|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
41-341 |
2.37e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 41 KEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAfKELNKAKAliVKDEEIEQDIPEVKREISLVKNll 120
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA-DELKKAEE--KKKADEAKKAEEKKKADEAKKK-- 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 121 ASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNLETVKKQLELEKQKTLKEKKRADM------ES 194
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakkkaeEK 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 195 AKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTASSQVKFAENSEKLEEKIRLLEMNKKTAMDwKSRTDDLTQQLQEA 274
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE-AKKAEEAKKKAEEA 1469
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253927 275 QlVAEGLKKQVHELSLSQKSIKTHSISPQKVRDLEKAEMRllKKKMKFERNC--AKHSQTVAKFEKFRR 341
Cdd:PTZ00121 1470 K-KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA--KKKADEAKKAeeAKKADEAKKAEEAKK 1535
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
33-347 |
1.15e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 33 QQKLERNLKEKSEETKLLQDQASGREKEinelrdllKKETLRADSSEEER--EHAFKELNKAKALIVKDEEIEQDIPEVK 110
Cdd:PTZ00121 1481 EAKKADEAKKKAEEAKKKADEAKKAAEA--------KKKADEAKKAEEAKkaDEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 111 REISLVKnllASERQKTESERKKaESEKKKAdkyLSELEVLRNSAHKtssdlltltsNLETVKKQLELEKQKTLKEKKRA 190
Cdd:PTZ00121 1553 KAEELKK---AEEKKKAEEAKKA-EEDKNMA---LRKAEEAKKAEEA----------RIEEVMKLYEEEKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 191 DMESAKArDQMKLAEDVSKKFEIVRARNEELKK---EMESQTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDL 267
Cdd:PTZ00121 1616 EEAKIKA-EELKKAEEEKKKVEQLKKKEAEEKKkaeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 268 TQQLQEAQLVAEGLKKQVHELSLSQKSIKTHSISPQKVRDLEKAEMRLLKK--KMKFERNCAKHSQTVAKFEKFRREFQC 345
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaeEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
..
gi 330253927 346 EE 347
Cdd:PTZ00121 1775 KE 1776
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
33-354 |
7.07e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 33 QQKLERNLKEKSEETKLLQDQASGREKEINELRDLLKKEtlradsSEEEREHAFKELNKAKALIVKDEEIEQDIPEVKRE 112
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAE------AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 113 ISLVKNLLASERQKTESERKKAESEKKKADKYLSElEVLRNSAHKTSSDllTLTSNLETVKKQLELEKQKtlKEKKRADM 192
Cdd:PTZ00121 1387 AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD-EAKKKAEEKKKAD--EAKKKAEEAKKADEAKKKA--EEAKKAEE 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 193 ESAKARDQMKlAEDVSKKFEIVRARNEELKKEMESQTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQ 272
Cdd:PTZ00121 1462 AKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK 1540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 273 EAQLV--AEGLKK--QVHELSLSQKSIKTHSISPQKVRDLEKAE-MRLLKKKMKFERNCAKHSQTVAKFEKFRRefqcEE 347
Cdd:PTZ00121 1541 KAEEKkkADELKKaeELKKAEEKKKAEEAKKAEEDKNMALRKAEeAKKAEEARIEEVMKLYEEEKKMKAEEAKK----AE 1616
|
....*..
gi 330253927 348 LGRLKLE 354
Cdd:PTZ00121 1617 EAKIKAE 1623
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
41-324 |
7.43e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 41 KEKSEETKLLQDQASGRE-KEINELRDLLKKETLRADSSEEERehafKELNKAKALIVKDEEiEQDIPEVKREISLVKNL 119
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADElKKAEELKKAEEKKKAEEAKKAEED----KNMALRKAEEAKKAE-EARIEEVMKLYEEEKKM 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 120 LASERQKTESERKKAESekkkadkyLSELEVLRNSAHKTSSDLLTLTSNLETVKKQLELEKQKTLKEKKRADMESAKARD 199
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEE--------LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 200 QMKLAEDVSKKFEIVRARNEELKKEMESQTassqvKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQlVAE 279
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKK-----KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK-KDE 1753
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 330253927 280 GLKKQVHELSLSQKSIKTHSISPQKVRDLEKAEMRLLKKKMKFER 324
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-369 |
7.54e-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: 63.54 E-value: 7.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 1 MATDGDTKENGSTVkaSLEKEISRLKFEIVSLQQK---LERNLKEKSEETKLLQDQASGREKEINELRDLLKKetLRADS 77
Cdd:TIGR02168 660 VITGGSAKTNSSIL--ERRREIEELEEKIEELEEKiaeLEKALAELRKELEELEEELEQLRKELEELSRQISA--LRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 78 SEEEREHafkelnkakalivkdEEIEQDIPEVKREISLVKNLLASERQKTESERKKAESEkkkadkyLSELEVLRNSAHK 157
Cdd:TIGR02168 736 ARLEAEV---------------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA-------EAEIEELEAQIEQ 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 158 TSSDLLTLTSNLETVKKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQtassQVKFA 237
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 238 ENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIKTHsispqkvrdLEKAEMRLLK 317
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR---------LEGLEVRIDN 940
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253927 318 KK--------MKFERNCAKHSQTVAKFEKFRREF-----QCEELGRLKL----EFGSLTNRMNLLDEYF 369
Cdd:TIGR02168 941 LQerlseeysLTLEEAEALENKIEDDEEEARRRLkrlenKIKELGPVNLaaieEYEELKERYDFLTAQK 1009
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
13-287 |
5.63e-09 |
|
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: 60.75 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 13 TVKASLEKEISRLKFEIVSLQQKLE--RNLKEKSEETKLLQDQASGREKEINELRDLLKKETLrADSSEEEREHAFKELN 90
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAylTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEE-TQERINRARKAAPLAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 91 KAKALivkdEEIEQDIPEVKREISLVKNLLASERQKTES---ERKKAESEKKKADKYLSELEVLRNSAHKT------SSD 161
Cdd:TIGR00618 298 HIKAV----TQIEQQAQRIHTELQSKMRSRAKLLMKRAAhvkQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsireiSCQ 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 162 LLTLTSNLETVKKQLELEKQK-----TLKEKKRADMESAKARDQMKLAEdvskKFEIVRARNEElkkEMESQTASSQVKF 236
Cdd:TIGR00618 374 QHTLTQHIHTLQQQKTTLTQKlqslcKELDILQREQATIDTRTSAFRDL----QGQLAHAKKQQ---ELQQRYAELCAAA 446
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 330253927 237 AENsEKLEEKIRLLEMNKKtamdwKSRTDDLTQQLQEAQ--LVAEGLKKQVHE 287
Cdd:TIGR00618 447 ITC-TAQCEKLEKIHLQES-----AQSLKEREQQLQTKEqiHLQETRKKAVVL 493
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-296 |
1.84e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 18 LEKEISRLKFEIVSLQ-QKLERNLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNKAKALI 96
Cdd:COG1196 225 LEAELLLLKLRELEAElEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 97 VKDEEIEQDIPEVKREISLVKNLLASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNLET----- 171
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEeleel 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 172 VKKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTA--SSQVKFAENSEKLEEKIRL 249
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAleEAAEEEAELEEEEEALLEL 464
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 330253927 250 LEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIK 296
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
12-243 |
1.25e-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: 55.54 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 12 STVKASLEKEISRLKFEIVSLQQKLERNLKEKSE---ETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKE 88
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKAllkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 89 LNKAKALIVK----------DEEIE-----QDIPEVKREISLVKNLLASERQKTESERKKaesekkkadkyLSELEVLRN 153
Cdd:COG4942 99 LEAQKEELAEllralyrlgrQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRAD-----------LAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 154 SAHKTSSDLLTLTSNLETVKKQLELEKQKtlKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTASSQ 233
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
250
....*....|
gi 330253927 234 VKFAENSEKL 243
Cdd:COG4942 246 AGFAALKGKL 255
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
15-354 |
1.49e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 56.30 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 15 KASLEKEISRLKFEIVSLQQKLERNLKE---KSEETKLLQDQASgREKEINELRDLLKKETLRADSSEEEREHAFKELNK 91
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEearKAEEAKKKAEDAR-KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDA 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 92 AKALIVKDEEIEQDIPEVKREISLVKnllASERQKTESERKKAESEKKKADKYLSEL----EVLRNSAHKTSSDLltlTS 167
Cdd:PTZ00121 1164 RKAEEARKAEDAKKAEAARKAEEVRK---AEELRKAEDARKAEAARKAEEERKAEEArkaeDAKKAEAVKKAEEA---KK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 168 NLETVKKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIVRArnEELKKEMESQTASSQVKFAENSEKLEEKI 247
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA--EEKKKADEAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 248 RLLEMNKKtAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIKTHSISPQKVRDLEKAEMRLLKKKMKFERNCA 327
Cdd:PTZ00121 1316 KADEAKKK-AEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
330 340
....*....|....*....|....*..
gi 330253927 328 KHSQTVAKFEKFRREFQCEELGRLKLE 354
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-297 |
2.17e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 17 SLEKEISRLKFEIVSLQQK---LERNLKEKSEETKLLQDQASGREKEINELRDLL-----KKETLRAD--SSEEEREHAF 86
Cdd:TIGR02168 236 ELREELEELQEELKEAEEEleeLTAELQELEEKLEELRLEVSELEEEIEELQKELyalanEISRLEQQkqILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 87 KELNKAKALIVKDE----EIEQDIPEVKREISLVKNLLASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDL 162
Cdd:TIGR02168 316 RQLEELEAQLEELEskldELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 163 LTLTSNLETVKKQLE-LEkqktlKEKKRADMESAKARDQMKLAEdvskkFEIVRARNEELKKEMEsQTASSQVKFAENSE 241
Cdd:TIGR02168 396 ASLNNEIERLEARLErLE-----DRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELE-ELQEELERLEEALE 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 330253927 242 KLEEKIRLLEmnkktamdwkSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIKT 297
Cdd:TIGR02168 465 ELREELEEAE----------QALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-294 |
2.48e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 16 ASLEKEISRLKFEIVSLQQKLERNLKEKSEETKLLQDQASGR-----------EKEINELRDLLKKETLRADSSEEEREH 84
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEqlrvkekigelEAEIASLERSIAEKERELEDAEERLAK 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 85 AFKELNKAKALIvkdEEIEQDIPEVKREISLVKNLLASERQKTESERkkaesekkkadkylSELEVLRNSAHKTSSDLLT 164
Cdd:TIGR02169 327 LEAEIDKLLAEI---EELEREIEEERKRRDKLTEEYAELKEELEDLR--------------AELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 165 LTSNLETVKKQ---LELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEivrARNEELKKEMESQTassqvkfaensE 241
Cdd:TIGR02169 390 YREKLEKLKREineLKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE---EEKEDKALEIKKQE-----------W 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 330253927 242 KLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKS 294
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
7-283 |
4.61e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 7 TKENGSTVKASLEKEISRLKFEIVSLQQKLERNLKEKSE-ETKLLQDQASGREKE----INELRDLLKK---ETLRADSS 78
Cdd:PRK03918 446 TEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRElEKVLKKESELIKLKElaeqLKELEEKLKKynlEELEKKAE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 79 EEE--REHAFK----------ELNKAKALIVKDEEIEQDIPEVKREISLVKNLLASERQKTESErkkaesekkkADKYLS 146
Cdd:PRK03918 526 EYEklKEKLIKlkgeikslkkELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE----------LEERLK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 147 ELEvlrnSAHKTSSDLLTLTSNLETVKKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKF---EIVRARNEELKK 223
Cdd:PRK03918 596 ELE----PFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseeEYEELREEYLEL 671
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330253927 224 EMESQTASSQVKFAENS-EKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKK 283
Cdd:PRK03918 672 SRELAGLRAELEELEKRrEEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKK 732
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-250 |
9.20e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 15 KASLEKEISRLKfeivSLQQKLERNLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNKAKA 94
Cdd:COG1196 297 LARLEQDIARLE----ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 95 LIvkdEEIEQDIPEVKREISLVKNLLASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNLETVKK 174
Cdd:COG1196 373 EL---AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253927 175 QLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIVRARnEELKKEMESQTA--SSQVKFAENSEKLEEKIRLL 250
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-LLLLLEAEADYEgfLEGVKAALLLAGLRGLAGAV 526
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
10-319 |
1.16e-06 |
|
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: 53.05 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 10 NGSTV-KASLEKEISRLKFEIVSL----QQKLERNLKEKSEETKLLQDQASGREKE-----------------INELRDL 67
Cdd:pfam02463 112 NGKNVtKKEVAELLESQGISPEAYnflvQGGKIEIIAMMKPERRLEIEEEAAGSRLkrkkkealkklieetenLAELIID 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 68 LKKETLRADSSEEEREHAFKELNKAKALIVKDEEIEQDIPE--VKREISLVKNLLASERQKTESERKKAESEKKKADKYL 145
Cdd:pfam02463 192 LEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLklNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 146 SELEVLRNSAHKTSSDLLTLTSNLETVKKQLELEKQKT---LKEKKRADMESAKARDQMKLAEDVSKKFEIVRA---RNE 219
Cdd:pfam02463 272 KENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKvddEEKLKESEKEKKKAEKELKKEKEEIEELEKELKeleIKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 220 ELKKEMESQTASSQVKFAENSEKLEEKIRLLEMNKKTAM--DWKSRTDDLTQQlQEAQLVAEGLKKQVHELSLSQKSIKT 297
Cdd:pfam02463 352 EAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAklKEEELELKSEEE-KEAQLLLELARQLEDLLKEEKKEELE 430
|
330 340
....*....|....*....|..
gi 330253927 298 HSISPQKVRDLEKAEMRLLKKK 319
Cdd:pfam02463 431 ILEEEEESIELKQGKLTEEKEE 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
29-369 |
1.19e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 29 IVSlQQKLERNLKEKSEETKLLQDQASG------REKE-----------INELRDLLK-----KETLRADSSEEERehaF 86
Cdd:TIGR02168 140 IIE-QGKISEIIEAKPEERRAIFEEAAGiskykeRRKEterklertrenLDRLEDILNelerqLKSLERQAEKAER---Y 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 87 KELNKAKalivkdEEIEQDIpEVKREISLVKNL--LASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLT 164
Cdd:TIGR02168 216 KELKAEL------RELELAL-LVLRLEELREELeeLQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 165 LtsNLETVKKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIvrarnEELKKEMESQTASSQVKFAENSEKLE 244
Cdd:TIGR02168 289 E--LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-----AEELAELEEKLEELKEELESLEAELE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 245 EKIRLLEMNKKTAMDW-------KSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQK----SIKTHSISPQKVrDLEKAEM 313
Cdd:TIGR02168 362 ELEAELEELESRLEELeeqletlRSKVAQLELQIASLNNEIERLEARLERLEDRRErlqqEIEELLKKLEEA-ELKELQA 440
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253927 314 RLLKKKMKFERNCAKHSQTVAKFEKFRREFQC---------EELGRLKLEFGSLTNRMNLLDEYF 369
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEaeqaldaaeRELAQLQARLDSLERLQENLEGFS 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
9-288 |
1.21e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 9 ENGSTVKASLEKEISRLKFEIVSLQ--QKLERNLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAF 86
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 87 KELNK----AKALIVKDEEIEQDIPEVKREISLVKNLLAsERQKTESERKKAESEKKKADKYLSELevlrnsaHKTSSDL 162
Cdd:PRK03918 245 KELESlegsKRKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL-------REIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 163 LTLTSNLETVKKQL-ELEKQKTLKEKKRADMESAKaRDQMKLAEDVsKKFEIVRA---RNEELKKEMESqtassqvkfaE 238
Cdd:PRK03918 317 SRLEEEINGIEERIkELEEKEERLEELKKKLKELE-KRLEELEERH-ELYEEAKAkkeELERLKKRLTG----------L 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 330253927 239 NSEKLEEKIRLLEMNKKTAMDwksRTDDLTQQLQEAQLVAEGLKKQVHEL 288
Cdd:PRK03918 385 TPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEEL 431
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
21-297 |
2.31e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.36 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 21 EISRLKFEIVSLQQKLERNLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEE------------REHAFKE 88
Cdd:TIGR01612 1112 EINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAISNDDPEEIEkkienivtkidkKKNIYDE 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 89 LNKAKALIVKDEEIEQDIPEVKR-EISLVKNLLASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDL---LT 164
Cdd:TIGR01612 1192 IKKLLNEIAEIEKDKTSLEEVKGiNLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMgieMD 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 165 LTSNLETVKKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIvrarnEELKKEMESQTASSQVKFAENSEKLE 244
Cdd:TIGR01612 1272 IKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIEDFSEESDI-----NDIKKELQKNLLDAQKHNSDINLYLN 1346
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 330253927 245 EKIRL---LEMNK-KTAMDwksRTDDLTQQLQEAQlvaeglKKQVHELSLSQKSIKT 297
Cdd:TIGR01612 1347 EIANIyniLKLNKiKKIID---EVKEYTKEIEENN------KNIKDELDKSEKLIKK 1394
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
9-340 |
5.06e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 9 ENGSTVKASLEKEISRLKFEIVSLQQKLE-----RNLKEK-----SEETKLL--------------QDQASGREKEINEL 64
Cdd:pfam01576 253 EEETAQKNNALKKIRELEAQISELQEDLEseraaRNKAEKqrrdlGEELEALkteledtldttaaqQELRSKREQEVTEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 65 RDLLKKETLRADSSEEE--REH--AFKELN----KAKALIVKDEEIEQDIPEVKREISLVKNLLASERQKTESERKKAES 136
Cdd:pfam01576 333 KKALEEETRSHEAQLQEmrQKHtqALEELTeqleQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 137 EKKKADKYLSELEVLRNSA----HKTSSDLLTLTSNLEtvkkqlELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFE 212
Cdd:pfam01576 413 QLQELQARLSESERQRAELaeklSKLQSELESVSSLLN------EAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLN 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 213 I---VRA----RN---------EELKKEMESQTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQL 276
Cdd:pfam01576 487 LstrLRQledeRNslqeqleeeEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAA 566
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253927 277 VAEGLKKQVHELslsQKSIKTHSISPQKVRDLEKAemrLLKKKMKFERNCAKHSQTVAKFEKFR 340
Cdd:pfam01576 567 AYDKLEKTKNRL---QQELDDLLVDLDHQRQLVSN---LEKKQKKFDQMLAEEKAISARYAEER 624
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
164-312 |
5.39e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.11 E-value: 5.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 164 TLTSNLETVKKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTASSQVKFAENSEKL 243
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEITDQA 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253927 244 EEKIRLlemnkktamdwksrTDDLTQQLQEAQLVAEGLKKQVHELSLSQKsikthsISPQKVRDLEKAE 312
Cdd:PRK11448 226 AKRLEL--------------SEEETRILIDQQLRKAGWEADSKTLRFSKG------ARPEKGRNLAIAE 274
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-257 |
7.52e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 8 KENGSTVKASLEKEISRLKFEIVSLQQKLE--------RNLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSE 79
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNdlearlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 80 EEREHAFKELNKAKALIVKDE-EIEQDIPEVKREISLVKNLLASERQkTESERKKAESEKKKADKYLSELEVLRNSAhKT 158
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEkEIENLNGKKEELEEELEELEAALRD-LESRLGDLKKERDELEAQLRELERKIEEL-EA 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 159 SSDLLTLTSNLETVKKQLELEKQKTLKEKKRADMES---------------AKARDQMKLaEDVSKK----FEIVRARNE 219
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsledvqaelqRVEEEIRAL-EPVNMLaiqeYEEVLKRLD 989
|
250 260 270
....*....|....*....|....*....|....*...
gi 330253927 220 ELKKEMEsqtassqvKFAENSEKLEEKIRLLEMNKKTA 257
Cdd:TIGR02169 990 ELKEKRA--------KLEEERKAILERIEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
18-343 |
7.72e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 18 LEKEISRLKFEIVSLQQKLER--NLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNKAKAL 95
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 96 IVKDEEIEQDIPEVKREISLVKNLLAserQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLT---SNLETV 172
Cdd:PRK03918 344 KKKLKELEKRLEELEERHELYEEAKA---KKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITariGELKKE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 173 KKQL-----ELEKQKT----------------LKEKKRADMES-----AKARDQMKLAEDVSKKFEIVRARNEELKK--E 224
Cdd:PRK03918 421 IKELkkaieELKKAKGkcpvcgrelteehrkeLLEEYTAELKRiekelKEIEEKERKLRKELRELEKVLKKESELIKlkE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 225 MESQTASSQVKFAE-NSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEaqlvAEGLKKQVHELSlsqksikthsispQ 303
Cdd:PRK03918 501 LAEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK----LEELKKKLAELE-------------K 563
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 330253927 304 KVRDLEKAEMRLLKKKMKFERNCAKH-SQTVAKFEKFRREF 343
Cdd:PRK03918 564 KLDELEEELAELLKELEELGFESVEElEERLKELEPFYNEY 604
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
13-281 |
7.92e-06 |
|
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: 50.36 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 13 TVKASLEKEISRLKFEIVSLQQKLERNLKEKSEETKLLQDQASGREKEINELRDLLKKEtLRADSSEEEREHAFKELNKA 92
Cdd:pfam02463 269 QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAE-KELKKEKEEIEELEKELKEL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 93 KALIVKDEEIEQDIPEVKREISLVKNLLASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNLETV 172
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 173 KKQLELEKQKTL-KEKKRADMESAKARDQMKLA---EDVSKKFEIVRARNEELKKEMESQTASSQVKFAENSEKLEEKIR 248
Cdd:pfam02463 428 ELEILEEEEESIeLKQGKLTEEKEELEKQELKLlkdELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
250 260 270
....*....|....*....|....*....|...
gi 330253927 249 LLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGL 281
Cdd:pfam02463 508 GLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
17-321 |
9.40e-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: 50.02 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 17 SLEKEISRLKFEIVSLQQK---LERNLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADsseeerehafkELNKAk 93
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKElknLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKIN-----------KLNSD- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 94 aLIVKDEEIEQDipevKREISLVKNLLAS-ERQKTESERKKaesekkkaDKYLSELEVLRNSAHKTSS---DLLTLTSNL 169
Cdd:TIGR04523 105 -LSKINSEIKND----KEQKNKLEVELNKlEKQKKENKKNI--------DKFLTEIKKKEKELEKLNNkynDLKKQKEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 170 ETVKKQLELEKQKtlKEKKRADMESAKARDQMKLAEDVSKKfeivrARNEELKK---EMESQTASSQVKFAENSEKLEEK 246
Cdd:TIGR04523 172 ENELNLLEKEKLN--IQKNIDKIKNKLLKLELLLSNLKKKI-----QKNKSLESqisELKKQNNQLKDNIEKKQQEINEK 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253927 247 IRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIKTH--SISPQKVRDLEKAEMRLLKKKMK 321
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEisDLNNQKEQDWNKELKSELKNQEK 321
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
46-295 |
1.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 46 ETKLLQDQASGREKEINELRDLLKKetlradsSEEEREHAFKELNKAKALIVKDEEIEQDIPEVKREISLVKNLLASerq 125
Cdd:PRK02224 200 EEKDLHERLNGLESELAELDEEIER-------YEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAE--- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 126 kTESERKKAESEKKKADKYLSELEVLRNSAhKTSSDLLTLTSnlETVKKQLE-LEKQktlKEKKRADMESAKARDQMKL- 203
Cdd:PRK02224 270 -TEREREELAEEVRDLRERLEELEEERDDL-LAEAGLDDADA--EAVEARREeLEDR---DEELRDRLEECRVAAQAHNe 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 204 -AEDVSKKFEIVRARNEELK---KEMESQTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAE 279
Cdd:PRK02224 343 eAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
250
....*....|....*.
gi 330253927 280 GLKKQVHELSLSQKSI 295
Cdd:PRK02224 423 ELREREAELEATLRTA 438
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
12-343 |
1.21e-05 |
|
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: 49.72 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 12 STVKASLEKEISRLKFEIVSLQQKLERNLKEKSEETKLLQDQASGREKEINEL-----RDLLKKETLRADSS-------- 78
Cdd:pfam05483 249 ITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIkmslqRSMSTQKALEEDLQiatkticq 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 79 -EEEREHAFKELNKAKA---LIVKdeeieqdipEVKREISLVKNLLASERQKTESERKKAESEKKKADKYLSELEvlrns 154
Cdd:pfam05483 329 lTEEKEAQMEELNKAKAahsFVVT---------EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELE----- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 155 ahktssDLLTLTSN----LETVKKQLElEKQKTLKEKKRADmesakardqmKLAEDVSKKFE----IVRARNEELkKEME 226
Cdd:pfam05483 395 ------EMTKFKNNkeveLEELKKILA-EDEKLLDEKKQFE----------KIAEELKGKEQelifLLQAREKEI-HDLE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 227 SQTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTqqLQEAQLVAEGlKKQVHELSLSQKSIKTHsispqkvr 306
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLL--LENKELTQEA-SDMTLELKKHQEDIINC-------- 525
|
330 340 350
....*....|....*....|....*....|....*..
gi 330253927 307 dlEKAEMRLLKKKMKFERncaKHSQTVAKFEKFRREF 343
Cdd:pfam05483 526 --KKQEERMLKQIENLEE---KEMNLRDELESVREEF 557
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-367 |
1.47e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 40 LKEKSEET--KLlqDQASGREKEINELRDLLKKetlRADSSEEEREHA--FKELN------KAKALIVKDEEIEQDIPEV 109
Cdd:COG1196 170 YKERKEEAerKL--EATEENLERLEDILGELER---QLEPLERQAEKAerYRELKeelkelEAELLLLKLRELEAELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 110 KREISLVKNLLAS---ERQKTESERkkaesekkkaDKYLSELEVLRNSAHKTSSDLLTLTSNLETVKKQLELEKQKT--- 183
Cdd:COG1196 245 EAELEELEAELEEleaELAELEAEL----------EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRrel 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 184 LKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSR 263
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 264 TDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIKTHSISPQKVRD-LEKAEMRLLKKKMKFERNCAKHSQTVAKfEKFRRE 342
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEeEEEALEEAAEEEAELEEEEEALLELLAE-LLEEAA 473
|
330 340
....*....|....*....|....*
gi 330253927 343 FQCEELGRLKLEFGSLTNRMNLLDE 367
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLE 498
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
7-288 |
2.41e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 7 TKENGSTVKASLEK---EISRLKFEIVSLQQKLERNLKEK---SEETKLLQDQASGREKEINELRD------------LL 68
Cdd:PRK02224 235 TRDEADEVLEEHEErreELETLEAEIEDLRETIAETEREReelAEEVRDLRERLEELEEERDDLLAeaglddadaeavEA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 69 KKETLRADSSEEE--------------------REHAFKELNKAKALIVKDEEIEQDIPEVKREISLVKNLLASERQKTE 128
Cdd:PRK02224 315 RREELEDRDEELRdrleecrvaaqahneeaeslREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 129 SERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNLETVKKQLE-----LEKQK------TLKEKKRADmESAKA 197
Cdd:PRK02224 395 ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeaealLEAGKcpecgqPVEGSPHVE-TIEED 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 198 RDQmklAEDVSKKFEIVRARNEELKKEMESqtASSQVKFAENSEKLEEKIRLLEmnkktamdwkSRTDDLTQQLQEAQLV 277
Cdd:PRK02224 474 RER---VEELEAELEDLEEEVEEVEERLER--AEDLVEAEDRIERLEERREDLE----------ELIAERRETIEEKRER 538
|
330
....*....|.
gi 330253927 278 AEGLKKQVHEL 288
Cdd:PRK02224 539 AEELRERAAEL 549
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
43-304 |
2.75e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 43 KSEETKLLQDQASGREKEINELRDLLKKETLRadSSEEEREHAfKELNKAKALIVKDEEIEQDIPEVKREISLVKNLLAS 122
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK--KAEEAKIKA-EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 123 ERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDlLTLTSNLETVKKQLELEKQKTLKEKKRADMESAKARDQMK 202
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 203 LAEDVSKKFEivRARNEELKKEMESQTASSQVKFAENSEKLEEKI-----------RLLEMNKKTAmDWKSRTDDLTQQL 271
Cdd:PTZ00121 1738 EAEEDKKKAE--EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieeeldeedekRRMEVDKKIK-DIFDNFANIIEGG 1814
|
250 260 270
....*....|....*....|....*....|....*..
gi 330253927 272 QEAQLVAEGLKK----QVHELSLSQKSIKTHSISPQK 304
Cdd:PTZ00121 1815 KEGNLVINDSKEmedsAIKEVADSKNMQLEEADAFEK 1851
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
3-337 |
2.93e-05 |
|
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: 48.56 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 3 TDGDTKENGSTVKASLEKEISRLKFEIVSLQQKLERNLKEKSEETKLLQDQasgrEKEINELRDLLKKETLRADSSEEER 82
Cdd:pfam05483 68 SDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQ----RKAIQELQFENEKVSLKLEEEIQEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 83 EHAFKELNKAKALIvkdeeieqdipevkreiSLVKNLLASERQKTEserkkaesekkkadKYLSELEvlrnsahKTSSDL 162
Cdd:pfam05483 144 KDLIKENNATRHLC-----------------NLLKETCARSAEKTK--------------KYEYERE-------ETRQVY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 163 LTLTSNLEtvkkqleleKQKTLKEKKRADMESAKARDQMKLAEDvskkFEIVRARNEELKKEM---ESQTASSQVKFAEN 239
Cdd:pfam05483 186 MDLNNNIE---------KMILAFEELRVQAENARLEMHFKLKED----HEKIQHLEEEYKKEIndkEKQVSLLLIQITEK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 240 SEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLS-QKSIKTHSISPQKVRDLEKAEMRLLKK 318
Cdd:pfam05483 253 ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSlQRSMSTQKALEEDLQIATKTICQLTEE 332
|
330 340
....*....|....*....|...
gi 330253927 319 K--MKFERNCAK--HSQTVAKFE 337
Cdd:pfam05483 333 KeaQMEELNKAKaaHSFVVTEFE 355
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
36-259 |
4.33e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.64 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 36 LERNLKEKSEETKLLQDQASGREKEINELRDllkketlradSSEEEREHAFKELNKAKALivkDEEIEQDIPEVKREISL 115
Cdd:pfam15709 325 LEKREQEKASRDRLRAERAEMRRLEVERKRR----------EQEEQRRLQQEQLERAEKM---REELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 116 VKNLLASERQKTESERKkaesekkkadKYLSELEVLRNSAHKTSSdlltltsnlETVKKQLELEKQKTLKEKKRADMESA 195
Cdd:pfam15709 392 RKQRLEEERQRQEEEER----------KQRLQLQAAQERARQQQE---------EFRRKLQELQRKKQQEEAERAEAEKQ 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253927 196 KARD-QMKLAEDVSKKFEIVRARNEELKKEMESQTASSQVKFAENSEKLEEKIRL-LEMNKKTAMD 259
Cdd:pfam15709 453 RQKElEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLaLEEAMKQAQE 518
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
18-223 |
4.44e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.38 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 18 LEKEISRLKFEIVSLQQKlernlkeKSEETKLLQDQ--ASGREKEINELRDLLKKEtlraDSSEEEREHA-FKELNKAKa 94
Cdd:PRK11637 101 LNKQIDELNASIAKLEQQ-------QAAQERLLAAQldAAFRQGEHTGLQLILSGE----ESQRGERILAyFGYLNQAR- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 95 livkdeeiEQDIPEVKREISLVKNLLASERQKTESERKKAESEKKKADKylseLEVLRNSAHKTssdLLTLTSNLETVKK 174
Cdd:PRK11637 169 --------QETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQK----LEQARNERKKT---LTGLESSLQKDQQ 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 330253927 175 QL-ELEKQKT-LKEK-KRADMEsAKARdqmklAEDVSKKFEIVRARNEELKK 223
Cdd:PRK11637 234 QLsELRANESrLRDSiARAERE-AKAR-----AEREAREAARVRDKQKQAKR 279
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-274 |
4.84e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 16 ASLEKEISRLKFEIVSLQQKLERnlkeKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNKAKAL 95
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 96 IvkdEEIEQDIpevkreISLVKNLLASERQKTESERkkaesekkKADKYLSELEVLRNSAHKTSSDLLTLTSNLETV-KK 174
Cdd:TIGR02168 847 I---EELSEDI------ESLAAEIEELEELIEELES--------ELEALLNERASLEEALALLRSELEELSEELRELeSK 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 175 QLELEKQKTLKEKKRADMESAKARDQMKLAedvskkfEIVRARNEELKKEMESQtASSQVKFAENSEKLEEKIRLLEMNK 254
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRID-------NLQERLSEEYSLTLEEA-EALENKIEDDEEEARRRLKRLENKI 981
|
250 260 270
....*....|....*....|....*....|....
gi 330253927 255 K-------TAMD----WKSRTDDLTQQ---LQEA 274
Cdd:TIGR02168 982 KelgpvnlAAIEeyeeLKERYDFLTAQkedLTEA 1015
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
78-361 |
5.30e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 78 SEEEREHAFKELNKakalIVKDEEIEQDIPEVKREISLVKNLLASERQKTESERKKAESEKKKADKYLSELEVLRNSAHK 157
Cdd:PRK03918 143 SDESREKVVRQILG----LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 158 TSSDLLTLTSNLETVKK------QLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEmesqtAS 231
Cdd:PRK03918 219 LREELEKLEKEVKELEElkeeieELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEK-----AE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 232 SQVKFAENSEKLEEKIRLLEmnkKTAMDWKSRTDDLTQQLQEaqlvAEGLKKQVHELSlsqksikthsispQKVRDLEKA 311
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIE---KRLSRLEEEINGIEERIKE----LEEKEERLEELK-------------KKLKELEKR 353
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 330253927 312 EMRLLKKKMKFERNCAKhsqtVAKFEKFRREFQCEELGRLKLEFGSLTNR 361
Cdd:PRK03918 354 LEELEERHELYEEAKAK----KEELERLKKRLTGLTPEKLEKELEELEKA 399
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
47-367 |
6.05e-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: 47.73 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 47 TKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNKAKALIVKDEEIEQDIPEVKREISLVKNlLASERQK 126
Cdd:TIGR00606 572 KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLER-LKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 127 TESERKKAESEKKKADKYLSELEVLRNSA-------HKTSSDLLTLTSNLETV-----KKQLELEKQKTLKEKKRADMeS 194
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLTDENQSCcpvcqrvFQTEAELQEFISDLQSKlrlapDKLKSTESELKKKEKRRDEM-L 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 195 AKARDQMKLAEDVSKKFEIVRARNEELKKEMEsqtassqvKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEA 274
Cdd:TIGR00606 730 GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ--------RLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMEL 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 275 QLVAEGLKKQVHELSLSQKSIKTHSISpQKVRDlEKAEMRLLKKKMKFERNCAKHSQTVAKFEKFRrefqCEELGRLKLE 354
Cdd:TIGR00606 802 KDVERKIAQQAAKLQGSDLDRTVQQVN-QEKQE-KQHELDTVVSKIELNRKLIQDQQEQIQHLKSK----TNELKSEKLQ 875
|
330
....*....|...
gi 330253927 355 FGSLTNRMNLLDE 367
Cdd:TIGR00606 876 IGTNLQRRQQFEE 888
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
51-275 |
2.06e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 51 QDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNKAKALIvkdEEIEQDIPEVKREISLVKNLLAsERQKTESE 130
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL---EALQAEIDKLQAEIAEAEAEIE-ERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 131 RKKAESEKKKADKYLSELevlrnsahKTSSDLLTLTSNLETVKKQLE-----LEKQKTLKEKkradMESAKARDQMKLAE 205
Cdd:COG3883 91 RARALYRSGGSVSYLDVL--------LGSESFSDFLDRLSALSKIADadadlLEELKADKAE----LEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253927 206 dvskkFEIVRARNEELKKEMESQTASSQVKFAENSEK---LEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQ 275
Cdd:COG3883 159 -----LEALKAELEAAKAELEAQQAEQEALLAQLSAEeaaAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
6-296 |
3.13e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 6 DTKENGSTVKASLEKEISRLKFEIVSLQQKLERNLKEKSEETKLLQDQASGREKEINELRDLLKKETlradsseeEREHA 85
Cdd:TIGR04523 384 QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS--------VKELI 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 86 FKELNKAKalivkdEEIEQDIPEVKREISLVKNLLasERQKTESERKKaesekkkadkylSELEVLRNSAHKTSSDLLTL 165
Cdd:TIGR04523 456 IKNLDNTR------ESLETQLKVLSRSINKIKQNL--EQKQKELKSKE------------KELKKLNEEKKELEEKVKDL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 166 TSNLETVK-KQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKfeIVRARNEELKKEMESQTASSQvkfaeNSEKLE 244
Cdd:TIGR04523 516 TKKISSLKeKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK--EIDEKNKEIEELKQTQKSLKK-----KQEEKQ 588
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 330253927 245 EKIRLLEMNKKtamDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIK 296
Cdd:TIGR04523 589 ELIDQKEKEKK---DLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
61-327 |
4.82e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 61 INELRDLLKKETLRADSSEEEREHAFKELNKAKALIVKDEEIEQDIPEVKREISLVKNLLASERQKTESERKKAESEKKK 140
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 141 ADKYLSEL---------EVLRNSAHKTSSDLLTLTSNLETVKKQLELEKQKTLKEK--------KRADMESAKARDQMKL 203
Cdd:PRK01156 251 KNRYESEIktaesdlsmELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDienkkqilSNIDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 204 AEDVSK---KFEIVRARNEELKKEMES--QTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSRTddltqqLQEAQLVA 278
Cdd:PRK01156 331 LSVLQKdynDYIKKKSRYDDLNNQILEleGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEI------LKIQEIDP 404
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 330253927 279 EGLKKQVHELSLSQKSIKThsispqKVRDLEKAEMRLLKKKMKFERNCA 327
Cdd:PRK01156 405 DAIKKELNEINVKLQDISS------KVSSLNQRIRALRENLDELSRNME 447
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
15-212 |
4.89e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 15 KASLEKEISRLKFEIVslqQKLERNLKE-KSEETKLLqdQASGREKEINELRDLLKKEtlradssEEEREHAFKELNKAK 93
Cdd:PRK03918 572 LAELLKELEELGFESV---EELEERLKElEPFYNEYL--ELKDAEKELEREEKELKKL-------EEELDKAFEELAETE 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 94 ALIvkdEEIEQDIPEVKREISlvknllASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNLETVK 173
Cdd:PRK03918 640 KRL---EELRKELEELEKKYS------EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAK 710
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 330253927 174 KQLE-----LEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFE 212
Cdd:PRK03918 711 KELEklekaLERVEELREKVKKYKALLKERALSKVGEIASEIFE 754
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
6-342 |
5.76e-04 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 44.31 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 6 DTKENGSTVKASLEKEISRL-KFEIVSLQQKLERNLKEKseetkllqdQASGREKEINELRDLLKKETLRADSSEEEREH 84
Cdd:COG5644 100 DSDDSVNSDKLENEGSVSSIdENELVDLDTLLDNDQPEK---------NESGNNDHATDKENLLESDASSSNDSESEESD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 85 AFKELNKAKAliVKDEEIEQDipEVKREISLVKNLLASErQKTESERKKAESEKKKADKYLSElevlRNSAHKTSSDLLT 164
Cdd:COG5644 171 SESEIESSDS--DHDDENSDS--KLDNLRNYIVSLKKDE-ADAESVLSSDDNDSIEEIKYDPH----ETNKESGSSETID 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 165 LTSNLETVKKQLELEKQKTLKEKKRADMESAKARDQMKLaeDVSKKFEIVRARNEELKKEMESQTASSQVKFAENsekle 244
Cdd:COG5644 242 ITDLLDSIPMEQLKVSLKPLVSESSKLDAPLAKSIQDRL--ERQAAYEQTKNDLEKWKPIVADNRKSDQLIFPMN----- 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 245 EKIRLLEMNKKTAMDWKSRTD---DLTQQLQEAQLVAEGLKKQVHELSLSQksikthsISPQKVRDlEKAEMRLLKKKMK 321
Cdd:COG5644 315 ETARPVPSNNGLASSFEPRTEserKMHQALLDAGLENESALKKQEELALNK-------LSVEEVAE-RTRQLRFMRELMF 386
|
330 340
....*....|....*....|....*.
gi 330253927 322 FERNCAKH-----SQTVAKFEKFRRE 342
Cdd:COG5644 387 REERKAKRvakikSKTYRKIRKNRKE 412
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
14-296 |
6.54e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 44.07 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 14 VKASLEKEISRlKFEIVSLQQKLErNLKEKSEETKLlQDQASGR--EKEINELRDLLKKETLRADS--SEEEREHAFKEL 89
Cdd:PLN03229 467 LKKEIDLEYTE-AVIAMGLQERLE-NLREEFSKANS-QDQLMHPvlMEKIEKLKDEFNKRLSRAPNylSLKYKLDMLNEF 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 90 NKAKALI---VKDEEIEQDI----------PEVKREISLVKNLLASERQKTESERKKAESEKKKADKYLSELE---VLRn 153
Cdd:PLN03229 544 SRAKALSekkSKAEKLKAEInkkfkevmdrPEIKEKMEALKAEVASSGASSGDELDDDLKEKVEKMKKEIELElagVLK- 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 154 sahktSSDLltltsNLETVKKQLELEKQKTLKEKKRADMESakardqmkLAEDVSKKFEIV------RARNEELKKEMES 227
Cdd:PLN03229 623 -----SMGL-----EVIGVTKKNKDTAEQTPPPNLQEKIES--------LNEEINKKIERVirssdlKSKIELLKLEVAK 684
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253927 228 QTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIK 296
Cdd:PLN03229 685 ASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLKNDDDKEEDSK 753
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
16-325 |
7.76e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 16 ASLEKEISRLKFEIVSLQQKLER---NLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNKA 92
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQlreELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 93 KAlivKDEEIEQDIPEVKREIslvkNLLASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNLETV 172
Cdd:COG4372 107 QE---EAEELQEELEELQKER----QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 173 KKQLELEKQktLKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTASSQVKFAENSEKLEEKIRLLEM 252
Cdd:COG4372 180 EAEQALDEL--LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253927 253 NKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIKTHSISPQKVRDLEKAEMRLLKKKMKFERN 325
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
8-349 |
7.90e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 8 KENGSTVKASLEKEISRLKFEIVsLQQKLERNLKEKSEETKLLQdQASGREKEINELR----DLLKKETLRADSSEEERE 83
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKI-HLQESAQSLKEREQQLQTKE-QIHLQETRKKAVVlarlLELQEEPCPLCGSCIHPN 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 84 HAFKELNKAKALIVKDEEIEQDIPEVKREISLVKNLLASERQ-------KTESERKKAESEKKKADKYLSELEVLRNsah 156
Cdd:TIGR00618 515 PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKqraslkeQMQEIQQSFSILTQCDNRSKEDIPNLQN--- 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 157 kTSSDLLTLTSNLETVKKQLELEKQKTLKEKK-RADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTASSQVK 235
Cdd:TIGR00618 592 -ITVRLQDLTEKLSEAEDMLACEQHALLRKLQpEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVL 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 236 FAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIKthsispQKVRDLEKAEMRL 315
Cdd:TIGR00618 671 PKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLG------SDLAAREDALNQS 744
|
330 340 350
....*....|....*....|....*....|....
gi 330253927 316 LKKKMKFERNCAKHsQTVAKFEKFRREFQCEELG 349
Cdd:TIGR00618 745 LKELMHQARTVLKA-RTEAHFNNNEEVTAALQTG 777
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
13-131 |
8.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 13 TVKASLEKEISRLKFEIVSLQQKLERNlKEKSEETKLLQD-QASGREKEINELR-DLLKKETLRAdssEEEREHAFKELN 90
Cdd:COG1579 52 TELEDLEKEIKRLELEIEEVEARIKKY-EEQLGNVRNNKEyEALQKEIESLKRRiSDLEDEILEL---MERIEELEEELA 127
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 330253927 91 KAKALIvkdEEIEQDIPEVKREISLVKNLLASERQKTESER 131
Cdd:COG1579 128 ELEAEL---AELEAELEEKKAELDEELAELEAELEELEAER 165
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
146-325 |
9.03e-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: 43.21 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 146 SELEVLRNSAHKTSSDLLTLTSNLETVKKQLE-LEKQKTLKEKKRADMESAKARDQMKLAEdVSKKFEIVRARNEELKKE 224
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAaLERRIAALARRIRALEQELAALEAELAE-LEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 225 MESQTASSQ-------VKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSLSQKSIKT 297
Cdd:COG4942 106 LAELLRALYrlgrqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185
|
170 180
....*....|....*....|....*...
gi 330253927 298 HSISPQKVRDLEKAEMRLLKKKMKFERN 325
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAA 213
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
19-269 |
1.13e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 19 EKEISRLKFEivslQQKLERNLKEKSEETKLLQDQASGREKEINELrdllKKETLRADSSEEERE-HAFKELNKAKALIV 97
Cdd:pfam07888 149 ETELERMKER----AKKAGAQRKEEEAERKQLQAKLQQTEEELRSL----SKEFQELRNSLAQRDtQVLQLQDTITTLTQ 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 98 KDEEIEQDIPE---VKREISLVKNLLASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNL----- 169
Cdd:pfam07888 221 KLTTAHRKEAEneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALregra 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 170 ------ETVKKQLELEKQKTlkEKKRADMESAKARDQMKLAEDVSKKFEIVRARN------EELKKEMESQTASSQVKFA 237
Cdd:pfam07888 301 rwaqerETLQQSAEADKDRI--EKLSAELQRLEERLQEERMEREKLEVELGREKDcnrvqlSESRRELQELKASLRVAQK 378
|
250 260 270
....*....|....*....|....*....|....*...
gi 330253927 238 ENSEKLEEK------IRLLEMNKKTAMDWKSRTDDLTQ 269
Cdd:pfam07888 379 EKEQLQAEKqelleyIRQLEQRLETVADAKWSEAALTS 416
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
15-354 |
1.17e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.35 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 15 KASLEKEISRLKFE-IVSLQQKLERNLkekseetkLLQDQAsgREKEINELRDLLK-KETLRADSSEEEREHAfkeLNKA 92
Cdd:PLN02939 118 NSKDGEQLSDFQLEdLVGMIQNAEKNI--------LLLNQA--RLQALEDLEKILTeKEALQGKINILEMRLS---ETDA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 93 KALIVKDEEIEQDIPEvkreiSLVKNLLASERQKTESERKKAESEKKkadkylsELEVLRNSAHKTSSDLLTLTSNLETV 172
Cdd:PLN02939 185 RIKLAAQEKIHVEILE-----EQLEKLRNELLIRGATEGLCVHSLSK-------ELDVLKEENMLLKDDIQFLKAELIEV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 173 KKQLE----LEKQKTLKEKKRADMESAKARDQmklaEDVSKkfeivrarneelkkemesqtaSSQVKFAENSEKLEEKIR 248
Cdd:PLN02939 253 AETEErvfkLEKERSLLDASLRELESKFIVAQ----EDVSK---------------------LSPLQYDCWWEKVENLQD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 249 LLemnkktamdwksrtDDLTQQLQEAQLVAEG---LKKQVHELSLSQKSIKTHSISPQKVrDLEKAEMRLLKKkmKFERN 325
Cdd:PLN02939 308 LL--------------DRATNQVEKAALVLDQnqdLRDKVDKLEASLKEANVSKFSSYKV-ELLQQKLKLLEE--RLQAS 370
|
330 340
....*....|....*....|....*....
gi 330253927 326 CAKHSQTVAKFEKFRREFQcEELGRLKLE 354
Cdd:PLN02939 371 DHEIHSYIQLYQESIKEFQ-DTLSKLKEE 398
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
174-384 |
1.43e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 174 KQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKfeivRARNEELKKEMESQTASSQVKFAENSEKLEEKIrllEMN 253
Cdd:PRK09510 104 KQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAK----AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEA---EAA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 254 KKTAMDWKSRTDDLTQQ--LQEAQLVAEGLKKQVHELSLSQKSIKthsispQKVRDLEKAEMrllKKKMKFERNCAKhsq 331
Cdd:PRK09510 177 KKAAAEAKKKAEAEAAAkaAAEAKKKAEAEAKKKAAAEAKKKAAA------EAKAAAAKAAA---EAKAAAEKAAAA--- 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 330253927 332 tvAKFEKFRREFQCEELGRLkleFGSLTNRMNLLDEYFSTDVEGTAGLGKATG 384
Cdd:PRK09510 245 --KAAEKAAAAKAAAEVDDL---FGGLDSGKNAPKTGGGAKGNGAQGAGAGNG 292
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
15-365 |
1.53e-03 |
|
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: 43.11 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 15 KASLEKEISRLKFEIVSL---QQKLERNLKEKSEETKLLQDQASGR-------EKEINELRDLLKK-----ETLRADSSE 79
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLApdkLKSTESELKKKEKRRDEMLGLAPGRqsiidlkEKEIPELRNKLQKvnrdiQRLKNDIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 80 EER--EHAFKELNKAKALIVKDEEIEQ---DIPEVKREIS-LVKNLLASERQKTESE-RKKAESEKKKADKYLSELEVLR 152
Cdd:TIGR00606 770 QETllGTIMPEEESAKVCLTDVTIMERfqmELKDVERKIAqQAAKLQGSDLDRTVQQvNQEKQEKQHELDTVVSKIELNR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 153 NSAHKTSSDLLTLTSNLETVK-------------KQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEivrARNE 219
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKseklqigtnlqrrQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ---QEKE 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 220 ELKKEMESQTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSRtddltqQLQEAQLVAEGLKKQVHELSLSQKSIKTHS 299
Cdd:TIGR00606 927 ELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDD------YLKQKETELNTVNAQLEECEKHQEKINEDM 1000
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253927 300 ISPQKVRDLEKAEMRLLKKK---MKFERNCAKHSQTVAKFEKFRREFQCEElgrLKLEFGSLTNRMNLL 365
Cdd:TIGR00606 1001 RLMRQDIDTQKIQERWLQDNltlRKRENELKEVEEELKQHLKEMGQMQVLQ---MKQEHQKLEENIDLI 1066
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
39-341 |
1.75e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 39 NLKEKSEETKLLQDQASGREKEINELRdllkketlradsseEEREHAFKELNKAKAlivKDEEIEQDIPEVKREISLVKN 118
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELK--------------EKRDELNEELKELAE---KRDELNAQVKELREEAQELRE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 119 L---LASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNLETVKKQLE-----LEKQKTLKEKKRA 190
Cdd:COG1340 65 KrdeLNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlsPEEEKELVEKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 191 DMESAKARDQmklAEDVSKKFEIVRARNEELKKEMEsqTASSQVK-FAENSEKLEEKIRLLemnKKTAMDWKSRTDDLTQ 269
Cdd:COG1340 145 LEKELEKAKK---ALEKNEKLKELRAELKELRKEAE--EIHKKIKeLAEEAQELHEEMIEL---YKEADELRKEADELHK 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 330253927 270 QLQEAQLVAEGLKKQVHELSlsqksikthsispQKVRDLEKAEMRLLKKKMKFERNCAKHS---QTVAKFEKFRR 341
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQ-------------KELRELRKELKKLRKKQRALKREKEKEEleeKAEEIFEKLKK 278
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
7-200 |
1.93e-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: 42.40 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 7 TKENGSTVKASL---EKEISRLKFEIVSLQQKLE---RNLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEE 80
Cdd:pfam05483 571 SEENARSIEYEVlkkEKQMKILENKCNNLKKQIEnknKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 81 ---------EREHAFKELNKAKALivkdEEIEQDIPEVKREISLVKNLLASERQKTESERKKAESEKKKADKYL----SE 147
Cdd:pfam05483 651 kfeeiidnyQKEIEDKKISEEKLL----EEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIeerdSE 726
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 148 LEVLRNSAHKTSS-------DLLTLTSNLETVKKQLELEKQKTLKEKKRADMESAKARDQ 200
Cdd:pfam05483 727 LGLYKNKEQEQSSakaaleiELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
17-325 |
2.14e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 17 SLEKEISRLKFEIVSLQQKLERNLKEkseetklLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNKAKAli 96
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDE-------LNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 97 vKDEEIEQDIPEVKREISLVKNLLASERQKTESErkkaesekkkaDKYLSELEVLRNSahktssdlltltsnLETvkKQL 176
Cdd:COG1340 79 -ERDELNEKLNELREELDELRKELAELNKAGGSI-----------DKLRKEIERLEWR--------------QQT--EVL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 177 ELEKQKTLKEKKRADMESAKARDQmklAEDVSKKFEIVRARNEELKKEMEsqTASSQVK-FAENSEKLEEKIRLLemnKK 255
Cdd:COG1340 131 SPEEEKELVEKIKELEKELEKAKK---ALEKNEKLKELRAELKELRKEAE--EIHKKIKeLAEEAQELHEEMIEL---YK 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253927 256 TAMDWKSRTDDLTQQLQEAQLVAEGLKKQ-------VHELSLSQKSIKTHSISPQKVRDLEKAEMRLLKKKMKFERN 325
Cdd:COG1340 203 EADELRKEADELHKEIVEAQEKADELHEEiielqkeLRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKG 279
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
9-344 |
2.58e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 9 ENGSTVKASLEKEISRLKFEivSLQQKLERNLKEKSEETKLLQdqasGRekeINELRDLLkkETLRADSSeeerehafke 88
Cdd:pfam15921 197 EEASGKKIYEHDSMSTMHFR--SLGSAISKILRELDTEISYLK----GR---IFPVEDQL--EALKSESQ---------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 89 lNKAKALIVKDEE-IEQDIPEVKREISLVKNLLASERQKTESERkkaesekkkadkylSELEVLRNSAHKTSSDLLTLTS 167
Cdd:pfam15921 256 -NKIELLLQQHQDrIEQLISEHEVEITGLTEKASSARSQANSIQ--------------SQLEIIQEQARNQNSMYMRQLS 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 168 NLETVKKQL--ELEKQKTLKEKKRADMESakardQMKLAEDvskkfEIVRARNEELKKEMESQTASSQV-KFAENSEKLE 244
Cdd:pfam15921 321 DLESTVSQLrsELREAKRMYEDKIEELEK-----QLVLANS-----ELTEARTERDQFSQESGNLDDQLqKLLADLHKRE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 245 EKIRL-LEMNKK----------TAMDWKSRTDDLTQQLQEAQLVAEGLKKQVH-ELSLSQKSIKTHSISPQKVRD----- 307
Cdd:pfam15921 391 KELSLeKEQNKRlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKVSSltaql 470
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 330253927 308 ------LEKAEMRLLKKKMKFERNCAKHSQTVAKFEKFRREFQ 344
Cdd:pfam15921 471 estkemLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIE 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
79-288 |
3.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 79 EEEREHAFKELNKAKALIVKDEEIEQDIPEVKREISLVKNLLASERQKTESERKkaesekkkadkyLSELEVLRNSAHKT 158
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE------------IAELEAELERLDAS 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 159 SSDLLTLTSNLETVKKQL--------ELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTA 230
Cdd:COG4913 684 SDDLAALEEQLEELEAELeeleeeldELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253927 231 SSQVK--FAENSEKLEEKIRLLEMNKKTAM-----DWKSRTDDLTQQLQEA--------QLVAEGLKKQVHEL 288
Cdd:COG4913 764 ERELRenLEERIDALRARLNRAEEELERAMrafnrEWPAETADLDADLESLpeylalldRLEEDGLPEYEERF 836
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
15-288 |
3.89e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 15 KASLEKEISRLKFEIVSLQQ-KLERNLKEKSEETKL--LQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNK 91
Cdd:pfam01576 379 KQALESENAELQAELRTLQQaKQDSEHKRKKLEGQLqeLQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIK 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 92 AKALIVKDEEIEQDIPEVKREISLVKNLLASERQKTESERKK-------AESEKKKADKYLSELEV-LRNSAHKTSSDLL 163
Cdd:pfam01576 459 LSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSlqeqleeEEEAKRNVERQLSTLQAqLSDMKKKLEEDAG 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 164 TLTSNLETVKK-QLELE-KQKTLKEKKRA--DMESAKAR-----------------------------DQMkLAED--VS 208
Cdd:pfam01576 539 TLEALEEGKKRlQRELEaLTQQLEEKAAAydKLEKTKNRlqqelddllvdldhqrqlvsnlekkqkkfDQM-LAEEkaIS 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 209 KKFEIVRARNEELKKEMESQTASSQVKFAENSEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHEL 288
Cdd:pfam01576 618 ARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEM 697
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
174-287 |
4.22e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 40.07 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 174 KQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTASSQVKFAENSEKLEEKIRLLE-- 251
Cdd:pfam13904 68 RQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVLQew 147
|
90 100 110
....*....|....*....|....*....|....*.
gi 330253927 252 MNKKTAMDWKSRTDDLTQQLQEAQLVAEglKKQVHE 287
Cdd:pfam13904 148 ERKKLEQQQRKREEEQREQLKKEEEEQE--RKQLAE 181
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
34-218 |
5.30e-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: 39.91 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 34 QKLERNLKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFKELNKAKALIVKDEEieqDIPEVK--R 111
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE---QLGNVRnnK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 112 EI-SLVKNLLASERQKTESErkkaesekkkaDKYLS---ELEVLRNSAHKTSSDLLTLTSNLETVKKQLELEKQKTLKEK 187
Cdd:COG1579 90 EYeALQKEIESLKRRISDLE-----------DEILElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170 180 190
....*....|....*....|....*....|.
gi 330253927 188 KRADMESAKARDqmKLAEDVSKKFEIVRARN 218
Cdd:COG1579 159 EELEAEREELAA--KIPPELLALYERIRKRK 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
17-321 |
6.44e-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: 6.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 17 SLEKEISRLKFEIVSLQQKLERN--------LKEKSEETKLLQDQASGREKEINELRDLLKKetLRADSSEEEREhafke 88
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLNNQKEQDwnkelkseLKNQEKKLEEIQNQISQNNKIISQLNEQISQ--LKKELTNSESE----- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 89 lnkakalivkDEEIEQDIPEVKREISLVKNllaserqkteserkkaesekkKADKYLSELEVLRNSAHKTSSDLLT---L 165
Cdd:TIGR04523 358 ----------NSEKQRELEEKQNEIEKLKK---------------------ENQSYKQEIKNLESQINDLESKIQNqekL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 166 TSNLETVKKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKKFEIVRARNEELKKEMESQTASSQVKFAENSEKLEE 245
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQ 486
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253927 246 KIRLLEMNKKTAMDWKSRTDDLTQQLQEAQLVAEGLKKQVHELSlSQKSIKTHSISpQKVRDLEKAEMRLLKKKMK 321
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE-SEKKEKESKIS-DLEDELNKDDFELKKENLE 560
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
16-210 |
6.58e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 16 ASLEKEISRLKFEIVSLQQKLErNLKEKSEEtklLQDQASGREKEINELRDLLKKetlRADSSEEErehafKELNKAKAL 95
Cdd:COG3883 40 DALQAELEELNEEYNELQAELE-ALQAEIDK---LQAEIAEAEAEIEERREELGE---RARALYRS-----GGSVSYLDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 96 IVKDEEIEQDIpevkREISLVKNLLASER---QKTESERKKAESEKKKADKYLSELEVLRNSAHKTSSDLLTLTSNLETV 172
Cdd:COG3883 108 LLGSESFSDFL----DRLSALSKIADADAdllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 330253927 173 KKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSKK 210
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-341 |
7.22e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 9 ENGSTVKASLEKEISRLKFEIVSlqqklERNLKEKSEETKLLQDQASGREKEINElrdllkKETLRADSSEEEREHAFKE 88
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNH-----EGKAEAKAHVGQDEGLKPSYKDFDFDA------KEDNRADEATEEAFGKAEE 1102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 89 LNKAKALIVKDEEIEQDIPEVKREISLVKNLLASERQKTESERKKAE-SEKKKADKYLSELEVLRNSAHKTSSDLLTLTS 167
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEdAKRVEIARKAEDARKAEEARKAEDAKKAEAAR 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 168 NLETVKKQLELEKQ---KTLKEKKRAD----------MESAKARDQMKLAEDVSKKFEIVRA-----RNEELKKEMESQT 229
Cdd:PTZ00121 1183 KAEEVRKAEELRKAedaRKAEAARKAEeerkaeearkAEDAKKAEAVKKAEEAKKDAEEAKKaeeerNNEEIRKFEEARM 1262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 230 A----------------------SSQVKFAENSEKLEEKIRLLEMNKKTamDWKSRTDDLTQQLQEAQLVAEGLKKQVHE 287
Cdd:PTZ00121 1263 AhfarrqaaikaeearkadelkkAEEKKKADEAKKAEEKKKADEAKKKA--EEAKKADEAKKKAEEAKKKADAAKKKAEE 1340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 330253927 288 LSLSQKSIKTHsiSPQKVRDLEKAEMRLLKKKMKFERNCAKHSQTVAKFEKFRR 341
Cdd:PTZ00121 1341 AKKAAEAAKAE--AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK 1392
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
12-354 |
7.38e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 12 STVKASL---EKEISRLKFEIVSLQQKLERNLKE----KSEETKL---------LQDQASGREKEINELRD-------LL 68
Cdd:pfam15921 499 SDLTASLqekERAIEATNAEITKLRSRVDLKLQElqhlKNEGDHLrnvqteceaLKLQMAEKDKVIEILRQqienmtqLV 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 69 KKETLRADSSEEEREHAFKELNKAKaLIVKDEEIEQDIPEVK-REISLVKNLLASERQK---TESERKKAESE-KKKADK 143
Cdd:pfam15921 579 GQHGRTAGAMQVEKAQLEKEINDRR-LELQEFKILKDKKDAKiRELEARVSDLELEKVKlvnAGSERLRAVKDiKQERDQ 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 144 YLSELEVLRNSAHKTSSDLLTLTSNLETVKKQLELEKQKTLKEKKRADMESAKARDQMKLAEDVSkkfeivrARNEELKK 223
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSD-------GHAMKVAM 730
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 224 EMESQTASSQVKFaensEKLEEKIRLLEMNKKTAMDWKSRTDDLTQQL-QEAQLVAEGLKKQVHELSLsqksikthsisp 302
Cdd:pfam15921 731 GMQKQITAKRGQI----DALQSKIQFLEEAMTNANKEKHFLKEEKNKLsQELSTVATEKNKMAGELEV------------ 794
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 330253927 303 qkvrdLEKAEMRLLKKKMKFERNCAKHSQTVAKFEKFRREfQCEELGRLKLE 354
Cdd:pfam15921 795 -----LRSQERRLKEKVANMEVALDKASLQFAECQDIIQR-QEQESVRLKLQ 840
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
8-246 |
8.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 8 KENGSTVKASLEKEISRLKFEIVSLQQKLERNlKEKSEETKLLQDQASGREKEINELRDLLKKETLRADSSEEEREHAFK 87
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE-KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 88 ELNKAKALIVKDEEIEQDIPEVKREISLVKNLLASERQKTESERKKAESEKKKADKYLSELEVLRNSAHKTSsdlltlts 167
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK-------- 1764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253927 168 nlETVKKQLELEKQKTLKEKKRADMESAKARDQM-KLAEDVSKKFEIVRARNEE------LKKEMESqTASSQVKFAENS 240
Cdd:PTZ00121 1765 --EEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVdKKIKDIFDNFANIIEGGKEgnlvinDSKEMED-SAIKEVADSKNM 1841
|
....*.
gi 330253927 241 EKLEEK 246
Cdd:PTZ00121 1842 QLEEAD 1847
|
|
| |
