG 107
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 108 GKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKilriqlelnqvKSEIDRKIAEKDEEIDQLKRNHLRVVESMQS 187
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK-----------KAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 188 TldAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRAN 267
Cdd:PTZ00121 1548 A--DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 268 LMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAI 347
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 348 TDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLAL-KGGKKQIQKLEARVRELENEVENEQKRNIEavK 426
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE--E 1783
|
410 420
....*....|....*....|..
gi 9581821 427 GLRKHERRVKELTYQTEEDRKN 448
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
54-523 |
1.96e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 54 ELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIdqekSELQASLE 133
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI----EELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 134 EAEASLEHEEGKILRIQLELNQVKSEID--RKIAEKDEEIDQLKRNHLRVVESMQSTLDAEirsrNDALRIKKKMEGDLN 211
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDEL----REIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 212 EMEIQLNHANRQAAEaIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVER-RANLMQAEIEELRASLEQTERSRRVA 290
Cdd:PRK03918 325 GIEERIKELEEKEER-LEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlKKRLTGLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 291 EQELLDASERVQLLHTQNTSLINTKKKLETD-------------------ISQIQGEMEDIVQEARNAEEKAKKAITDAA 351
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrelteehrkelLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 352 MMAEELKKEQDtsahLERMKKNMEQtVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVENeQKRNIEAVKGLRKH 431
Cdd:PRK03918 484 ELEKVLKKESE----LIKLKELAEQ-LKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS-LKKELEKLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 432 ERRVKELTYQTEEDRKNVLR---------LQDLVDKLQTKVKAYKR--QAEEAEEQSNVNLAKFRKIQHELEEAEERADI 500
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKeleelgfesVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAE 637
|
490 500
....*....|....*....|...
gi 9581821 501 AESQVNKLRVKSREVHTKVISEE 523
Cdd:PRK03918 638 TEKRLEELRKELEELEKKYSEEE 660
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-523 |
2.11e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 45 KQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEqIAEGGKHIHELEKIKKQIDQE 124
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 125 KSELQASLEEAEASLEHEEGKILRIQlELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKK 204
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELE-EKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 205 KMEGDLNEMEiqlnHANRQAAEAIRNLRNTQGMLKDTQLHLDDALrgqddlkEQLAMVERRANLMQAEIEElraslEQTE 284
Cdd:PRK03918 388 KLEKELEELE----KAKEEIEEEISKITARIGELKKEIKELKKAI-------EELKKAKGKCPVCGRELTE-----EHRK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 285 RSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQG--EMEDIVQEARNAEEKAKKaitdaaMMAEELKKEQD 362
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKK------YNLEELEKKAE 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 363 TSAHLERMKKNMEQTVKDLQHRLDEAEQL--ALKGGKKQIQKLEARVRELENEVENEQKRNIEAVkglrkhERRVKELty 440
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELEKLEELkkKLAELEKKLDELEEELAELLKELEELGFESVEEL------EERLKEL-- 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 441 qtEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEeqsnvnlakfrKIQHELEEAEERADIAESQVNKLRVKSREVHTKVI 520
Cdd:PRK03918 598 --EPFYNEYLELKDAEKELEREEKELKKLEEELD-----------KAFEELAETEKRLEELRKELEELEKKYSEEEYEEL 664
|
...
gi 9581821 521 SEE 523
Cdd:PRK03918 665 REE 667
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1-203 |
2.28e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 1 SLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESL 80
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 81 DQLETLKREN------------------KNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEA---SL 139
Cdd:COG4942 111 RALYRLGRQPplalllspedfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEeraAL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9581821 140 EHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIK 203
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
86-458 |
3.08e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 86 LKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIA 165
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 166 EKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHL 245
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 246 DDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQL---LHTQNTSLINTKKKLETDI 322
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaakLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 323 SQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMeqtvKDLQHRLDEAEQLALKGGKKQIQK 402
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK----DELELKKSEDLLKETQLVKLQEQL 486
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 9581821 403 LEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDK 458
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
22-523 |
3.92e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 22 RSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVknayEESLDQLETLKRENKNLQQEISDLT 101
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA----EEKKKADEAKKAEEKKKADEAKKKA 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 102 EQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKilRIQLELNQVKSEIDR-KIAEKDEEIDQLKRNHLR 180
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA--ADEAEAAEEKAEAAEkKKEEAKKKADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 181 VVESMQSTLDAEiRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQgmlkdtqlhlddalRGQDDLKEQLA 260
Cdd:PTZ00121 1390 KKKADEAKKKAE-EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA--------------KKADEAKKKAE 1454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 261 MVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLEtdiSQIQGEMEDIVQEARNAE 340
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD---EAKKAEEAKKADEAKKAE 1531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 341 EKAKkaiTDAAMMAEELKKEQDTSAhLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKR 420
Cdd:PTZ00121 1532 EAKK---ADEAKKAEEKKKADELKK-AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM 1607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 421 NIEAVKGLRKHERRVKELTyQTEEDRKNVLRLQDLVDKLQTKVKAYKRqAEEAEEQSNVNLAkfRKIQHELEEAEERADI 500
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKK-AEEENKIKAAEEA--KKAEEDKKKAEEAKKA 1683
|
490 500
....*....|....*....|...
gi 9581821 501 AESQVNKLRVKSREVHTKVISEE 523
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEE 1706
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
22-166 |
5.36e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 22 RSNAACAALDKKQRNFDKVLAEWKQKYEET--QAELEAsQKESRSLSTELFKVKNAYEESLDQLE-TLKRENKNLQQEIS 98
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIkkEALLEA-KEEIHKLRNEFEKELRERRNELQKLEkRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9581821 99 DLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEH------EEGKilriQLELNQVKSEIDRKIAE 166
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltaEEAK----EILLEKVEEEARHEAAV 173
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
40-381 |
5.91e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 40 VLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKK 119
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 120 QIDQEKSELQASLEEAEA---SLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSR 196
Cdd:COG4372 105 SLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 197 -NDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEE 275
Cdd:COG4372 185 lDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 276 LRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAE 355
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330 340
....*....|....*....|....*.
gi 9581821 356 ELKKEQDTSAHLERMKKNMEQTVKDL 381
Cdd:COG4372 345 LLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
91-517 |
6.45e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.42 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 91 KNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLE-EAEASLEHEEGKILRIQLELNQVK-SEIDRKIAEKD 168
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHrRNQLQPDPAKTKALQTVIEMKDTKiSSLERNIRDLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 169 EEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEgdlnEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDa 248
Cdd:pfam10174 254 DEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKID----QLKQELSKKESELLALQTKLETLTNQNSDCKQHIEV- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 249 lrgqddLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGE 328
Cdd:pfam10174 329 ------LKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 329 MEDIVQEARNAE-------EKAKKAITDAAMMAEELKKEQDTSAHLERMKKNM-EQTVKDLQHRLDEAEQL--ALKGGKK 398
Cdd:pfam10174 403 IENLQEQLRDKDkqlaglkERVKSLQTDSSNTDTALTTLEEALSEKERIIERLkEQREREDRERLEELESLkkENKDLKE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 399 QIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQtkvkaykrQAEEAEEQSN 478
Cdd:pfam10174 483 KVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNP 554
|
410 420 430
....*....|....*....|....*....|....*....
gi 9581821 479 VNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHT 517
Cdd:pfam10174 555 EINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVEN 593
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
162-389 |
7.35e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 162 RKIAEKDEEIDQLKRnHLRVVESMQSTLDAEIRSRNDALRIKKKMEgDLNEMEIQLNHANRQAAEA---IRNLRNTQGML 238
Cdd:COG4913 610 AKLAALEAELAELEE-ELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIDVASAEREIAELeaeLERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 239 KDTQLHLDDALRGQDDLKEQLAMVERRA-------NLMQAEIEELRASLEQTERSRRVAEQELLDasERVQLLHTQNtSL 311
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIgrlekelEQAEEELDELQDRLEAAEDLARLELRALLE--ERFAAALGDA-VE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 312 INTKKKLETDISQIQGEMEDIVQEARNAEEKAKK--------------AITDAAMMAEELkKEQDTSAHLERMK----KN 373
Cdd:COG4913 765 RELRENLEERIDALRARLNRAEEELERAMRAFNRewpaetadldadleSLPEYLALLDRL-EEDGLPEYEERFKellnEN 843
|
250
....*....|....*.
gi 9581821 374 MEQTVKDLQHRLDEAE 389
Cdd:COG4913 844 SIEFVADLLSKLRRAI 859
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
40-284 |
7.46e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 40 VLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAyEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKK 119
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 120 QIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDR--KIAEKDEEIDQLKRN--HLRVVESMQSTLDAEIRS 195
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEieRLREKREALAELNDERRE 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 196 RNDALRIKKK-MEGDLNEMEIQLNHANRQAAEAirnlrntqgMLKDTQLHLDDALRGQDDLKEQLAMVERRAnlmqAEIE 274
Cdd:PRK02224 628 RLAEKRERKReLEAEFDEARIEEAREDKERAEE---------YLEQVEEKLDELREERDDLQAEIGAVENEL----EELE 694
|
250
....*....|
gi 9581821 275 ELRASLEQTE 284
Cdd:PRK02224 695 ELRERREALE 704
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
28-175 |
8.68e-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: 37.98 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 28 AALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNL--QQEISDLTEQIA 105
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9581821 106 EGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLK 175
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| |
