|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-618 |
4.47e-18 |
|
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: 89.35 E-value: 4.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 51 LNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQnailQHTLQQQQQMLQQETMRNGELEDTQSKLEKQVSK 130
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER----LANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 131 QEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLS 210
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 211 QLDMVLDqtKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELR---DVLQKAQLSLE 287
Cdd:TIGR02168 425 ELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarlDSLERLQENLE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 288 EKYTTIKDLTAElRECKMEIEDKKQELIEMD------------------------------QALKERNWELKQRAAQVTH 337
Cdd:TIGR02168 503 GFSEGVKALLKN-QSGLSGILGVLSELISVDegyeaaieaalggrlqavvvenlnaakkaiAFLKQNELGRVTFLPLDSI 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 338 LDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESL------NEKLQNAKEQLREKEFIML--------------- 396
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvVDDLDNALELAKKLRPGYRivtldgdlvrpggvi 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 397 -----QNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQRE 471
Cdd:TIGR02168 662 tggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 472 IERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLEARM---QAEIKKLSSEVDSLKEAY---------------- 532
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIeelEAQIEQLKEELKALREALdelraeltllneeaan 821
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 533 -QIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQA 611
Cdd:TIGR02168 822 lRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
....*..
gi 1907166662 612 KISGHEK 618
Cdd:TIGR02168 902 ELRELES 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
126-620 |
4.96e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 126 KQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENK 205
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 206 SMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLS 285
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 286 LEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKernwELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSEL 365
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALA----ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 366 ELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMkemesvIKEQEDYIATQYKEVIDLGQELR 445
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG------LAGAVAVLIGVEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 446 LTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLEARMQAEIKKLSSEV 525
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 526 DSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANEALLIKESE 605
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
490
....*....|....*
gi 1907166662 606 LTRLQAKISGHEKTE 620
Cdd:COG1196 705 EERELAEAEEERLEE 719
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
243-593 |
6.19e-17 |
|
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: 85.88 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 243 ELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAqlsLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALK 322
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE---LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 323 ERNWELKQRAAQVTHLDMTIREHRGEM---EQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNE 399
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIeelEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 400 QEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQnthselvEARRQEVQAQREIERLAGEL 479
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA-------LLRSELEELSEELRELESKR 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 480 EDIKQLSKEKEAHGNRLAEELGASQVREAHLEARmqaeikklssevdsLKEAYQIEMISHQENHAKWKLSAESQKTSVQQ 559
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNLQER--------------LSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907166662 560 LNEQLEK-------AKQELEEAQDTVSNLHQQVQDRNEVIE 593
Cdd:TIGR02168 977 LENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
34-613 |
5.91e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 34 RQLDSALEICK-EELALHLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHtlqqqqqmlqqetm 112
Cdd:COG1196 216 RELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-------------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 113 rngELEDTQSKLEkQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKME 192
Cdd:COG1196 282 ---ELEEAQAEEY-ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 193 KEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQL 272
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 273 QELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQAL---KERNWELKQRAAQVTHLDMTIREHRGEM 349
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELaeaAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 350 EQKIIKLEGTL----EKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKE 425
Cdd:COG1196 518 GLRGLAGAVAVligvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 426 QEDYIATQYKEVIDLGQELRLtqeqmQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQV 505
Cdd:COG1196 598 GAAVDLVASDLREADARYYVL-----GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 506 REAHLEARMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKwKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQV 585
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA-EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*...
gi 1907166662 586 QDRNEVIEAANEALlikESELTRLQAKI 613
Cdd:COG1196 752 ALEELPEPPDLEEL---ERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-581 |
1.63e-14 |
|
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: 77.79 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 216 LDQTKTELEKTTNSVKELERLQHHTETElTETMQKREALENELQNAHGELksTLRQLQELRDVLQKAQLSLEEKYTTIKD 295
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQ-AEKAERYKELKAELRELELAL--LVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 296 LTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGEMEQkiiklegtlekselelkeCNKQVE 375
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN------------------LERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 376 SLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQykevidlgqelrltQEQMQNTH 455
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL--------------EEQLETLR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 456 SELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLE-ARMQAEIKKLSSEVDSLKEAYqi 534
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEAL-- 463
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1907166662 535 EMISHQENHAKWKL-SAESQKTSVQQLNEQLEKAKQELEEAQDTVSNL 581
Cdd:TIGR02168 464 EELREELEEAEQALdAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
281-613 |
5.29e-14 |
|
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: 76.25 E-value: 5.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 281 KAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREhrgeMEQKIIKLEGTL 360
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA----LRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 361 EKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDL 440
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 441 GQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLEARMQ---AE 517
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEelsEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 518 IKKLSSEVDSLKEAYQiemishqenhakwklsaeSQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANE 597
Cdd:TIGR02168 903 LRELESKRSELRRELE------------------ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIE 964
|
330
....*....|....*..
gi 1907166662 598 ALLIK-ESELTRLQAKI 613
Cdd:TIGR02168 965 DDEEEaRRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
170-500 |
1.06e-13 |
|
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: 75.09 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 170 LTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQ 249
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 250 KREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELREckmeIEDKKQELIEMDQALKERNWELK 329
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 330 QRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEI 409
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 410 ERTQQRMKEMESVIKEQEDYIatqykevidlgQELRLTQEQMQNTHSELvearrqEVQAQREIERLAGE----LEDIKQL 485
Cdd:TIGR02168 897 EELSEELRELESKRSELRREL-----------EELREKLAQLELRLEGL------EVRIDNLQERLSEEysltLEEAEAL 959
|
330
....*....|....*
gi 1907166662 486 SKEKEAHGNRLAEEL 500
Cdd:TIGR02168 960 ENKIEDDEEEARRRL 974
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
133-622 |
6.56e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 133 QELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTG---TARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQL 209
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREeleKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 210 SQLDMVLDQTKTELEKTTNSVKELERLQhhtetELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEK 289
Cdd:PRK03918 262 RELEERIEELKKEIEELEEKVKELKELK-----EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 290 YTTIKDLTAELRECKMEIE--DKKQELIEMDQALKERNWELKQRAAQVTHLDM-----TIREHRGEMEQKIIKLEGTLEK 362
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLTGLTPEKLekeleELEKAKEEIEEEISKITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 363 SELELKECNKQVESLNEK-----LQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQ---- 433
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseli 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 434 -YKEVIDLGQELR-----LTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVRE 507
Cdd:PRK03918 497 kLKELAEQLKELEeklkkYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 508 AHLEARMQAEIKKLSSEVDSLKEAYQ--IEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQV 585
Cdd:PRK03918 577 KELEELGFESVEELEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
490 500 510
....*....|....*....|....*....|....*..
gi 1907166662 586 QDrnEVIEAANEALLIKESELTRLQAKISGHEKTEDT 622
Cdd:PRK03918 657 SE--EEYEELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
45-573 |
1.28e-12 |
|
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: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 45 EELALHLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSKL 124
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 125 EkqvsKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGEN 204
Cdd:COG1196 329 E----EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 205 KSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQL 284
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 285 SLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALK------ERNWELKQRAAQVTHLDmtirehrGEMEQKIIKLEG 358
Cdd:COG1196 485 ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavLIGVEAAYEAALEAALA-------AALQNIVVEDDE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 359 TLEKSELELKECNKQ----VESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQY 434
Cdd:COG1196 558 VAAAAIEYLKAAKAGratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALR 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 435 KEVIDLGQELRLTQE-QMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLE-A 512
Cdd:COG1196 638 RAVTLAGRLREVTLEgEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEErL 717
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907166662 513 RMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEE 573
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
397-632 |
1.43e-12 |
|
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: 70.18 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 397 QNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLA 476
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 477 GELEDIKQLSkEKEAHGNRLAEELGASQVREAhleARMQAEIKKLSSEVDSLKEAYQiemiSHQENHAKWKLSAESQKTS 556
Cdd:COG4942 104 EELAELLRAL-YRLGRQPPLALLLSPEDFLDA---VRRLQYLKYLAPARREQAEELR----ADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907166662 557 VQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQAKISGHEKTEDTKYLPAPFTTL 632
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
53-421 |
1.44e-12 |
|
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: 71.64 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 53 QLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETS-EQNAILQHTLQQQQQMLQQETMRNGELEDTQSKLEkQVSKQ 131
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrEREKAERYQALLKEKREYEGYELLKEKEALERQKE-AIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 132 EQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTarqaklEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQ 211
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 212 LDMVLDQTKTELEKTTNSVKELERlqhhtetELTETMQKREALENELQnahgelkstlrqlqELRDVLQKAQLSLEEKYT 291
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELER-------EIEEERKRRDKLTEEYA--------------ELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 292 TIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREhrgeMEQKIIKLEGTLEKSELELKECN 371
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG----IEAKINELEEEKEDKALEIKKQE 454
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907166662 372 KQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMES 421
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
24-613 |
2.64e-12 |
|
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: 70.53 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 24 NRGMDTKNVVRQLDSALEICKEELALHLNQLE----RNKEKFERQLKKKSEEVYCLQKELKIKTHNLEET-----SEQNA 94
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDQLEalksESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKassarSQANS 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 95 ILQHTLQQQQQMLQQETMRNGELEDtqskLEKQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTA 174
Cdd:pfam15921 297 IQSQLEIIQEQARNQNSMYMRQLSD----LESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 175 RQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERL--------QHHTETELTE 246
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALlkamksecQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 247 TMQKREALEnELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNW 326
Cdd:pfam15921 453 IQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 327 ELKQRAAQVTHLDmtirehrgemeqkiiKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLK 406
Cdd:pfam15921 532 ELQHLKNEGDHLR---------------NVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 407 KEIERTQQRMKEMEsVIKEQEDyiaTQYKEVIDLGQELRLTQEQMQNTHSELVEARRqevqaqreierlageleDIKQls 486
Cdd:pfam15921 597 KEINDRRLELQEFK-ILKDKKD---AKIRELEARVSDLELEKVKLVNAGSERLRAVK-----------------DIKQ-- 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 487 kEKEahgnrlaeelgasqvreahleaRMQAEIKKLSSEVDSLKEAYQIEmishqenHAKWKLSAESQKTSVQQLNEQLEK 566
Cdd:pfam15921 654 -ERD----------------------QLLNEVKTSRNELNSLSEDYEVL-------KRNFRNKSEEMETTTNKLKMQLKS 703
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1907166662 567 AKQELEEAQDTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQAKI 613
Cdd:pfam15921 704 AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKI 750
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-442 |
4.81e-12 |
|
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: 69.71 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 32 VVRQLDSALEICKEELALHLNQLERNKEKFER--QLKKKSEEVyclqkELKIKTHNLEETSEQnailqhtlqqqqqmlqq 109
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKAERyqALLKEKREY-----EGYELLKEKEALERQ----------------- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 110 etmrngeledtQSKLEKQVSKQEQELQKqresSTEKLRKMEEKYETAIREVDLKRQKIIELTGTarqaklEMDQYKEELS 189
Cdd:TIGR02169 239 -----------KEAIERQLASLEEELEK----LTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 190 KMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERlqhhtetELTETMQKREALENELQNAHGELKSTL 269
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER-------EIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 270 RQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGEm 349
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 350 eqkiiklegtLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDY 429
Cdd:TIGR02169 450 ----------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
410
....*....|...
gi 1907166662 430 IATQYKEVIDLGQ 442
Cdd:TIGR02169 520 IQGVHGTVAQLGS 532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-422 |
1.29e-11 |
|
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: 68.56 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 144 EKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTEL 223
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 224 EKTTNSVKELE-RLQHHTET-----------ELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYT 291
Cdd:TIGR02169 754 ENVKSELKELEaRIEELEEDlhkleealndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 292 TIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLD---MTIREHRGEMEQKIIKLEGTLEKSELELK 368
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLEsrlGDLKKERDELEAQLRELERKIEELEAQIE 913
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 369 ECNKQVESLNEKLQNAKEQLREKEFIMLQNEQE------ISQLKKEIERTQQRMKEMESV 422
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALEPV 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
208-516 |
2.12e-11 |
|
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: 67.79 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 208 QLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLE 287
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 288 EKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQvthldmTIREHRGEMEQKIIKLEGTLEKSELEL 367
Cdd:TIGR02169 755 NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS------KLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 368 kecnkqvESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLT 447
Cdd:TIGR02169 829 -------EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 448 QEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKE-KEAHGNRLAEELGASQVREahLEARMQA 516
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdEEIPEEELSLEDVQAELQR--VEEEIRA 969
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-482 |
6.72e-11 |
|
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: 66.23 E-value: 6.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 117 LEDTQSKLEKQVSKqeqeLQKQRESsTEKLRKMEEKYETAIREVdlkrqkiieLTGTARQAKLEMDQYKEELSKMEKEII 196
Cdd:TIGR02168 191 LEDILNELERQLKS----LERQAEK-AERYKELKAELRELELAL---------LVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 197 HLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELR 276
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 277 DVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREhrgemeqkiikL 356
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-----------L 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 357 EGTLEKSELELKECNKQVESLNEKLQNAkeQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKE 436
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907166662 437 VIDLGQELRLTQEQMQNtHSELVEARRQEVQAQREIERLAGELEDI 482
Cdd:TIGR02168 484 LAQLQARLDSLERLQEN-LEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
215-609 |
6.90e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 6.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 215 VLDQTKTELEKTTNSVKELERLQHHT-----ETELTETMQKREALENELQNAhgelKSTLRQLQELRDVLQKAQLSLEEK 289
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEKEEKDLHErlnglESELAELDEEIERYEEQREQA----RETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 290 YTTIKDLTAELRECKMEIEDKKQELIEMDQA---LKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELE 366
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERleeLEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 367 LKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQE---DYIATQYKEVIDLGQE 443
Cdd:PRK02224 337 AQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRerfGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 444 LRLTQEQMQNTHSELVEARRQEVQAQREIERL--AG-------ELED--IKQLSKEKEAHGNRLAEELGASQVREAHLEA 512
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALleAGkcpecgqPVEGspHVETIEEDRERVEELEAELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 513 RMQA--EIKKLSSEVDSLKEAYQI--EMISHQENhakwklSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDR 588
Cdd:PRK02224 497 RLERaeDLVEAEDRIERLEERREDleELIAERRE------TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEA 570
|
410 420
....*....|....*....|.
gi 1907166662 589 NEVIEAANEALLIKESELTRL 609
Cdd:PRK02224 571 REEVAELNSKLAELKERIESL 591
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
50-426 |
8.76e-11 |
|
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: 65.85 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 50 HLNQLERNKE--KFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSKLEKQ 127
Cdd:TIGR02168 669 NSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 128 VSKQEQELQKQRESSTEkLRKMEEKYETAIREVDlkrQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSM 207
Cdd:TIGR02168 749 IAQLSKELTELEAEIEE-LEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 208 QLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLE 287
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 288 EKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKernwELKQRAAQVTHLDMtirehrGEMEQKIIKLEGTLEKSELEL 367
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRID----NLQERLSEEYSLTL------EEAEALENKIEDDEEEARRRL 974
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907166662 368 KECNKQVESLNEKLQNAKEQLRE----KEFImlqnEQEISQLKKEIERTQQRMKEMESVIKEQ 426
Cdd:TIGR02168 975 KRLENKIKELGPVNLAAIEEYEElkerYDFL----TAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
243-613 |
1.01e-10 |
|
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: 65.47 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 243 ELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALK 322
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 323 ERNWELKQRAAQVthldmtirehrGEMEQKIIKLEGTLEksELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEI 402
Cdd:TIGR02169 755 NVKSELKELEARI-----------EELEEDLHKLEEALN--DLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 403 SQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDI 482
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLREL 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 483 KqlskekeahgnRLAEELGASQVREAHLEARMQAEIKKLSSEVDSLkEAYQIEMISHQENhakwKLSAESQKTSVQQLNE 562
Cdd:TIGR02169 902 E-----------RKIEELEAQIEKKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEE----ELSLEDVQAELQRVEE 965
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166662 563 QLE-------KAKQELEEAQDTVSNLhqqvQDRNEVIEAANEALLIKESELTRLQAKI 613
Cdd:TIGR02169 966 EIRalepvnmLAIQEYEEVLKRLDEL----KEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
39-613 |
2.73e-10 |
|
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: 64.32 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 39 ALEICKEELALHLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRN-GEL 117
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSiAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 118 EDTQSKLEKQVSKQEQELQKQRESSTE----------KLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEE 187
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEElereieeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 188 LSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKS 267
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 268 TLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECK---MEIEDKKQ-------ELIEMD------------------- 318
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRaveEVLKASIQgvhgtvaQLGSVGeryataievaagnrlnnvv 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 319 -----------QALKERNwelkqrAAQVTHLDMTiREHRGEMEQKIIKLEGTLEKSeLELKECNKQVES----------L 377
Cdd:TIGR02169 554 veddavakeaiELLKRRK------AGRATFLPLN-KMRDERRDLSILSEDGVIGFA-VDLVEFDPKYEPafkyvfgdtlV 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 378 NEKLQNAKEQLREKEFIMLQNE-------------------QEISQLKKEIERTQQRMKEMEsvikeqedyiatqyKEVI 438
Cdd:TIGR02169 626 VEDIEAARRLMGKYRMVTLEGElfeksgamtggsraprggiLFSRSEPAELQRLRERLEGLK--------------RELS 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 439 DLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLEAR---MQ 515
Cdd:TIGR02169 692 SLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARieeLE 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 516 AEIKKLSSEVDSLKEAY--------QIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQD 587
Cdd:TIGR02169 772 EDLHKLEEALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKS 851
|
650 660
....*....|....*....|....*.
gi 1907166662 588 RNEVIEAANEALLIKESELTRLQAKI 613
Cdd:TIGR02169 852 IEKEIENLNGKKEELEEELEELEAAL 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
126-618 |
4.55e-10 |
|
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: 63.12 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 126 KQVSKQEQELQKqresSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENK 205
Cdd:TIGR04523 117 EQKNKLEVELNK----LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 206 SMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHT---ETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKA 282
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNnqlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 283 QLSLEEKYTTIKDLTAELRECKMEIEDKKQE--------------------------LIEMDQALKERNWELKQRAAQVT 336
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwnkelkselknqekkleeiqnqISQNNKIISQLNEQISQLKKELT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 337 HLDMTIREHRGEMEQK---IIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQ 413
Cdd:TIGR04523 353 NSESENSEKQRELEEKqneIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 414 QRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHG 493
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 494 NRLAEELGASQVREAHLEarmqAEIKKLSSEVDSLKEayqiEMISHQENHAKWKLsaesqKTSVQQLNEQLEKAKQELEE 573
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLE----SEKKEKESKISDLED----ELNKDDFELKKENL-----EKEIDEKNKEIEELKQTQKS 579
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1907166662 574 AQDTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQAKISGHEK 618
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
264-611 |
5.79e-10 |
|
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: 63.16 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 264 ELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAElRECKMEIEDKKQELIEMDQALKERNWE--LKQRAAQVTHLDmT 341
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREYEGYELLKEKEalERQKEAIERQLA-S 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 342 IREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNA-KEQLREKEfimlqneQEISQLKKEIERTQQRMKEME 420
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvKEKIGELE-------AEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 421 SVIKEQEdyiatqykevidlgQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEEL 500
Cdd:TIGR02169 322 ERLAKLE--------------AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 501 GASQVREAHLearmQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKlSAESQKTSVQQ----LNEQLEKAKQELEEAQD 576
Cdd:TIGR02169 388 KDYREKLEKL----KREINELKRELDRLQEELQRLSEELADLNAAIA-GIEAKINELEEekedKALEIKKQEWKLEQLAA 462
|
330 340 350
....*....|....*....|....*....|....*
gi 1907166662 577 TVSNLHQQVQDRNEVIEAANEALLIKESELTRLQA 611
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
361-613 |
5.85e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 361 EKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDL 440
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 441 GQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIK----QLSKEKEAHGNRLAEELGASQVREAHLEARmQA 516
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEekleELKEELESLEAELEELEAELEELESRLEEL-EE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 517 EIKKLSSEVDSLKEayQIEMISHQenhakwklsAESQKTSVQQLNEQLEKAKQELEEAQDTVSN-----LHQQVQDRNEV 591
Cdd:TIGR02168 380 QLETLRSKVAQLEL--QIASLNNE---------IERLEARLERLEDRRERLQQEIEELLKKLEEaelkeLQAELEELEEE 448
|
250 260
....*....|....*....|..
gi 1907166662 592 IEAANEALLIKESELTRLQAKI 613
Cdd:TIGR02168 449 LEELQEELERLEEALEELREEL 470
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
45-530 |
1.95e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 45 EELALHLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNgELEDTQSKL 124
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE-EYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 125 EKQVSKQEQELQ------KQRESSTEKLRKMEEKYETAIREVDlKRQKIIELTGTARQAKLEMDQYKEELS-----KMEK 193
Cdd:PRK03918 313 EKRLSRLEEEINgieeriKELEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEELERLKKRLTgltpeKLEK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 194 EIIHLKRDGENKSMQLSQLDMV---LDQTKTELEKTTNSVKELERLQHHTETELTETMQKR--EALENELQNAHGELKST 268
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEI 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 269 LRQLQELRDVLQKAQLSLEEKYTTIKdltaeLRECKMEIEDKKQELIEMDQALKERNWELKQraaqvthldmTIREHRGE 348
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIK-----LKELAEQLKELEEKLKKYNLEELEKKAEEYE----------KLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 349 MEQKIIKLEGTLEKSEL---ELKECNKQVESLNEKLQNAKEQLREKEFimlqneqeisqlkKEIERTQQRMKEMESVIKE 425
Cdd:PRK03918 537 LKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGF-------------ESVEELEERLKELEPFYNE 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 426 qedyiatqYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEahgnrlAEELGASQV 505
Cdd:PRK03918 604 --------YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE------YEELREEYL 669
|
490 500
....*....|....*....|....*
gi 1907166662 506 REAHLEARMQAEIKKLSSEVDSLKE 530
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKK 694
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
292-606 |
3.41e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.70 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 292 TIKDLTAELRECKMEIEDKKQEL---------IEMDQALkernwELKQRAA---QVTHLDMTIREH---RGEMEQKIIKL 356
Cdd:COG4913 156 DIRALKARLKKQGVEFFDSFSAYlarlrrrlgIGSEKAL-----RLLHKTQsfkPIGDLDDFVREYmleEPDTFEAADAL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 357 EG---TLEKSELELKECNKQVESL------NEKLQNAKEQLREKEFIM-----LQNEQEISQLKKEIERTQQRMKEmesv 422
Cdd:COG4913 231 VEhfdDLERAHEALEDAREQIELLepirelAERYAAARERLAELEYLRaalrlWFAQRRLELLEAELEELRAELAR---- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 423 ikeqedyiatqykevidLGQELRLTQEQMQNTHSELVEARRQEVQAQ-REIERLAGELEDIKQLSKEKEAHGNRLAEelg 501
Cdd:COG4913 307 -----------------LEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEA--- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 502 asQVREAHLEA-RMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKlsaesqkTSVQQLNEQLEKAKQELEEAQDTVSN 580
Cdd:COG4913 367 --LLAALGLPLpASAEEFAALRAEAAALLEALEEELEALEEALAEAE-------AALRDLRRELRELEAEIASLERRKSN 437
|
330 340
....*....|....*....|....*.
gi 1907166662 581 LHQQVQdrnEVIEAANEALLIKESEL 606
Cdd:COG4913 438 IPARLL---ALRDALAEALGLDEAEL 460
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
402-621 |
3.52e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 402 ISQLKKEIERTQQRMKEMES-------VIKEQEDYI---------ATQYKEVID---------LGQELRLTQEQMQNTHS 456
Cdd:COG1196 167 ISKYKERKEEAERKLEATEEnlerledILGELERQLeplerqaekAERYRELKEelkeleaelLLLKLRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 457 ELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLEARMQAEIKKLSSEVDSLKEAyQIEM 536
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL-EEEL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 537 ISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQAKISGH 616
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
....*
gi 1907166662 617 EKTED 621
Cdd:COG1196 406 EEAEE 410
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
186-573 |
6.34e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 186 EELSKMEKEIIHLKrDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGEL 265
Cdd:PRK03918 145 ESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 266 KSTLRQLQELRdvlqkaqlSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDmtireh 345
Cdd:PRK03918 224 EKLEKEVKELE--------ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK------ 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 346 rgEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEfimlQNEQEISQLKKEIERTQQRMKEMESVIKE 425
Cdd:PRK03918 290 --EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHEL 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 426 QEDyiATQYKEVIDlGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQV 505
Cdd:PRK03918 364 YEE--AKAKKEELE-RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPV 440
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907166662 506 --------REAHLEARMQAEIKKLSSEVDSLKEayQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEE 573
Cdd:PRK03918 441 cgrelteeHRKELLEEYTAELKRIEKELKEIEE--KERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKK 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
39-317 |
6.46e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 39 ALEICKEELALHLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELE 118
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 119 DTQSKLEKQVSKQEQELQKQRESSTE----------KLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEEL 188
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 189 SKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKST 268
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907166662 269 LRQLQElrdvlqKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEM 317
Cdd:TIGR02168 942 QERLSE------EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
243-621 |
7.89e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 243 ELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLE--EKYTTIKDLTAELRECKMEIEDKKQELiemdQA 320
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERL----EE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 321 LKERNWELKQRAAQVTHLDMTIREHRGEMEQKiikLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQ 400
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEEL---LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 401 EISQLKKEIERTQQR----------------------MKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSEL 458
Cdd:COG4717 228 ELEQLENELEAAALEerlkearlllliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 459 VEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLEArmQAEIKKLSSEVDSLKEAYQIEMIS 538
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE--ELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 539 HQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVS--NLHQQVQDRNEVIEAANEALLIKESELTRLQAKISGH 616
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
....*
gi 1907166662 617 EKTED 621
Cdd:COG4717 466 EEDGE 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
116-335 |
1.09e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 116 ELEDTQSKLeKQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEI 195
Cdd:COG4942 28 ELEQLQQEI-AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 196 IHLKRDGEnKSMQLSQLDMVLDQTK-TELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQE 274
Cdd:COG4942 107 AELLRALY-RLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907166662 275 LRDVLQKAQlslEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQV 335
Cdd:COG4942 186 ERAALEALK---AERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
64-623 |
1.13e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 64 QLKKKSEEVYCLQKE-LKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSKLEKQVSKQEQELQKQRESS 142
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEErNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 143 TEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEiihlKRDGENKSMQLSQLDMVLDQTKTE 222
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK----AEAAEKKKEEAKKKADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 223 LEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRE 302
Cdd:PTZ00121 1390 KKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 303 CKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHldmtiREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLN--EK 380
Cdd:PTZ00121 1470 KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK-----AAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKkaEE 1544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 381 LQNAKEQLREKEFIMLQNEQEISQLKKEIER---TQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSE 457
Cdd:PTZ00121 1545 KKKADELKKAEELKKAEEKKKAEEAKKAEEDknmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE 1624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 458 LVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEEL-GASQVREAHLEARMQAEIKKLSSEVDSLKEAYQIEM 536
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA 1704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 537 ISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQAKISGH 616
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
....*..
gi 1907166662 617 EKTEDTK 623
Cdd:PTZ00121 1785 LDEEDEK 1791
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
126-324 |
1.16e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.92 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 126 KQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENK 205
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 206 SMQLSQLDMVLDQtkTELEKTTNSVKELERLQHHTETELTETMQKREALENELQnahgELKSTLRQLQELRDVLQKAQLS 285
Cdd:COG3883 99 GGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA----ELEAKLAELEALKAELEAAKAE 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1907166662 286 LEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKER 324
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
240-445 |
1.40e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 240 TETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQ 319
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 320 ALKERNWELkQRAAQVTHLDMTIR-EHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQN 398
Cdd:COG4942 105 ELAELLRAL-YRLGRQPPLALLLSpEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907166662 399 EQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELR 445
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
343-637 |
1.45e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 343 REHRGEMEQKIIKLEGTLEKSELELKECNKQVESLN------EKLQNAKEQLREKEFIMLQNEqeISQLKKEIERTQQRM 416
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQLKSLErqaekaERYKELKAELRELELALLVLR--LEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 417 KEMEsvikeqedyiatqykevidlgQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRL 496
Cdd:TIGR02168 249 KEAE---------------------EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 497 AEELGASQVREAHLEARMQAEIKKLSSEVDSLKE-AYQIEMIshQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQ 575
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAElEEKLEEL--KEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907166662 576 DTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQAKISGHEKTEDTKYLPAPFTTLTEIIP 637
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-530 |
1.61e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.13 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 28 DTKNVVRQLDSALEiCKEELALH--LNQLERNKEKFERQLKKKSEevyclQKELKIKT-HNLEETSEQNAILQHTLQQQQ 104
Cdd:PRK02224 184 DQRGSLDQLKAQIE-EKEEKDLHerLNGLESELAELDEEIERYEE-----QREQARETrDEADEVLEEHEERREELETLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 105 QMLQQETMRNGELEDTQSKLEKQVSKQEQELQKQRESSTEKLRKME---EKYETAIREVDLKRQKIIELTGTARQAKLEM 181
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 182 DQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQH-------HTETELTETMQKREAL 254
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEelrerfgDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 255 ENELQNAHGELKSTLRQLQELRDVLQKAQLSLEE----------KYTTIKDLTAELRECKMEIEDKKQELIEMDQALKER 324
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 325 NWELKQRAAQVTHLDmTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEfimlQNEQEISQ 404
Cdd:PRK02224 498 LERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAE----EEAEEARE 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 405 LKKEIERTQQRMKEMesviKEQEDYIATQYKEVIDLGQELRLTQEQMQNThSELVEARRQEVQAQRE-IERLAGE----- 478
Cdd:PRK02224 573 EVAELNSKLAELKER----IESLERIRTLLAAIADAEDEIERLREKREAL-AELNDERRERLAEKRErKRELEAEfdear 647
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1907166662 479 LEDIKQLSKEKEAHGNRLAEELgaSQVREAhlEARMQAEIKKLSSEVDSLKE 530
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKL--DELREE--RDDLQAEIGAVENELEELEE 695
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
113-613 |
1.96e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 113 RNGELEDTQSKLEKQVSKQEQELQKQR-ESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEmdqykeELSKM 191
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLELLEAElEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 192 EKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEkttNSVKELERLQHHTETELTETMQKREALEN---ELQNAHGELKST 268
Cdd:COG4913 344 EREIERLERELEERERRRARLEALLAALGLPLP---ASAEEFAALRAEAAALLEALEEELEALEEalaEAEAALRDLRRE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 269 LRQLQELRDVLQKAQLSLEEKYTTIKDLTAElrECKMEIEDKK--QELIEMDQalKERNWEL----------------KQ 330
Cdd:COG4913 421 LRELEAEIASLERRKSNIPARLLALRDALAE--ALGLDEAELPfvGELIEVRP--EEERWRGaiervlggfaltllvpPE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 331 RAAQV------THLDMTIREHRGEMEQKIIKLEGTLEKS---ELELKECN------------------------------ 371
Cdd:COG4913 497 HYAAAlrwvnrLHLRGRLVYERVRTGLPDPERPRLDPDSlagKLDFKPHPfrawleaelgrrfdyvcvdspeelrrhpra 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 372 -------KQVESLNEKlqNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIAtQYKEVIDLGQEL 444
Cdd:COG4913 577 itragqvKGNGTRHEK--DDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRL 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 445 RLTQEQMQNTHSelVEARRQEVQAQRE-IERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLE---ARMQAEIKK 520
Cdd:COG4913 654 AEYSWDEIDVAS--AEREIAELEAELErLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEkelEQAEEELDE 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 521 LSSEVDSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQ--------VQDRNEVI 592
Cdd:COG4913 732 LQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpaeTADLDADL 811
|
570 580
....*....|....*....|....*
gi 1907166662 593 EAANE--ALL--IKESELTRLQAKI 613
Cdd:COG4913 812 ESLPEylALLdrLEEDGLPEYEERF 836
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
117-496 |
2.26e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 117 LEDTQSKLEKQVSKQEQELQKQRESSTEKLRKME---EKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEK 193
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 194 EIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREA----------LENELQNAHG 263
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 264 ELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLtaelRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIR 343
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDL----VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 344 EHRGEMEQKiiklEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEqEISQLKKEIERTQQRMKEMESVI 423
Cdd:PRK02224 548 ELEAEAEEK----REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLREKREALAELN 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 424 KEQEDYIATQYKEVIDLGQEL---RLTQEQ---------MQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEA 491
Cdd:PRK02224 623 DERRERLAEKRERKRELEAEFdeaRIEEARedkeraeeyLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
....*
gi 1907166662 492 HGNRL 496
Cdd:PRK02224 703 LENRV 707
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
391-610 |
2.65e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 391 KEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIAtQYKE---VIDLGQELRLTQEQMQNTHSELVEARRQEVQ 467
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEAALE-EFRQkngLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 468 AQREIERLAGELEDIKQLSKEKEAHG--NRLAEELGASQVREAHLEARMQAE---IKKLSSEVDSLKEAYQIEMishqen 542
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEA------ 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166662 543 hAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANEALlikESELTRLQ 610
Cdd:COG3206 312 -QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY---ESLLQRLE 375
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
350-533 |
4.75e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 350 EQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDY 429
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 430 IATQYKEVIDLGQ----ELRLTQEQMQNT------HSELVEARRQEVQA-QREIERLAGELEDIKQLSKEKEAHGNRLAE 498
Cdd:COG4942 106 LAELLRALYRLGRqpplALLLSPEDFLDAvrrlqyLKYLAPARREQAEElRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907166662 499 E---LGASQVREAHLEARMQAEIKKLSSEVDSLKEAYQ 533
Cdd:COG4942 186 EraaLEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
243-436 |
6.41e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 6.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 243 ELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALK 322
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 323 ERNWELKQR---------------------AAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKL 381
Cdd:COG4942 101 AQKEELAELlralyrlgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907166662 382 QNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKE 436
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
170-392 |
6.64e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 6.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 170 LTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQ 249
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 250 KREALENELQNAHGELKSTLRQLQELRD-------VLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALK 322
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRqpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 323 ERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKE 392
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
342-531 |
8.20e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 8.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 342 IREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEM-- 419
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 420 ----------ESVIKEQED---------YIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELE 480
Cdd:COG4942 112 alyrlgrqppLALLLSPEDfldavrrlqYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907166662 481 dikQLSKEKEAHGNRLAEELGASQVREAHL---EARMQAEIKKLSSEVDSLKEA 531
Cdd:COG4942 192 ---ALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
38-502 |
9.34e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 38 SALEICKEELALHLNQLERNKEKFERQLKKKSEEVyclqKELKIKTHNLEETSEqnaiLQHTLQQQQQMLQQETMRNGEL 117
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEI----EELEEKVKELKELKE----KAEEYIKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 118 EDTQSKLEKQVSKQEQELQKqRESSTEKLRKMEEKYETAIREVDlKRQKIIELTGTARQAKLEMDQYKEELS-----KME 192
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLE-ELEERHELYEEAKAKKEELERLKKRLTgltpeKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 193 KEIIHLKRDGENKSMQLSQLDMV---LDQTKTELEKTTNSVKELERLQHHTETELTETMQKR--EALENELQNAHGELKS 267
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 268 TLRQLQELRDVLQKAQ--LSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMD----QALKERNWELKqraAQVTHLDMT 341
Cdd:PRK03918 471 IEEKERKLRKELRELEkvLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKaeeyEKLKEKLIKLK---GEIKSLKKE 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 342 IREHRgEMEQKIIKLEGTLEKSELELKECNKQVESLN-EKLQNAKEQLRE-----KEFIMLQNeqeisqLKKEIERTQQR 415
Cdd:PRK03918 548 LEKLE-ELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKElepfyNEYLELKD------AEKELEREEKE 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 416 MKEMESVIKEQEDYIATQYKEVIDLgqELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNR 495
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEEL--RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
....*..
gi 1907166662 496 LAEELGA 502
Cdd:PRK03918 699 LKEELEE 705
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
355-519 |
1.70e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 54.78 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 355 KLEGTLEKSELELKECNKQVESLN-EKLQNAKEQLREKEfimLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQ 433
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEAEAIKkEALLEAKEEIHKLR---NEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 434 YKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQaqreierlagELEDIKQLSKEkEAHgNRLAEEL-------GASQVR 506
Cdd:PRK12704 109 EEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----------ELERISGLTAE-EAK-EILLEKVeeearheAAVLIK 176
|
170
....*....|...
gi 1907166662 507 EAHLEARMQAEIK 519
Cdd:PRK12704 177 EIEEEAKEEADKK 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
44-409 |
1.77e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.07 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 44 KEELALHLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSK 123
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 124 LEKQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTG----TARQAKLEMDQYKEELSKMEKEIIHLK 199
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 200 RDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENElqnaHGELKSTLRQLQELRDVL 279
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNE----YLELKDAEKELEREEKEL 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 280 QKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMD-QALKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEG 358
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907166662 359 TLEKSElELKECNKQVESLNEKLQNAKEQLRE-KEFIMLQNEQEISQLKKEI 409
Cdd:PRK03918 702 ELEERE-KAKKELEKLEKALERVEELREKVKKyKALLKERALSKVGEIASEI 752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
264-580 |
2.45e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 264 ELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDqALKERNWELKQRAAQVthldmtiR 343
Cdd:PRK03918 180 RLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEEIEELEKELESL-------E 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 344 EHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFiMLQNEQEISQLKKEIERTQQRMKEMESVI 423
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 424 KEQEDYIAtQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAG-ELEDIKQLSKEKEAHGNRLAEELGA 502
Cdd:PRK03918 331 KELEEKEE-RLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 503 SQVREAHLEARmqaeIKKLSSEVDSLKEAYQI------EMISHQENHAKWKLSAESQKTS--VQQLNEQLEKAKQELEEA 574
Cdd:PRK03918 410 ITARIGELKKE----IKELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIEkeLKEIEEKERKLRKELREL 485
|
....*.
gi 1907166662 575 QDTVSN 580
Cdd:PRK03918 486 EKVLKK 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
292-527 |
2.64e-07 |
|
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: 53.61 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 292 TIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVthldmtirehrGEMEQKIIKLEGTLEKSELELKECN 371
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-----------AALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 372 KQVESLNEKLQNAKEQLREKEFIMLQNEQEI-------SQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQEL 444
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 445 RLTQEQMQNTHSELVEARRQEVQAQREIERLageledIKQLSKEKEAHGNRLAeELGASQVREAHLEARMQAEIKKLSSE 524
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKL------LARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAER 242
|
...
gi 1907166662 525 VDS 527
Cdd:COG4942 243 TPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
251-517 |
4.34e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 251 REALEN--ELQNAHGELKSTLRQLQELRDVLQKAQlsleekyttikdltaelreckmEIEDKKQELIEMDQALKERNWEL 328
Cdd:COG4913 228 DALVEHfdDLERAHEALEDAREQIELLEPIRELAE----------------------RYAAARERLAELEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 329 KQRAAQvthldmtirehrgEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREkefimlQNEQEISQLKKE 408
Cdd:COG4913 286 AQRRLE-------------LLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG------NGGDRLEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 409 IERTQQRMKEMESVIKEQEDYIAT----------QYKEVIDLGQELRLT-QEQMQNTHSELVEARRQEVQAQREIERLAG 477
Cdd:COG4913 347 IERLERELEERERRRARLEALLAAlglplpasaeEFAALRAEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEA 426
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907166662 478 ELEDIKQ----LSKEKEAHGNRLAEELGAS-----------QVREAHLEARMQAE 517
Cdd:COG4913 427 EIASLERrksnIPARLLALRDALAEALGLDeaelpfvgeliEVRPEEERWRGAIE 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
250-433 |
5.28e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 250 KREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELK 329
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 330 QRAAQVTHLDM------------------TIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREK 391
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907166662 392 efiMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQ 433
Cdd:COG3883 177 ---QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-407 |
5.65e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 216 LDQTKTELEKTTNSVKELERLQHHTET--ELTETMQKREALENELQNAHGELKSTL--RQLQELRDVLQKAQLSLEEKYT 291
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERyaAARERLAELEYLRAALRLWFAQRRLELleAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 292 TIKDLTAELRECKM--------EIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKS 363
Cdd:COG4913 317 RLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907166662 364 ELELKECNKQVESLNEKLQNAKEQLREKefimlqnEQEISQLKK 407
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRRELREL-------EAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
351-574 |
6.87e-07 |
|
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: 52.46 E-value: 6.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 351 QKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYI 430
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 431 ATQYKEvidLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHL 510
Cdd:COG4942 100 EAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907166662 511 EArMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEA 574
Cdd:COG4942 177 EA-LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
30-499 |
7.89e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 30 KNVVRQLDSALEICKEELALHLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQ 109
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 110 ETMRNGELEDTQSKLEKQVSKQEQ----------ELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKL 179
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEaeeallerleRLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 180 EMDQYKEELSKMEKEIIHLKRD-GENKSMQLSQLDM-VLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENE 257
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEElAEAAARLLLLLEAeADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 258 LQNAHGELK-STLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERnwELKQRAAQVT 336
Cdd:COG1196 544 LAAALQNIVvEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA--DARYYVLGDT 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 337 HLDMTIREHRGEMEQKIIK-LEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQR 415
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVtLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 416 MKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELE-DIKQLSKEKEAHG- 493
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELErELERLEREIEALGp 781
|
....*..
gi 1907166662 494 -NRLAEE 499
Cdd:COG1196 782 vNLLAIE 788
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
178-605 |
1.37e-06 |
|
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: 52.13 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 178 KLEMDQYKEELSKMEKEIIHLKRDGENKSMQLS---QLDMVLDQTKTELEKTTNSVK-ELERLQHHTETELTETMQKREA 253
Cdd:pfam10174 288 KNKIDQLKQELSKKESELLALQTKLETLTNQNSdckQHIEVLKESLTAKEQRAAILQtEVDALRLRLEEKESFLNKKTKQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 254 LEnELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKyttIKDLTAELReckmeieDKKQELIEmdqaLKERNWELKQRAA 333
Cdd:pfam10174 368 LQ-DLTEEKSTLAGEIRDLKDMLDVKERKINVLQKK---IENLQEQLR-------DKDKQLAG----LKERVKSLQTDSS 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 334 QVTHLDMTIREHRGEMEQKIIKLEgtlEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQ 413
Cdd:pfam10174 433 NTDTALTTLEEALSEKERIIERLK---EQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 414 QRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQE-------------QMQNTHSELVEARRQEVQAQREIERLAGELE 480
Cdd:pfam10174 510 SSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNaeeavrtnpeindRIRLLEQEVARYKEESGKAQAEVERLLGILR 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 481 DIKQLSKEKEAHGNRLaEELGASQVREAHlearMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKwklsAESQKTSVQQL 560
Cdd:pfam10174 590 EVENEKNDKDKKIAEL-ESLTLRQMKEQN----KKVANIKHGQQEMKKKGAQLLEEARRREDNLA----DNSQQLQLEEL 660
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 561 NEQLEKAKQELEEAQDTVSNLHQQVQDRN---------------EVIEAANEALLIKESE 605
Cdd:pfam10174 661 MGALEKTRQELDATKARLSSTQQSLAEKDghltnlraerrkqleEILEMKQEALLAAISE 720
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
24-534 |
2.09e-06 |
|
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: 51.17 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 24 NRGMDTKNVVRQLDSALEICKEELAL----------HLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQ- 92
Cdd:TIGR04523 89 DKLKKNKDKINKLNSDLSKINSEIKNdkeqknklevELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQk 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 93 ----NAILQHTLQQQQQMLQQETMRNGELED--------TQSKLEKQVSKQEQELQKQRESSTEKLRKMEEKYETAIREV 160
Cdd:TIGR04523 169 eeleNELNLLEKEKLNIQKNIDKIKNKLLKLelllsnlkKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 161 DLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQ-----TKTELEKTTNSVKELER 235
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQN 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 236 LQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELI 315
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 316 EMDQALKERNWELKQRAAQVTHLDMTIREHRGEM----------EQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAK 385
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIkdltnqdsvkELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 386 EQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQE 465
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNK 568
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907166662 466 --VQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLEARM---QAEIKKLSSEVDSLKEAYQI 534
Cdd:TIGR04523 569 eiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELekaKKENEKLSSIIKNIKSKKNK 642
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
348-575 |
8.38e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 348 EMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEfimlqneQEISQLKKEIERTQQRMKEMESVIKE-- 425
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-------AEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 426 ---QEDYIATQYKEVIDLGQEL-----RLTQ-EQMQNTHSELVEARRQevqAQREIERLAGELEDIKQLSKEKEAHGNRL 496
Cdd:COG3883 93 ralYRSGGSVSYLDVLLGSESFsdfldRLSAlSKIADADADLLEELKA---DKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907166662 497 AEELGASQVREAHLEARMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQ 575
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
127-484 |
9.01e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 127 QVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQkiIELTGTARQAKLEmdqyKEELSKMEKEIIHLKRDGENKS 206
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRK--LEEAEKARQAEMD----RQAAIYAEQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 207 MQLSQLDMVLDQTKT-ELEKTTNSVKELERLQhhtetelTETMQKREALENELQNAhgelkstlrqlqelrdvlQKAQLS 285
Cdd:pfam17380 353 IRQEERKRELERIRQeEIAMEISRMRELERLQ-------MERQQKNERVRQELEAA------------------RKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 286 LEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWElKQRAAQVTHLDMTIREHRGEMEQKIIKLEgtLEKSEL 365
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREME-RVRLEEQERQQQVERLRQQEEERKRKKLE--LEKEKR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 366 ELKECNKQVESLNEK-LQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEdyiatqykevidlGQEL 444
Cdd:pfam17380 485 DRKRAEEQRRKILEKeLEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE-------------MEER 551
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907166662 445 RLTQEQMQNTHSElvEARRQEVQAQREIERLAGELEDIKQ 484
Cdd:pfam17380 552 RRIQEQMRKATEE--RSRLEAMEREREMMRQIVESEKARA 589
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
431-623 |
9.41e-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: 48.61 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 431 ATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHL 510
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 511 EARMQAEIKKLSSEVDSL---KEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQD 587
Cdd:COG4942 96 RAELEAQKEELAELLRALyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907166662 588 RNEVIEAANEALLIKESELTRLQAKISGHEKTEDTK 623
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
116-606 |
1.50e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 116 ELEDTQSKLEKQVSKQEQELQKQRESSteKLRKMEEKYETAIREVDLKRQKIIELTGTAR----QAKLEMDQYKEELSKM 191
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQLLK--QLRARIEELRAQEAVLEETQERINRARKAAPlaahIKAVTQIEQQAQRIHT 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 192 EKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQ 271
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQK 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 272 LQ---ELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGE 348
Cdd:TIGR00618 395 LQslcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 349 MEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFI---------MLQNEQEISQLKKEIERTQQRMKEM 419
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrMQRGEQTYAQLETSEEDVYHQLTSE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 420 ESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEArRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEE 499
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL-QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 500 LGASQVREAHLEARMQAEIKKLssevdsLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVS 579
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTL------TQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLR 707
|
490 500
....*....|....*....|....*..
gi 1907166662 580 NLHQQVQDRNEVIEAANEALLIKESEL 606
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDL 734
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
348-525 |
1.86e-05 |
|
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: 46.84 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 348 EMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESvikeqe 427
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 428 dyiatqYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAhgnRLAEELGASQVRE 507
Cdd:COG1579 88 ------NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA---ELDEELAELEAEL 158
|
170
....*....|....*...
gi 1907166662 508 AHLEARMQAEIKKLSSEV 525
Cdd:COG1579 159 EELEAEREELAAKIPPEL 176
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
116-593 |
2.25e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 48.12 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 116 ELEDTQSKLEKQVSKQEQ---ELQKQRESSTEKLRKMEEKYETAI----REVDLKRQKIIELTGTARQAKLE-----MDQ 183
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQnknHINNELESKEEQLSSYEDKLFDVCgsqdEESDLERLKEEIEKSSKQRAMLAgatavYSQ 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 184 YKEELSKMEKEIIHL-KRDGENKSmqlsQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAH 262
Cdd:TIGR00606 668 FITQLTDENQSCCPVcQRVFQTEA----ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKE 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 263 GELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKK-QELIEMDQALKERNWELKQRAAQVTHLDMT 341
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTiMERFQMELKDVERKIAQQAAKLQGSDLDRT 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 342 IREHRGEMEQKIIKLEGTLEKSELElkecNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMES 421
Cdd:TIGR00606 824 VQQVNQEKQEKQHELDTVVSKIELN----RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 422 VIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDI--------KQLSKEKEAHG 493
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIenkiqdgkDDYLKQKETEL 979
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 494 NRLAEELGASQVREAHLEARMQAEIKKLSSEvdSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNE----QLEKAKQ 569
Cdd:TIGR00606 980 NTVNAQLEECEKHQEKINEDMRLMRQDIDTQ--KIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQmqvlQMKQEHQ 1057
|
490 500
....*....|....*....|....
gi 1907166662 570 ELEEAQDTVSNLHQQVQDRNEVIE 593
Cdd:TIGR00606 1058 KLEENIDLIKRNHVLALGRQKGYE 1081
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
307-440 |
2.73e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 307 IEDKKQELIEMDQALKERNWELKQRAAQvthldmtirEHRGEMEQKIIKLEGTLEK-----SEL--ELKECNKQVESLNE 379
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKEHEE---------RELTEEEEEIRRLEEQVERleaevEELeaELEEKDERIERLER 448
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907166662 380 KLQNAKEQLREKefimLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIAtQYKEVIDL 440
Cdd:COG2433 449 ELSEARSEERRE----IRKDREISRLDREIERLERELEEERERIEELKRKLE-RLKELWKL 504
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
39-490 |
2.81e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 39 ALEICKEELALHLNQLERNKEKFERQLKKKSEEVYcLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELE 118
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK-KADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE 1422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 119 DTQSKLEKQVSKQEQELQKQRESSTEKLRKMEE--KYETAIREVDLKRqKIIELTGTARQAKlEMDQYKEELSKMEKEII 196
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakKAEEAKKKAEEAK-KADEAKKKAEEAK-KADEAKKKAEEAKKKAD 1500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 197 HLKRDGENKSmQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALEN--------ELQNAHGELKST 268
Cdd:PTZ00121 1501 EAKKAAEAKK-KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKaeekkkaeEAKKAEEDKNMA 1579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 269 LRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDmtirEHRGE 348
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE----ELKKA 1655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 349 MEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEfiMLQNEQEISQLKKEIERTQQRMKEMESVIKEQED 428
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE--EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907166662 429 YIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKE 490
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
243-573 |
2.89e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 243 ELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALK 322
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 323 ERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLR------------- 389
Cdd:pfam07888 122 AQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRslskefqelrnsl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 390 -EKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKE----QEDYIATQYKeVIDLGQELRLTQEQMQNTHSELVEARRQ 464
Cdd:pfam07888 202 aQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslQERLNASERK-VEGLGEELSSMAAQRDRTQAELHQARLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 465 EVQAQREIERLAGEL-EDIKQLSKEKEAhgnrLAEELGASQVREAHLEARMQAEIKKLS---SEVDSLKEAYQIEMISHQ 540
Cdd:pfam07888 281 AAQLTLQLADASLALrEGRARWAQERET----LQQSAEADKDRIEKLSAELQRLEERLQeerMEREKLEVELGREKDCNR 356
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907166662 541 ENHAKWKLSAESQKTSV---QQLNEQLEKAKQELEE 573
Cdd:pfam07888 357 VQLSESRRELQELKASLrvaQKEKEQLQAEKQELLE 392
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
136-507 |
3.24e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 3.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 136 QKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRdgenKSMQLSQLDMV 215
Cdd:PRK04863 347 QEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT----RAIQYQQAVQA 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 216 LDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAhgelKSTLRQLQELRDVLQKA--QLSLEEKYTTI 293
Cdd:PRK04863 423 LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVA----QAAHSQFEQAYQLVRKIagEVSRSEAWDVA 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 294 KDLTAELRECKMeiedkkqeLIEMDQALKERNWELKQRAAQvthlDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQ 373
Cdd:PRK04863 499 RELLRRLREQRH--------LAEQLQQLRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 374 VESLNEKLQNAKEQlrekefiMLQNEQEISQLKKEIERTQQRMKEMesvIKEQE--DYIATQYKEVIDLGQELrltQEQM 451
Cdd:PRK04863 567 LESLSESVSEARER-------RMALRQQLEQLQARIQRLAARAPAW---LAAQDalARLREQSGEEFEDSQDV---TEYM 633
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907166662 452 QNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVRE 507
Cdd:PRK04863 634 QQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFGGVLLSE 689
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
253-426 |
3.55e-05 |
|
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: 46.07 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 253 ALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKE--RNWELKQ 330
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 331 RAAQVTHLdmtiREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREkefimlqneqEISQLKKEIE 410
Cdd:COG1579 94 LQKEIESL----KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE----------ELAELEAELE 159
|
170
....*....|....*.
gi 1907166662 411 RTQQRMKEMESVIKEQ 426
Cdd:COG1579 160 ELEAEREELAAKIPPE 175
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
66-500 |
4.47e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 66 KKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSKLEKQVSKQEQELQKQRE-SSTE 144
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAE 1561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 145 KLRKMEE-KYETAIREVDLKRQKIIELTGTARQAklEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTEL 223
Cdd:PTZ00121 1562 EKKKAEEaKKAEEDKNMALRKAEEAKKAEEARIE--EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 224 EKTTNSVKELERLQHHTETELTETMQKREALENELQNAhgelkstlrqlqelrdvlQKAQLSLEEKYTTIKDLTAELREC 303
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA------------------EEAKKAEEDEKKAAEALKKEAEEA 1701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 304 KMEIEDKKQELIEMDQALKERNWElKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQN 383
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 384 AKEQLREK-EFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLG----QELRLTQEQMQNTHSEL 458
Cdd:PTZ00121 1781 IEEELDEEdEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKnmqlEEADAFEKHKFNKNNEN 1860
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1907166662 459 VEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEEL 500
Cdd:PTZ00121 1861 GEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
126-575 |
5.96e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 126 KQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKME---KEIIHLKRDG 202
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkKAEEKKKADE 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 203 ENKSMQLSQLDMV---------LDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQ 273
Cdd:PTZ00121 1295 AKKAEEKKKADEAkkkaeeakkADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 274 ELRDVLQKAQLSLEEKYttikdlTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIR---------- 343
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKK------KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKkaeeakkade 1448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 344 -----EHRGEMEQKIIKLEGTLEKSELELK-ECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMK 417
Cdd:PTZ00121 1449 akkkaEEAKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 418 EMESVIKEQEDYIATQYKEvidlGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLA 497
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKK----ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166662 498 EELGASQVREAHlEARMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQ 575
Cdd:PTZ00121 1605 KKMKAEEAKKAE-EAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-352 |
1.27e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 141 SSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTK 220
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 221 TELEKTTNSVKELERLQHHTE--------------TELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSL 286
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907166662 287 EEKYTTIKDLTAELREckmEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGEMEQK 352
Cdd:COG4942 177 EALLAELEEERAALEA---LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
295-608 |
1.29e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 295 DLTAELRECKMEIEDKKQELIEMDQALKERNWELK------QRAAQVTHLDMTIREHRGemeqKIIKLEGTLEKSELELK 368
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESdleqdyQAASDHLNLVQTALRQQE----KIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 369 ECNKQVESLNEKLQNAKEQLRekefimlQNEQEISQLKKEIERTQQRMKEMESVikeqedyiATQYKEVIDLGQELR--- 445
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAE-------AAEEEVDELKSQLADYQQALDVQQTR--------AIQYQQAVQALERAKqlc 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 446 ----LTQEQMQNTHSELV---------------------EARRQEVQAQREIERLAGELE--DIKQLSKEKEAHGNR--- 495
Cdd:PRK04863 431 glpdLTADNAEDWLEEFQakeqeateellsleqklsvaqAAHSQFEQAYQLVRKIAGEVSrsEAWDVARELLRRLREqrh 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 496 LAEELGASQVREAHLEARMQAE----------IKKLSSEVD--SLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQ 563
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRLRQQqraerllaefCKRLGKNLDdeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907166662 564 LEKAKQELE-------EAQDTVSNLHQQV---QDRNEVIEAANEALLIKESELTR 608
Cdd:PRK04863 591 LQARIQRLAarapawlAAQDALARLREQSgeeFEDSQDVTEYMQQLLERERELTV 645
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
216-425 |
1.40e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 216 LDQTKTELEKTTNSVKELeRLQH---HTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEkyTT 292
Cdd:COG3206 184 LPELRKELEEAEAALEEF-RQKNglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPE--LL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 293 IKDLTAELREckmEIEDKKQELIEMDQALKERNWELKQRAAQvthldmtIREHRGEMEQKIIKLegtLEKSELELKECNK 372
Cdd:COG3206 261 QSPVIQQLRA---QLAELEAELAELSARYTPNHPDVIALRAQ-------IAALRAQLQQEAQRI---LASLEAELEALQA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907166662 373 QVESLNEKLQNAKEQLREkefiMLQNEQEISQLKKEIERTQQRMKEMESVIKE 425
Cdd:COG3206 328 REASLQAQLAQLEARLAE----LPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
113-388 |
1.53e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 113 RNGELEDTQSKLEKQVSKQEQELQKQRESSTEkLRKMEEKY-----ETAIREVDLKRQKIIEltgtARQAKLEMDQYKEE 187
Cdd:PRK04863 845 RRVELERALADHESQEQQQRSQLEQAKEGLSA-LNRLLPRLnlladETLADRVEEIREQLDE----AEEAKRFVQQHGNA 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 188 LSKMEKEIIHLKRDGEnksmQLSQLDMVLDQTKTELEKTTN---SVKELERLQHH-----------TETELTETMQKR-E 252
Cdd:PRK04863 920 LAQLEPIVSVLQSDPE----QFEQLKQDYQQAQQTQRDAKQqafALTEVVQRRAHfsyedaaemlaKNSDLNEKLRQRlE 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 253 ALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDkkqeliEMDQALKERNWELKQRa 332
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS------GAEERARARRDELHAR- 1068
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907166662 333 aqvthldmtIREHRGEMEQkiikLEGTLEKSELELKECNKQVESLNEKLQNAKEQL 388
Cdd:PRK04863 1069 ---------LSANRSRRNQ----LEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
246-460 |
1.64e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 246 ETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTtikDLTAELRECKMEIEDKKQELIEMDQALKERN 325
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYD---ELVEEAKTIKAEIEELTDELLNLVMDIEDPS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 326 WELKQRAAQVTHLDMTIREHRGEME------------QKIIKLEGTLEKSELELKECNKQVEslneKLQNAKEQLREK-- 391
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQFQKVIKmyekggvcptctQQISEGPDRITKIKDKLKELQHSLE----KLDTAIDELEEImd 330
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907166662 392 EFIMLQNEQ-----EISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTqeqmQNTHSELVE 460
Cdd:PHA02562 331 EFNEQSKKLlelknKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI----VKTKSELVK 400
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
242-515 |
1.76e-04 |
|
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: 45.21 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 242 TELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKD--------LTAELRECKMEIEDKKQE 313
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDqwkekrdeLNGELSAADAAVAKDRSE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 314 LIEMD-QALKERNWELKQRAAQVTHLDmTIREHRGEMEQKIIKLEGTLEKSELELK--------ECNKQVESLNEKLQNA 384
Cdd:pfam12128 324 LEALEdQHGAFLDADIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNrrrskikeQNNRDIAGIKDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 385 KEQL-REKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELrltqEQMQNTHSELVEARR 463
Cdd:pfam12128 403 REARdRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELL----LQLENFDERIERARE 478
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1907166662 464 QEVQAQREIERLAGELEDIKQLSKEKEAHGNRlaEELGASQVREAHLEARMQ 515
Cdd:pfam12128 479 EQEAANAEVERLQSELRQARKRRDQASEALRQ--ASRRLEERQSALDELELQ 528
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
82-430 |
1.78e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 82 KTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSKLeKQVSKQEQELQKQRESSTEKLRKM---EEKYETAIR 158
Cdd:PLN02939 95 DDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMI-QNAEKNILLLNQARLQALEDLEKIlteKEALQGKIN 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 159 EVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHlkrDGENKSMQLSQLDMVLDQTKTELEKTTNSVKEL-ERLQ 237
Cdd:PLN02939 174 ILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLI---RGATEGLCVHSLSKELDVLKEENMLLKDDIQFLkAELI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 238 HHTETEltETMQKREALENELQNAHGELKSTLRQLQElrDVLQKAQLSLeekyttikdltaelrECKMEIEDKKQELiem 317
Cdd:PLN02939 251 EVAETE--ERVFKLEKERSLLDASLRELESKFIVAQE--DVSKLSPLQY---------------DCWWEKVENLQDL--- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 318 dqalkernweLKQRAAQVTHLDMTIREHRgEMEQKIIKLEGTLEKSELElKECNKQVESLNEKLQNAKEQLREKEFIMLQ 397
Cdd:PLN02939 309 ----------LDRATNQVEKAALVLDQNQ-DLRDKVDKLEASLKEANVS-KFSSYKVELLQQKLKLLEERLQASDHEIHS 376
|
330 340 350
....*....|....*....|....*....|...
gi 1907166662 398 NEQEISQLKKEIERTQQRMKEmESVIKEQEDYI 430
Cdd:PLN02939 377 YIQLYQESIKEFQDTLSKLKE-ESKKRSLEHPA 408
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
182-423 |
1.87e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 182 DQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQ-TKTELEKTTNSVKELERLQHH------TETELTETMQKREAL 254
Cdd:PRK01156 472 NHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYlESEEINKSINEYNKIESARADledikiKINELKDKHDKYEEI 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 255 ENELQNAH-GELKSTLRQLQELRDV-----LQKAQLSLEEKYTTIKDLTAELRECKMEIEDKK-------QELIEMDQAL 321
Cdd:PRK01156 552 KNRYKSLKlEDLDSKRTSWLNALAVislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksiREIENEANNL 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 322 KERNWELKQRAAQVTHLDMTIREHRGEMEQK--IIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNE 399
Cdd:PRK01156 632 NNKYNEIQENKILIEKLRGKIDNYKKQIAEIdsIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRI 711
|
250 260
....*....|....*....|....
gi 1907166662 400 QEISQLKKEIERTQQRMKEMESVI 423
Cdd:PRK01156 712 NELSDRINDINETLESMKKIKKAI 735
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
116-535 |
2.26e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 116 ELEDTQSKLEKQVSKQEQ-------------ELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQA-KLEM 181
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKAleedlqiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRlEKNE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 182 DQYK---EELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHhTETELTETMQKREA----L 254
Cdd:pfam05483 377 DQLKiitMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKG-KEQELIFLLQAREKeihdL 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 255 ENELQNAHGELKSTLRQLQELRDVLQKAQL------------SLEEKYTT--IKDLTAELRECKMEIEDKKQELIEMDQA 320
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLknieltahcdklLLENKELTqeASDMTLELKKHQEDIINCKKQEERMLKQ 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 321 LKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQ 400
Cdd:pfam05483 536 IENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 401 EISQLKKEIERTQQRMKEMESVIKEQEDYIAT---QYKEVIDLGQ-ELRLTQEQMQNTHSELVEAR---RQEVQAQREIE 473
Cdd:pfam05483 616 ENKALKKKGSAENKQLNAYEIKVNKLELELASakqKFEEIIDNYQkEIEDKKISEEKLLEEVEKAKaiaDEAVKLQKEID 695
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 474 -RLAGELEDIKQLSKEKEAHGNRLAE----ELGASQVRE---AHLEARMQAEIKKLSSEVDSLKEAYQIE 535
Cdd:pfam05483 696 kRCQHKIAEMVALMEKHKHQYDKIIEerdsELGLYKNKEqeqSSAKAALEIELSNIKAELLSLKKQLEIE 765
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
155-480 |
2.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 155 TAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGEnksMQLSQLDMV--------LDQTKTELEKT 226
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE---YSWDEIDVAsaereiaeLEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 227 TNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTikDLTAELREckmE 306
Cdd:COG4913 684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAA---A 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 307 IEDKKQEliEMDQALKERNWELKQRAAQ-VTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVES-LNEKLQNA 384
Cdd:COG4913 759 LGDAVER--ELRENLEERIDALRARLNRaEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDgLPEYEERF 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 385 KEQLREkefimlQNEQEI----SQLKKEIERTQQRMKEMESVIKE----QEDYI-----ATQYKEVIDLGQELRLTQEQM 451
Cdd:COG4913 837 KELLNE------NSIEFVadllSKLRRAIREIKERIDPLNDSLKRipfgPGRYLrlearPRPDPEVREFRQELRAVTSGA 910
|
330 340
....*....|....*....|....*....
gi 1907166662 452 QNTHSELVEARRQEVqaQREIERLAGELE 480
Cdd:COG4913 911 SLFDEELSEARFAAL--KRLIERLRSEEE 937
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
132-622 |
2.43e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 132 EQELQKQRESsTEKLRKMEEKYETAIR-EVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLS 210
Cdd:COG4913 241 HEALEDAREQ-IELLEPIRELAERYAAaRERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 211 QLDMVLDQTKTELEKT-TNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEK 289
Cdd:COG4913 320 ALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 290 YTTIKD----LTAELRECKMEIEDKKQELiemdQALKERNWELKQRAAQVthldmtirehRGEMEQKIiklegTLEKSEL 365
Cdd:COG4913 400 LEALEEalaeAEAALRDLRRELRELEAEI----ASLERRKSNIPARLLAL----------RDALAEAL-----GLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 366 ----ELKecnkQVESLNEKLQNAKEQ-LREKEFIMLQNEQEISQLKKEIERTQQRMK----------------------- 417
Cdd:COG4913 461 pfvgELI----EVRPEEERWRGAIERvLGGFALTLLVPPEHYAAALRWVNRLHLRGRlvyervrtglpdperprldpdsl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 418 --EMESVIKEQEDYIATQYKEVIDL-----GQELR-----LTQE-QMQNTH------------SELV---EARRQEVQAQ 469
Cdd:COG4913 537 agKLDFKPHPFRAWLEAELGRRFDYvcvdsPEELRrhpraITRAgQVKGNGtrhekddrrrirSRYVlgfDNRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 470 REIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREAHLEArmqaeikklssEVDSLKEAYQIEmishqenhakwklS 549
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD-----------EIDVASAEREIA-------------E 672
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907166662 550 AESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQAKISGHEKTEDT 622
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
|
| CHD5 |
pfam04420 |
CHD5-like protein; Members of this family are probably coiled-coil proteins that are similar ... |
516-579 |
3.03e-04 |
|
CHD5-like protein; Members of this family are probably coiled-coil proteins that are similar to the CHD5 (Congenital heart disease 5) protein. In Saccharomyces cerevisiae this protein localizes to the ER and is thought to play a homeostatic role.
Pssm-ID: 427938 Cd Length: 158 Bit Score: 41.79 E-value: 3.03e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907166662 516 AEIKKLSSEVDSLKEayqiEM--ISHQENHAKW-KLsaesqKTSVQQLNEQLEKAKQELEEAQDTVS 579
Cdd:pfam04420 38 KEQRKLKAEILKLKE----ELnaTSAQDEFAKWaKL-----NRKHDKLLEELEKLKKSLSSAKSSFD 95
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
115-415 |
3.12e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 115 GELEDTQSKLEKQVSKQEqELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTA---RQAK--LE--------- 180
Cdd:PRK04863 355 ADLEELEERLEEQNEVVE-EADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAiqyQQAVqaLErakqlcglp 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 181 ------MDQYKEELSKMEKEIIHLKRDGENKsmqLSQLDMVLDQTKTELEKTTNSVKELERLQ-HHTETELTETMQKREA 253
Cdd:PRK04863 434 dltadnAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAAHSQFEQAYQLVRKIAGEVSRSEaWDVARELLRRLREQRH 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 254 L---ENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQ 330
Cdd:PRK04863 511 LaeqLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 331 RAAQVTHLDMTirehrgemEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIE 410
Cdd:PRK04863 591 LQARIQRLAAR--------APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
....*
gi 1907166662 411 RTQQR 415
Cdd:PRK04863 663 RLSQP 667
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
47-466 |
3.27e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 47 LALHLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSKLEK 126
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 127 QVS-----KQEQELQKQRESSTEKLRKMEEKYEtairEVDLKRQKIIELTGTARQAKLEMDQYKEELS-KMEKEIIHLKR 200
Cdd:COG4717 124 LLQllplyQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 201 DGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETE------------------------------------- 243
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallallglggsllsliltiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 244 ----------LTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQE 313
Cdd:COG4717 280 flvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 314 LIEMDQALKERNWELKQRAAQVTHLDMtiREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQ--NAKEQLREK 391
Cdd:COG4717 360 EEELQLEELEQEIAALLAEAGVEDEEE--LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 392 EFIMLQNEQEISQLKKEIERTQQRMKEME-----SVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEV 466
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEedgelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPV 517
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
349-671 |
3.92e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 349 MEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQED 428
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 429 YIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASQVREA 508
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 509 HLEARMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDR 588
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 589 NEVIEAANEALLIKESELTRLQAKISGHEKTEDTKYLPAPFTTLTEIIPDSQHPNFAKHSQISLFKCRKLRRSISASDLS 668
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
...
gi 1907166662 669 FKS 671
Cdd:COG4372 349 GLL 351
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
116-599 |
3.99e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 116 ELEDTQSKLEKQVSKQEQELQKQRESSTEKLRKMEEK---YETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKME 192
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 193 --KEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLR 270
Cdd:COG4717 130 lyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 271 QLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKmEIEDKKQELIEMDQ--ALKERNWELKQRAAQVTHLDMTIREHRGE 348
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 349 MEQKIIKLEGTLEKSELELKECNKQVESLNEKLQnakEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEqed 428
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELE---ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--- 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 429 yiatqykevIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQlskekeahgnRLAEELGASQVR-E 507
Cdd:COG4717 363 ---------LQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEE----------QLEELLGELEELlE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 508 AHLEARMQAEIKKLSSEVDSLKEayQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEE----------AQDT 577
Cdd:COG4717 424 ALDEEELEEELEELEEELEELEE--ELEELREELAELEAELEQLEEDGELAELLQELEELKAELRElaeewaalklALEL 501
|
490 500
....*....|....*....|....
gi 1907166662 578 VSNLHQQVQDRN--EVIEAANEAL 599
Cdd:COG4717 502 LEEAREEYREERlpPVLERASEYF 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
36-321 |
4.09e-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: 43.90 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 36 LDSALEICKEELAL---HLNQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETM 112
Cdd:TIGR02169 686 LKRELSSLQSELRRienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 113 RNGELEDTQSKLEKQVSKQEQELqkqRESSTEKLRKMEEKYETAIREVDLKRQKIieltgtarQAKLEMDQYKEELskME 192
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDLEARL---SHSRIPEIQAELSKLEEEVSRIEARLREI--------EQKLNRLTLEKEY--LE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 193 KEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALEN---ELQNAHGELKSTL 269
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAqlrELERKIEELEAQI 912
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907166662 270 RQLQELRDVLQKAQLSLEEKYTTIKDLTAELRE---CKMEIEDKKQELIEMDQAL 321
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEEEI 967
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
123-323 |
4.83e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 123 KLEKQVSKQEQELQKQRESSteKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDG 202
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKN--GLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 203 ENKSM--QLSQLDMVLDQTKTELEKTTNSVKELERlqhhtetELTETmqkREALENELQNAHGELKSTLRQLQELRDVLQ 280
Cdd:COG3206 264 VIQQLraQLAELEAELAELSARYTPNHPDVIALRA-------QIAAL---RAQLQQEAQRILASLEAELEALQAREASLQ 333
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907166662 281 KAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKE 323
Cdd:COG3206 334 AQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
246-577 |
5.00e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 246 ETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERN 325
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 326 WELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLqnakeqlrekefimLQNEQEISQL 405
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDI--------------LLLEDQNSKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 406 KKEIERTQQRMKEMESVIKEQEdyiatqykEVIDLGQELRLTQEQMQnthSELVEARRQEVQAQREIE----RLAGELED 481
Cdd:pfam01576 151 SKERKLLEERISEFTSNLAEEE--------EKAKSLSKLKNKHEAMI---SDLEERLKKEEKGRQELEkakrKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 482 IKQLSKEKEAHGNRLAEELGASQVREAHLEARMQAEIKKLSSEVDSLKEAyQIEMISHQENHAKWKLSAESQKTSVQQLN 561
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL-EAQISELQEDLESERAARNKAEKQRRDLG 298
|
330
....*....|....*.
gi 1907166662 562 EQLEKAKQELEEAQDT 577
Cdd:pfam01576 299 EELEALKTELEDTLDT 314
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
13-302 |
5.06e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 13 SQKLERTQMPLNRGMDTKNVVRQLDSALEICKEELALHLNQLERNKEKFERQLKKKSEEVYCLQKE---LKIKTHNLEET 89
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltlLNEEAANLRER 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 90 --SEQNAILQHTLQQQQQMLQQETMR------NGELEDTQSKLEKQvSKQEQELQKQRESSTEKLRKMEEKYETAIREVD 161
Cdd:TIGR02168 826 leSLERRIAATERRLEDLEEQIEELSedieslAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 162 LKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLkrdgenKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTE 241
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907166662 242 TELTETMQKREALENELQnahgELKSTLRQLQELRDVLQKAQLSLEEkytTIKDLTAELRE 302
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEYE----ELKERYDFLTAQKEDLTEAKETLEE---AIEEIDREARE 1032
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
408-594 |
6.32e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 408 EIERTQQRMKEMESVIKEQEDYIATQYkevidlgqeLRLTQEQmqNTHSELVEARRQEVQAQREierlageledikQLSK 487
Cdd:COG3096 247 AIRVTQSDRDLFKHLITEATNYVAADY---------MRHANER--RELSERALELRRELFGARR------------QLAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 488 EKEAHgNRLAEELGASQVREAHLEARMQAEIKKLSSEVDSLKEAYQIEMisHQENHAKWKLSAESQKTSVQQLNEQLEKA 567
Cdd:COG3096 304 EQYRL-VEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQEKIER--YQEDLEELTERLEEQEEVVEEAAEQLAEA 380
|
170 180
....*....|....*....|....*..
gi 1907166662 568 KQELEEAQDTVSNLHQQVQDRNEVIEA 594
Cdd:COG3096 381 EARLEAAEEEVDSLKSQLADYQQALDV 407
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
246-487 |
6.57e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 246 ETMQKREALENELQNAHGELKSTLRQLQELRDVLQKaqlsLEEKYTTIKDLTAELRECKMEIED-KKQELIEMDQAL-KE 323
Cdd:PRK11281 46 DALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEE----TEQLKQQLAQAPAKLRQAQAELEAlKDDNDEETRETLsTL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 324 RNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQN---AKEQLREKEFIMLQNEQ 400
Cdd:PRK11281 122 SLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGgkvGGKALRPSQRVLLQAEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 401 -----EISQLKKEIERTQQrmkeMESVIKEQEDYIATQYKEvidLGQELRLTQEQMQNTHSELVEARRQEVQAQREIER- 474
Cdd:PRK11281 202 allnaQNDLQRKSLEGNTQ----LQDLLQKQRDYLTARIQR---LEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAARi 274
|
250
....*....|....*...
gi 1907166662 475 -----LAGELEDIKQLSK 487
Cdd:PRK11281 275 qanplVAQELEINLQLSQ 292
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
117-358 |
7.17e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 117 LEDTQSKLEKQVSKQEQELQKQRESSTEKLRKMEEKYETAIREvdlkrqkiieltgtARQAKLEMDQYKEELSKMEKEIi 196
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEE--------------AKTIKAEIEELTDELLNLVMDI- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 197 hlkrdgENKSMQLSQLDMVLDQTKTELEKTTNSVKelerlQHHTETELTETMQKREALENELQNAHGELKstlrQLQELR 276
Cdd:PHA02562 251 ------EDPSAALNKLNTAAAKIKSKIEQFQKVIK-----MYEKGGVCPTCTQQISEGPDRITKIKDKLK----ELQHSL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 277 DVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKL 356
Cdd:PHA02562 316 EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
..
gi 1907166662 357 EG 358
Cdd:PHA02562 396 SE 397
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
243-611 |
7.62e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 243 ELTETMQKREALENELQNAHGEL---KSTLRQ----------LQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIED 309
Cdd:COG3096 314 ELEELSARESDLEQDYQAASDHLnlvQTALRQqekieryqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 310 KKQELIEMDQALKErnweLKQRAAQVthldmtirehrgemeQKIIKlegTLEKSELELKECNKQVESLNEKLQNAKEQLR 389
Cdd:COG3096 394 LKSQLADYQQALDV----QQTRAIQY---------------QQAVQ---ALEKARALCGLPDLTPENAEDYLAAFRAKEQ 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 390 EKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQY-KEVIDLGQELRLTQEQMQNTHSELVEARRQEVQa 468
Cdd:COG3096 452 QATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTaRELLRRYRSQQALAQRLQQLRAQLAELEQRLRQ- 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 469 QREIERLAGELedIKQLSKEKEAhgnrlAEELgasqvreAHLEARMQAEIKKLSSEVDSLKEAyQIEMISHQENHA---- 544
Cdd:COG3096 531 QQNAERLLEEF--CQRIGQQLDA-----AEEL-------EELLAELEAQLEELEEQAAEAVEQ-RSELRQQLEQLRarik 595
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907166662 545 -------KWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEvIEAANEALlikESELTRLQA 611
Cdd:COG3096 596 elaarapAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDE-LAARKQAL---ESQIERLSQ 665
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
39-420 |
8.39e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 8.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 39 ALEICKEELALHLNQLERNKEKFERQLKKKSeevycLQKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELE 118
Cdd:COG4717 106 ELEAELEELREELEKLEKLLQLLPLYQELEA-----LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 119 DTQSKLEKQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHL 198
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 199 KRDGENKSMQLSQ---------------LDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHG 263
Cdd:COG4717 261 LLGLGGSLLSLILtiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 264 ELKSTLRQLQELRDVLQKAQLSLEEKYtTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIR 343
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLEE-LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907166662 344 EHRGEMEQKIIKLEgtLEKSELELKECNKQVESLNEKLQNAKEQLREkefimLQNEQEISQLKKEIERTQQRMKEME 420
Cdd:COG4717 420 ELLEALDEEELEEE--LEELEEELEELEEELEELREELAELEAELEQ-----LEEDGELAELLQELEELKAELRELA 489
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
86-491 |
8.83e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 86 LEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSKLEKQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDlkrq 165
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 166 kiieltgtarqaklEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMvldQTKTELEKTTNSVKELERLQHHTETElt 245
Cdd:pfam07888 112 --------------ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVL---ERETELERMKERAKKAGAQRKEEEAE-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 246 etmqkREALENELQNAHGELKSTLRQLQELRDvlqkaqlSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERN 325
Cdd:pfam07888 173 -----RKQLQAKLQQTEEELRSLSKEFQELRN-------SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 326 wELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQeisQL 405
Cdd:pfam07888 241 -SLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAE---AD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 406 KKEIERTQQRMKEMESVIKEQEdyiATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQL 485
Cdd:pfam07888 317 KDRIEKLSAELQRLEERLQEER---MEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEY 393
|
....*.
gi 1907166662 486 SKEKEA 491
Cdd:pfam07888 394 IRQLEQ 399
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
374-500 |
1.17e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 374 VESLNEKLQNAKEQLREKEFIMLQNE-----QEISQLKKEIERTQQRMKEMESVIKEQEDYIAtqykeviDLGQELRLTQ 448
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERElteeeEEIRRLEEQVERLEAEVEELEAELEEKDERIE-------RLERELSEAR 454
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907166662 449 EQmqnthselveaRRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEEL 500
Cdd:COG2433 455 SE-----------ERREIRKDREISRLDREIERLERELEEERERIEELKRKL 495
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
280-445 |
1.17e-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: 41.45 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 280 QKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQraaqvthldmtIREHRGEMEQKIIKLEGT 359
Cdd:COG1579 6 LRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-----------LEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 360 LEKSELELKEC--NKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEV 437
Cdd:COG1579 75 IKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
....*...
gi 1907166662 438 IDLGQELR 445
Cdd:COG1579 155 EAELEELE 162
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
243-574 |
1.20e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 243 ELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALK 322
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 323 ERNWELKQRAAQVTHLD---MTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNE 399
Cdd:COG4372 112 ELQEELEELQKERQDLEqqrKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 400 QEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGEL 479
Cdd:COG4372 192 ANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 480 EDIKQLSKEKEAHGNRLAEELGASQVREAHLEARMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQ 559
Cdd:COG4372 272 DTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLL 351
|
330
....*....|....*
gi 1907166662 560 LNEQLEKAKQELEEA 574
Cdd:COG4372 352 DNDVLELLSKGAEAG 366
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
348-427 |
1.27e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 348 EMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEfimlqnEQEISQLKKEIERTQQRMKEME----SVI 423
Cdd:PRK00409 531 ELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA------QQAIKEAKKEADEIIKELRQLQkggyASV 604
|
....
gi 1907166662 424 KEQE 427
Cdd:PRK00409 605 KAHE 608
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
182-598 |
1.39e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.94 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 182 DQYKEELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVK--ELERLQHHTETELT----ETMQK----- 250
Cdd:pfam05701 38 KLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLEraQTEEAQAKQDSELAklrvEEMEQgiade 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 251 -REALENELQNAHGELKSTLRQLQELR---DVLQKAQLSL-EEKYTTIK---DLTAELRECKMEIEDKKQELIEMDQALK 322
Cdd:pfam05701 118 aSVAAKAQLEVAKARHAAAVAELKSVKeelESLRKEYASLvSERDIAIKraeEAVSASKEIEKTVEELTIELIATKESLE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 323 ernwelkqrAAQVTHLDMTIREHRGEM--EQKIIKLEGTLEKSELELKECNKQVESLNE----------KLQNAKEQLRE 390
Cdd:pfam05701 198 ---------SAHAAHLEAEEHRIGAALarEQDKLNWEKELKQAEEELQRLNQQLLSAKDlkskletasaLLLDLKAELAA 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 391 KEFIMLQNEQEISQLKKEIERTQQRMkeMESVIKEQEDYIATQYK---EVIDLGQELRLTQEQMQNTHSELVEARRQEVQ 467
Cdd:pfam05701 269 YMESKLKEEADGEGNEKKTSTSIQAA--LASAKKELEEVKANIEKakdEVNCLRVAAASLRSELEKEKAELASLRQREGM 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 468 AQREIERLAGELedikqlskekeahgNRLAEELGASQVREAHLEARMqAEIKKLssevdsLKEAYQiemishqenhakwk 547
Cdd:pfam05701 347 ASIAVSSLEAEL--------------NRTKSEIALVQAKEKEAREKM-VELPKQ------LQQAAQ-------------- 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1907166662 548 lSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANEA 598
Cdd:pfam05701 392 -EAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKAS 441
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
58-348 |
1.43e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 58 KEKFERQLKKKSEEVyclqKELKIKTHNLEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSKLEKQVSKQE---QE 134
Cdd:COG2433 349 KNKFERVEKKVPPDV----DRDEVKARVIRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEeqvER 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 135 LQKQRESSTEKLRKMEEKYETAIREVDLKRQKiieltgtaRQAKLEMDqykEELSKMEKEIIHLKRdgenksmQLSQLDM 214
Cdd:COG2433 425 LEAEVEELEAELEEKDERIERLERELSEARSE--------ERREIRKD---REISRLDREIERLER-------ELEEERE 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 215 VLDQTKTELEKTTN-----------SVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQEL--RDVLQK 281
Cdd:COG2433 487 RIEELKRKLERLKElwklehsgelvPVKVVEKFTKEAIRRLEEEYGLKEGDVVYLRDASGAGRSTAELLAEAgpRAVIVP 566
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907166662 282 AQLSlEEKYTTIKDLT-AELRECKMEIEDK------KQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGE 348
Cdd:COG2433 567 GELS-EAADEVLFEEGiPVLPAEDVTIQEVddlavvDEEELEAAIEDWEERAEERRREKKAEMLERLISEYRAE 639
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
399-612 |
1.46e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 399 EQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGE 478
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 479 LedikqlsKEKEAHGNRLAEELGASQVREA--------HLEARMQAEIKKLSSEVDSLKEAyqiemishqenhakwKLSA 550
Cdd:COG3883 95 L-------YRSGGSVSYLDVLLGSESFSDFldrlsalsKIADADADLLEELKADKAELEAK---------------KAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907166662 551 ESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQAK 612
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
220-335 |
1.64e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 220 KTELEKTTNSVKELERlqhhtetELTETMQKREALENELQNAHGELKSTLR-QLQELRDVLQKaqlsLEEKYTTIKDLTA 298
Cdd:COG0542 403 RMEIDSKPEELDELER-------RLEQLEIEKEALKKEQDEASFERLAELRdELAELEEELEA----LKARWEAEKELIE 471
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907166662 299 ELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQV 335
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
455-587 |
1.97e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 455 HSELVEARRQEVQAQReierlagelediKQLSKEKEAHgNRLAEELGASQVREAHLEARMQAEIKKLSSEVDSLKEAYQI 534
Cdd:PRK04863 284 HLEEALELRRELYTSR------------RQLAAEQYRL-VEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI 350
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907166662 535 EMisHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNLHQQVQD 587
Cdd:PRK04863 351 ER--YQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLAD 401
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
208-570 |
2.69e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.82 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 208 QLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLE 287
Cdd:pfam19220 28 DFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 288 EKYTTIKDLTAELRECKMEIED---KKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSE 364
Cdd:pfam19220 108 ELRIELRDKTAQAEALERQLAAeteQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 365 LELKECNKQVESLNEKLQNAKEQLREKE--FIMLQNEQE--ISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDL 440
Cdd:pfam19220 188 AELAELTRRLAELETQLDATRARLRALEgqLAAEQAEREraEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 441 GQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEdikqlskekeahgnRLAEELGASQVREAHLEARMQAEIKK 520
Cdd:pfam19220 268 RNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLE--------------RRTQQFQEMQRARAELEERAEMLTKA 333
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1907166662 521 LSSEVDSLKEAY-QIEMISHQENHAKWKLSAESQ--KTSVQQLNEQLEKAKQE 570
Cdd:pfam19220 334 LAAKDAALERAEeRIASLSDRIAELTKRFEVERAalEQANRRLKEELQRERAE 386
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
342-613 |
3.34e-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: 41.11 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 342 IREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMES 421
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 422 VIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEarrqEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELG 501
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKE----EEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 502 ASQVREAHLEARMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLNEQLEKAKQELEEAQDTVSNL 581
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
250 260 270
....*....|....*....|....*....|..
gi 1907166662 582 HQQVQDRNEVIEAANEALLIKESELTRLQAKI 613
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEK 425
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
219-431 |
3.46e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.78 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 219 TKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQnahGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTA 298
Cdd:pfam05667 301 THTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQ---EQLEDLESSIQELEKEIKKLESSIKQVEEELEELKE 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 299 ELRECKMEIEDKKQELIEMDQA---LKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVE 375
Cdd:pfam05667 378 QNEELEKQYKVKKKTLDLLPDAeenIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIK 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907166662 376 SLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQ--QRMKEMESVIKEQEDYIA 431
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSAytRRILEIVKNIKKQKEEIT 515
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
123-499 |
3.83e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 123 KLEKQVSKQEQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDG 202
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 203 ENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKA 282
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 283 QLSLEEkyttikdltAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEK 362
Cdd:COG4372 163 QEELAA---------LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 363 SELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLGQ 442
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907166662 443 ELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEE 499
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
52-425 |
3.84e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 52 NQLERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNAILQHTLQQQQQmlqqetmrngELEDTQSKLEKQvSKQ 131
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLES----------QINDLESKIQNQ-EKL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 132 EQELQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQ 211
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 212 LDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEekyt 291
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKE---- 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 292 tikdltaelrecKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEKSELElkecN 371
Cdd:TIGR04523 563 ------------IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE----N 626
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1907166662 372 KQVESLNEKLQNAKEQLrekefimlqnEQEISQLKKEIERTQQRMKEMESVIKE 425
Cdd:TIGR04523 627 EKLSSIIKNIKSKKNKL----------KQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
113-388 |
5.59e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 113 RNGELEDTQSKLEKQVSKQEQELQKQREsSTEKLRKM--------EEKYETAIREVDLKRQKiieltgtARQAKLEMDQY 184
Cdd:COG3096 844 RRSELERELAQHRAQEQQLRQQLDQLKE-QLQLLNKLlpqanllaDETLADRLEELREELDA-------AQEAQAFIQQH 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 185 KEELSKMEKEIIHLKRD---GENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETE-LTETMQKREALENELQN 260
Cdd:COG3096 916 GKALAQLEPLVAVLQSDpeqFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGlLGENSDLNEKLRARLEQ 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 261 AHGELKSTLRQLQELRD-------VLQKAQLSLEEKYTTIKDLTAELRECKMEIEDkkqeliEMDQALKERNWELKQRAA 333
Cdd:COG3096 996 AEEARREAREQLRQAQAqysqynqVLASLKSSRDAKQQTLQELEQELEELGVQADA------EAEERARIRRDELHEELS 1069
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907166662 334 QvthldmtireHRGEMEQkiikLEGTLEKSELELKECNKQVESLNEKLQNAKEQL 388
Cdd:COG3096 1070 Q----------NRSRRSQ----LEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
226-437 |
5.88e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 226 TTNSVKE--LERLQHHTETELTEtmqKREALENE-LQNAHGELKSTLRQLQELRDVLQKAQLSLEE----KYTTIKDLTA 298
Cdd:PRK05771 13 TLKSYKDevLEALHELGVVHIED---LKEELSNErLRKLRSLLTKLSEALDKLRSYLPKLNPLREEkkkvSVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 299 ELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQV---THLDMTIREHRGEM----------EQKIIKLEGTLEKSEL 365
Cdd:PRK05771 90 DVEEELEKIEKEIKELEEEISELENEIKELEQEIERLepwGNFDLDLSLLLGFKyvsvfvgtvpEDKLEELKLESDVENV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 366 ELKECNKQ-----VESLNEKLQNAKEQLREKEF-------------IMLQNEQEISQLKKEIERTQqrmKEMESVIKEQE 427
Cdd:PRK05771 170 EYISTDKGyvyvvVVVLKELSDEVEEELKKLGFerleleeegtpseLIREIKEELEEIEKERESLL---EELKELAKKYL 246
|
250
....*....|
gi 1907166662 428 DYIATQYKEV 437
Cdd:PRK05771 247 EELLALYEYL 256
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
239-415 |
5.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 239 HTETELTETMQKREALENELQNAHGELKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMD 318
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 319 QALKERNW------------------------------------ELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLEK 362
Cdd:COG3883 93 RALYRSGGsvsyldvllgsesfsdfldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907166662 363 SELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQR 415
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
187-336 |
6.12e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 187 ELSKMEKEIIHLKRDGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENELQNAHG--E 264
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907166662 265 LKSTLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVT 336
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
274-596 |
6.52e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 274 ELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKqraaqvthlDMTIREHRGEMEQKI 353
Cdd:pfam06160 176 EAREVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALE---------HLNVDKEIQQLEEQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 354 IKLEGTLEksELELKECNKQVESLNEKLQNAKEQLrEKEFIMLQN-EQEISQLKKEIERTQQRMKEMESVIKE-QEDYIA 431
Cdd:pfam06160 247 EENLALLE--NLELDEAEEALEEIEERIDQLYDLL-EKEVDAKKYvEKNLPEIEDYLEHAEEQNKELKEELERvQQSYTL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 432 TQYKEVIDLGQELRLtqEQMQNTHSELVEARRQEVQAQREI-ERLAGELEDIKQLSKEKEAHGNRLAeelgasQVREAHL 510
Cdd:pfam06160 324 NENELERVRGLEKQL--EELEKRYDEIVERLEEKEVAYSELqEELEEILEQLEEIEEEQEEFKESLQ------SLRKDEL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 511 EARMQ-AEIKKLSSEVDSLKEAYQIEMISHQENHAKWKLSAEsqktsVQQLNEQLEKAK-------QELEEAQDTVSNLH 582
Cdd:pfam06160 396 EAREKlDEFKLELREIKRLVEKSNLPGLPESYLDYFFDVSDE-----IEDLADELNEVPlnmdevnRLLDEAQDDVDTLY 470
|
330
....*....|....
gi 1907166662 583 QQVqdrNEVIEAAN 596
Cdd:pfam06160 471 EKT---EELIDNAT 481
|
|
| V_ATPase_I |
pfam01496 |
V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase ... |
220-283 |
6.76e-03 |
|
V-type ATPase 116kDa subunit family; This family consists of the 116kDa V-type ATPase (vacuolar (H+)-ATPases) subunits, as well as V-type ATP synthase subunit i. The V-type ATPases family are proton pumps that acidify intracellular compartments in eukaryotic cells for example yeast central vacuoles, clathrin-coated and synaptic vesicles. They have important roles in membrane trafficking processes. The 116kDa subunit (subunit a) in the V-type ATPase is part of the V0 functional domain responsible for proton transport. The a subunit is a transmembrane glycoprotein with multiple putative transmembrane helices it has a hydrophilic amino terminal and a hydrophobic carboxy terminal. It has roles in proton transport and assembly of the V-type ATPase complex. This subunit is encoded by two homologous gene in yeast VPH1 and STV1.
Pssm-ID: 460232 [Multi-domain] Cd Length: 748 Bit Score: 39.77 E-value: 6.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907166662 220 KTELEKTTNSV----KELERLQHHTETELTETMQKREALENEL--QNAHGE-LKSTLRQLQELRDVLQKAQ 283
Cdd:pfam01496 43 EEEIEKLDIIPikdtLDLETPEAPSPREIDELEEKLEKLENELreLNENYEtLKRNYNELTELRHVLRKAQ 113
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
167-232 |
6.90e-03 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 39.69 E-value: 6.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907166662 167 IIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGENKSMQLSQLDmVLDQTKTELEKTTNSVKE 232
Cdd:PLN02678 35 VIALDKEWRQRQFELDSLRKEFNKLNKEVAKLKIAKEDATELIAETK-ELKKEITEKEAEVQEAKA 99
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
375-618 |
7.00e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 375 ESLNEKLQNAKEQLREKEFIMLQNEQ---EISQLKKEIERTQQRMKEME---SVIKEQEDYIATQYKEVIDLGQE----- 443
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEkarEVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELERIRQEerkre 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 444 -LRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDI-KQLSKEKEAHGNRLAEELGASQVREAHLEARmQAEIKKL 521
Cdd:pfam17380 362 lERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAArKVKILEEERQRKIQQQKVEMEQIRAEQEEAR-QREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 522 SSEVDSLKEAYQIEMISHQENHAKWKLSAESQKTSVQQLnEQLEKAKQELEEAQDTVsnLHQQVQDRNEVIEAANEALLI 601
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQRRKI--LEKELEERKQAMIEEERKRKL 517
|
250
....*....|....*..
gi 1907166662 602 KESELTRLQAKISGHEK 618
Cdd:pfam17380 518 LEKEMEERQKAIYEEER 534
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
122-610 |
7.36e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 39.73 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 122 SKLEKQVSKQEQELQK-QRESSTEKLRKMEEKYETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKR 200
Cdd:pfam07111 62 SQQAELISRQLQELRRlEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 201 DGENKSMQLSQLDMVLDQTKTELEKTTNSVKELERLQHHTET-------ELTETMQKREALENELQNAHGELKSTLRQLQ 273
Cdd:pfam07111 142 LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETkrageakQLAEAQKEAELLRKQLSKTQEELEAQVTLVE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 274 ELRDVL----------QKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQRAAQVTHLD---- 339
Cdd:pfam07111 222 SLRKYVgeqvppevhsQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEpefp 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 340 MTIREHRGEMEQKIIKLEGTLEKSELELKECNKQVESLNEKLQNaKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEM 419
Cdd:pfam07111 302 KKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQE-QVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQM 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 420 E-----SVIKEQEDYIATQYKEVIDLGQELRLTQEQMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKEAHGn 494
Cdd:pfam07111 381 ElsraqEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALA- 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 495 RLAEELGASQVREAHLEARMQAEIKKLSSEVDSLKEAYQIEMISHQENHAKWKLSAESQKtsvQQLNEQLEKAKQELEEA 574
Cdd:pfam07111 460 QLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAER---QQLSEVAQQLEQELQRA 536
|
490 500 510
....*....|....*....|....*....|....*.
gi 1907166662 575 QDTVSNLHQQVQDRNEVIEAANEALLIKESELTRLQ 610
Cdd:pfam07111 537 QESLASVGQQLEVARQGQQESTEEAASLRQELTQQQ 572
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
121-288 |
7.68e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 121 QSKLEKQVSKQEQelQKQRESSTEKLRKMEEKYETAIREVDLKRQKIIELTG-----TARQAKLEmDQYKEELSKMEKEI 195
Cdd:PRK11637 54 QDIAAKEKSVRQQ--QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKqidelNASIAKLE-QQQAAQERLLAAQL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 196 IHLKRDGENKSMQL-----------------SQLDMVLDQTKTELEKTTNSVKELERLQHHTETELTETMQKREALENEL 258
Cdd:PRK11637 131 DAAFRQGEHTGLQLilsgeesqrgerilayfGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKL 210
|
170 180 190
....*....|....*....|....*....|
gi 1907166662 259 QNAHGELKSTLRQLQelrDVLQKAQLSLEE 288
Cdd:PRK11637 211 EQARNERKKTLTGLE---SSLQKDQQQLSE 237
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
276-596 |
7.84e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 39.82 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 276 RDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKERNWELKQraaqvTHLDMTIREHRGEMEQKIIK 355
Cdd:PRK04778 197 REILDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDH-----LDIEKEIQDLKEQIDENLAL 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 356 LEgtleksELELKECNKQVESLNEKLQNAKEQLrEKEFIMlqneqeisqlKKEIERTQQRMKEMESVIKEQEDyiatqyk 435
Cdd:PRK04778 272 LE------ELDLDEAEEKNEEIQERIDQLYDIL-EREVKA----------RKYVEKNSDTLPDFLEHAKEQNK------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 436 eviDLGQELRLTQEQMQNTHSELVEARrqevQAQREIERLAGELEDIKQLSKEKEAHGNRLAEELGASqvrEAHLEArMQ 515
Cdd:PRK04778 328 ---ELKEEIDRVKQSYTLNESELESVR----QLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEI---LKQLEE-IE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 516 AEIKKLSSEVDSLKEAyqiEMISHQE-NHAKWKLSA---------------------ESQKTSVQQLNEQL-------EK 566
Cdd:PRK04778 397 KEQEKLSEMLQGLRKD---ELEAREKlERYRNKLHEikryleksnlpglpedylemfFEVSDEIEALAEELeekpinmEA 473
|
330 340 350
....*....|....*....|....*....|
gi 1907166662 567 AKQELEEAQDTVSNLHQQVqdrNEVIEAAN 596
Cdd:PRK04778 474 VNRLLEEATEDVETLEEET---EELVENAT 500
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
294-499 |
7.96e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 39.60 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 294 KDLTAELRECKMEIEDKKQELIEmdqaLKERNWELKQRAAQVThldmtirehRGEMEQKIIKLEGTLEKSELELKECNKQ 373
Cdd:pfam05262 180 KKVVEALREDNEKGVNFRRDMTD----LKERESQEDAKRAQQL---------KEELDKKQIDADKAQQKADFAQDNADKQ 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 374 VESLNEKLQNAKEQLREKEFIMLQNEQEISQ-LKKEIERTQQRMKEMESVIKEQEDYIATqykeviDLGQELRlTQEQMq 452
Cdd:pfam05262 247 RDEVRQKQQEAKNLPKPADTSSPKEDKQVAEnQKREIEKAQIEIKKNDEEALKAKDHKAF------DLKQESK-ASEKE- 318
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907166662 453 nthselveARRQEVQAQREIERLAGELEDIKQLSKEKEAHGNRLAEE 499
Cdd:pfam05262 319 --------AEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
53-421 |
8.40e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 53 QLERNKEKFERQLKKKSEEVYCLQKELkikthnlEETSEQNAILQHTLQQQQQMLQQETMRNGELEDTQSKLEKQVSKQE 132
Cdd:pfam01576 205 ELEKAKRKLEGESTDLQEQIAELQAQI-------AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQ 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 133 QELQK---QRESSTEKLRKMEEKYETairevdLKRQKIIELTGTARQAKLEmdqykeelSKMEKEIIHLKR--DGENKSM 207
Cdd:pfam01576 278 EDLESeraARNKAEKQRRDLGEELEA------LKTELEDTLDTTAAQQELR--------SKREQEVTELKKalEEETRSH 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 208 QLSQLDM------VLDQTKTELEKTTNSVKELERLQHHTETEL--------------TETMQKREALENELQNAHGELKS 267
Cdd:pfam01576 344 EAQLQEMrqkhtqALEELTEQLEQAKRNKANLEKAKQALESENaelqaelrtlqqakQDSEHKRKKLEGQLQELQARLSE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 268 TLRQLQELRDVLQKAQLSLEEKYTTIKDLTAELRECKMEIEDKKQELIEMDQALKErnwELKQRAAQVTHLDMTIREHRG 347
Cdd:pfam01576 424 SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQE---ETRQKLNLSTRLRQLEDERNS 500
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907166662 348 EMEQkiiklegtLEKSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMES 421
Cdd:pfam01576 501 LQEQ--------LEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAA 566
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
125-490 |
9.49e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.32 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 125 EKQVSKQEQELQKQRESSTEKLRKMEEkyETAIREVDLKRQKIIELTGTARQAKLEMDQYKEELSKMEKEIIHLKRDGEN 204
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELIFLLQAREK--EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 205 KSMQLSQLDMVLdQTKTELEKTTNSVKELERLQHHTETELTETMQKREALE---NELQNAHGELKSTLRQLQELRDVLQK 281
Cdd:pfam05483 502 KELTQEASDMTL-ELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELEsvrEEFIQKGDEVKCKLDKSEENARSIEY 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 282 AQLSLEEKYTTIKDLTAELREckmEIEDKKQELIEMDQALKERNWELKQRAAQVTHLDMTIREHRGEMEQKIIKLEGTLE 361
Cdd:pfam05483 581 EVLKKEKQMKILENKCNNLKK---QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIID 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 362 KSELELKECNKQVESLNEKLQNAKEQLREKEFIMLQNEQEISQLKKEIERTQQRMKEMESVIKEQEDYIATQYKEVIDLG 441
Cdd:pfam05483 658 NYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQ 737
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907166662 442 QELRLTQE-QMQNTHSELVEARRQEVQAQREIERLAGELEDIKQLSKEKE 490
Cdd:pfam05483 738 SSAKAALEiELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
41-196 |
9.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 41 EICKEELALHLNQ-LERNKEKFERQLKKKSEEVYCLQKELKIKTHNLEETSEQNailQHTLQQQQQMLQQETMRNGELED 119
Cdd:PRK12704 52 EAIKKEALLEAKEeIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL---EKREEELEKKEKELEQKQQELEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907166662 120 TQSKLEKQVSKQEQELQK-----QRESSTEKLRKMEEKYETAIrevdlkrqkiieltgtARQAKLEMDQYKEELSKMEKE 194
Cdd:PRK12704 129 KEEELEELIEEQLQELERisgltAEEAKEILLEKVEEEARHEA----------------AVLIKEIEEEAKEEADKKAKE 192
|
..
gi 1907166662 195 II 196
Cdd:PRK12704 193 IL 194
|
|
| |
