|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-325 |
1.37e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 3 EQLDKTLARVVEGWNRHEAERTEvLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEE 82
Cdd:COG1196 239 AELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 83 RQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQ 162
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 163 REAQAAWETQQQFAL------LQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEA 236
Cdd:COG1196 398 LAAQLEELEEAEEALlerlerLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 237 QENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQ--DYELRLAREQARVRDLKSGNQQLEE 314
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgvEAAYEAALEAALAAALQNIVVEDDE 557
|
330
....*....|.
gi 26331630 315 QRAELVERLQA 325
Cdd:COG1196 558 VAAAAIEYLKA 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
20-342 |
4.38e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 20 EAERTEVLRGLQEERQAAE-----LTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQ 94
Cdd:COG1196 208 QAEKAERYRELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 95 QQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQawikQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQ 174
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEE----ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 175 FALLQTEVRRLEGDLDTVRRERDALQLEMS--LVQARYESQRIQMESELAVQLEQRVTERLAEAQEnsLRQAASLRDHHR 252
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRaaAELAAQLEELEEAEEALLERLERLEEELEELEEA--LAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 253 KQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKsgnqqLEEQRAELVERLQAMLQAHWE 332
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL-----LLEAEADYEGFLEGVKAALLL 516
|
330
....*....|
gi 26331630 333 EANQLLSTTL 342
Cdd:COG1196 517 AGLRGLAGAV 526
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-337 |
2.11e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 30 LQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQA----LTLRLEVEQQQCRTLQEERD 105
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELelalLVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 106 EARagqlSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAqaawETQQQFALLQTEVRRL 185
Cdd:TIGR02168 250 EAE----EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ----ILRERLANLERQLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 186 EGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQleqrvtERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQE 265
Cdd:TIGR02168 322 EAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL------EELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26331630 266 --LAAQLAQFKVEMADREERQQQVAQDYE-LRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQL 337
Cdd:TIGR02168 396 asLNNEIERLEARLERLEDRRERLQQEIEeLLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
82-343 |
2.26e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 82 ERQALTLRLEVEQ-QQCRTLQEERDEARAGQLSEHRKLEALQVALQEERqawIKQEHQLKERLQALQEEGQAQLEREKGN 160
Cdd:COG1196 199 ERQLEPLERQAEKaERYRELKEELKELEAELLLLKLRELEAELEELEAE---LEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 161 SQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDAL-----QLEMSLVQARYESQRIQMESELAVQLEQRVTERLAE 235
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerleELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 236 AQENSLRQAASLRDHHRKQLQELSGQHQ-QELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEE 314
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEElAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260
....*....|....*....|....*....
gi 26331630 315 QRAELVERLQAMLQAHWEEANQLLSTTLL 343
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-342 |
6.38e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 54 SLSEAMEALSREQEGARLQQrEKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAwI 133
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-V 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 134 KQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQ 213
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 214 RIQMESEL--AVQLEQRVTERLAEAQENSLRQAASlrDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERqqqvaqdy 291
Cdd:TIGR02168 823 RERLESLErrIAATERRLEDLEEQIEELSEDIESL--AAEIEELEELIEELESELEALLNERASLEEALALL-------- 892
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 26331630 292 ELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMlQAHWEEANQLLSTTL 342
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQL-ELRLEGLEVRIDNLQ 942
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
22-326 |
4.76e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 22 ERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQ 101
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 102 EERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQ----------LKERLQALQEEgqaqLEREKGNSQREAQAAWET 171
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQieqlkeelkaLREALDELRAE----LTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 172 QQQFALLQTEVRRLEGDLDTVRRERDALQLEMslvqARYESQRIQMESELAVQLEQR-VTERLAEAQENSLRQAASLRDH 250
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEI----EELEELIEELESELEALLNERaSLEEALALLRSELEELSEELRE 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 251 HRKQLQELSGQHqQELAAQLAQFKVEMA----DREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAM 326
Cdd:TIGR02168 906 LESKRSELRREL-EELREKLAQLELRLEglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-322 |
6.91e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.94 E-value: 6.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEGWNRHEAERTEVLRGLQEERQAAElTRSKQQETVTRLEQSLSEAMEALSREQEGArlqQREKEALEE 81
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIG-EIEKEIEQLEQEEEKLKERLEELEEDLSSL---EQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 82 ERQALTLRLEVEQQQCRTLQEERD--EARAGQlSEHRKLEALQVALQEERQAW----------IKQEHQLKERLQALQEE 149
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALNdlEARLSH-SRIPEIQAELSKLEEEVSRIearlreieqkLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 150 GQAQLE--REKGNSQREAQAAW-----ETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMEsela 222
Cdd:TIGR02169 838 LQEQRIdlKEQIKSIEKEIENLngkkeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE---- 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 223 vQLEQRVtERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQE-LAAQLAQFKVEMADREERQQQVAQDYElrlaREQAR 301
Cdd:TIGR02169 914 -KKRKRL-SELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEdVQAELQRVEEEIRALEPVNMLAIQEYE----EVLKR 987
|
330 340
....*....|....*....|.
gi 26331630 302 VRDLKSGNQQLEEQRAELVER 322
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAILER 1008
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-313 |
2.20e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.39 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLArvVEGWNRHEAERTEvlrgLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEE 81
Cdd:TIGR02168 222 LRELELALL--VLRLEELREELEE----LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 82 ERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEalqvALQEERQAWIKQEHQLKERLQALQEEGQaqlerEKGNS 161
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLD----ELAEELAELEEKLEELKEELESLEAELE-----ELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 162 QREAQAAWETQQQfallqtevrrlegDLDTVRRERDALQLEMSLVQARYESQRIQMES--ELAVQLEQRVTERLAEAQEN 239
Cdd:TIGR02168 367 LEELESRLEELEE-------------QLETLRSKVAQLELQIASLNNEIERLEARLERleDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26331630 240 SLRQAASLRDHHRKQLQELSGQHqqelaAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLE 313
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEEL-----ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-223 |
4.70e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.09 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 3 EQLDkTLARVVEGWNRHEAERTEvLRGLQEERQAAELTRSKQ-----QETVTRLEQSLSEAMEALSREQEGARLQQREKE 77
Cdd:COG4913 249 EQIE-LLEPIRELAERYAAARER-LAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 78 ALEEERQALTL-RLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQler 156
Cdd:COG4913 327 ELEAQIRGNGGdRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEAL--- 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26331630 157 ekgnsqreaqaawetQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAV 223
Cdd:COG4913 404 ---------------EEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGL 455
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-258 |
5.41e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALE- 80
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEa 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 81 ------EERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLK------ERLQALQE 148
Cdd:TIGR02168 790 qieqlkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaeiEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 149 EGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARY---ESQRIQMESELAV-- 223
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLeglEVRIDNLQERLSEey 949
|
250 260 270
....*....|....*....|....*....|....*
gi 26331630 224 QLEQRVTERLAEAQENSLRQAASLRDHHRKQLQEL 258
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
44-283 |
8.99e-11 |
|
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: 64.01 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 44 QQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARagqlsehRKLEALQV 123
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE-------AELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 124 ALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWetqqQFALLQTEVRRLEGDLDTVRRERDALQlem 203
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVR----RLQYLKYLAPARREQAEELRADLAELA--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 204 sLVQARYESQRIQMESELAVQLEQRVT-ERLAEAQENSLRQAASLRDHHRKQLQELSGQhQQELAAQLAQFKVEMADREE 282
Cdd:COG4942 164 -ALRAELEAERAELEALLAELEEERAAlEALKAERQKLLARLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
.
gi 26331630 283 R 283
Cdd:COG4942 242 R 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
17-337 |
2.63e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 17 NRHEAERTEV---LRGLQEERQAAELTRSKQQETVTRLEQSLsEAMEALsrEQEGARLQQrEKEALEEERQALTLRLEVE 93
Cdd:PRK02224 209 NGLESELAELdeeIERYEEQREQARETRDEADEVLEEHEERR-EELETL--EAEIEDLRE-TIAETEREREELAEEVRDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 94 QQQCRTLQEERDEARAGQLSEhrklEALQVALQEERQAWIKQEHQLKERLQALQEEGQA---QLEREKGNSQREAQAAWE 170
Cdd:PRK02224 285 RERLEELEEERDDLLAEAGLD----DADAEAVEARREELEDRDEELRDRLEECRVAAQAhneEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 171 TQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQME-----SELAVQLEQRVTERLAEAQ------EN 239
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGnaedfLEELREERDELREREAELEatlrtaRE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 240 SLRQAASLRDH--------------HRKQLQELSGQhQQELAAQLAQFKVEMADREERQQQVAQDYElrLAREQARVRDL 305
Cdd:PRK02224 441 RVEEAEALLEAgkcpecgqpvegspHVETIEEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVE--AEDRIERLEER 517
|
330 340 350
....*....|....*....|....*....|..
gi 26331630 306 KSGNQQLEEQRAELVERLQAMLQAHWEEANQL 337
Cdd:PRK02224 518 REDLEELIAERRETIEEKRERAEELRERAAEL 549
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
102-328 |
3.31e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 102 EERD-EARAGQLSEH-RKLEALQVALQEERQawikQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQ 179
Cdd:COG4913 219 EEPDtFEAADALVEHfDDLERAHEALEDARE----QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 180 TEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQrvterlAEAQENSLRQAASLRDHHRKQLQELS 259
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ------LEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26331630 260 GQHQQELAAQLAQFkvemADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQ 328
Cdd:COG4913 369 AALGLPLPASAEEF----AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
20-336 |
3.74e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 20 EAERTEVLRGLQEERQAAELTRSKQQETvtrleqslSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQ---- 95
Cdd:PTZ00121 1442 EAKKADEAKKKAEEAKKAEEAKKKAEEA--------KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkad 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 96 QCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAwetqqqf 175
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA------- 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 176 alLQTEVRRLEGDLDTVRRERdalqlEMSLVQARY-ESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRdhhrkQ 254
Cdd:PTZ00121 1587 --KKAEEARIEEVMKLYEEEK-----KMKAEEAKKaEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK-----K 1654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 255 LQELSGQHQQELA--AQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQlEEQRAELVERLQAMLQAHWE 332
Cdd:PTZ00121 1655 AEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE-EKKKAEELKKAEEENKIKAE 1733
|
....
gi 26331630 333 EANQ 336
Cdd:PTZ00121 1734 EAKK 1737
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
5-337 |
6.82e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 5 LDKTLARVVEGWNRHEAERTEVLRG---LQEERQAAELTRSKQQETVTR--------------LEQSLSEAMEALSREQE 67
Cdd:PRK04863 263 ITESTNYVAADYMRHANERRVHLEEaleLRRELYTSRRQLAAEQYRLVEmarelaelneaesdLEQDYQAASDHLNLVQT 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 68 GARLQQREKEAlEEERQALTLRLEVEQQQCRTLQEERDEARA-------------GQLSEH-RKLEALQ---------VA 124
Cdd:PRK04863 343 ALRQQEKIERY-QADLEELEERLEEQNEVVEEADEQQEENEAraeaaeeevdelkSQLADYqQALDVQQtraiqyqqaVQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 125 LQEERQAWIKQEHQLKERLQALQEEGQAQLE------REKGNSQREAQAAwetQQQFALLQTEVRRLEGDLDTVRRERDA 198
Cdd:PRK04863 422 ALERAKQLCGLPDLTADNAEDWLEEFQAKEQeateelLSLEQKLSVAQAA---HSQFEQAYQLVRKIAGEVSRSEAWDVA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 199 LQLEmslvqARYESQRIQmeselAVQLEQRvterlaEAQENSLRQAASLRDHHRKQLQELSGQHQQEL--AAQLAQFKVE 276
Cdd:PRK04863 499 RELL-----RRLREQRHL-----AEQLQQL------RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLddEDELEQLQEE 562
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26331630 277 M-ADREERQQQVAQDYELRLAREQARvrdlksgnQQLEEQRAELVERLQAMLQAHwEEANQL 337
Cdd:PRK04863 563 LeARLESLSESVSEARERRMALRQQL--------EQLQARIQRLAARAPAWLAAQ-DALARL 615
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-326 |
8.97e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEE 81
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 82 ERQALTLRLEVEQQQ-------------------CRTLQEER-DEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKE 141
Cdd:COG1196 489 AAARLLLLLEAEADYegflegvkaalllaglrglAGAVAVLIgVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKA 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 142 RL--------------QALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEV------------RRLEGDLDTVRRE 195
Cdd:COG1196 569 AKagratflpldkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLgrtlvaarleaaLRRAVTLAGRLRE 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 196 RDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKV 275
Cdd:COG1196 649 VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEE 728
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 26331630 276 EMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAM 326
Cdd:COG1196 729 QLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
22-374 |
1.62e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.91 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 22 ERTEVLRGLQE-ERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEgarlqqreKEALEEERQALTLRLEveqQQCRTL 100
Cdd:pfam17380 294 EKMEQERLRQEkEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQE--------RMAMERERELERIRQE---ERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 101 QEERDEARAGQLSEHRKLEALQValqeERQawiKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQT 180
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQM----ERQ---QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 181 EVRRLEGDldtvrRERdalqlEMSLVQARYESQRIQMEsELAVQLEQRVTERLAEAQENSLRQAAslRDHHRKQLQELSG 260
Cdd:pfam17380 436 EVRRLEEE-----RAR-----EMERVRLEEQERQQQVE-RLRQQEEERKRKKLELEKEKRDRKRA--EEQRRKILEKELE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 261 QHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVE---RLQAMlqahwEEANQL 337
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEersRLEAM-----EREREM 577
|
330 340 350
....*....|....*....|....*....|....*..
gi 26331630 338 LSTTLLPPNPQAPLAEPSSPGPLEPEKGERRTWAMPP 374
Cdd:pfam17380 578 MRQIVESEKARAEYEATTPITTIKPIYRPRISEYQPP 614
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
18-339 |
2.72e-09 |
|
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: 60.37 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 18 RHEAERTEVLRGLQEERQAAELtrskqQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQC 97
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEAL-----KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 98 ---RTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQ---LKERLQALQEEGQAQLEREKGNSQREA----QA 167
Cdd:pfam02463 229 ldyLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKenkEEEKEKKLQEEELKLLAKEEEELKSELlkleRR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 168 AWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQL--EQRVTERLAEAQENSLRQAA 245
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEklEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 246 SLRDHHRKQLQELSGQHQQELAAQLAQfKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQA 325
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELAR-QLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330
....*....|....
gi 26331630 326 MLQAHWEEANQLLS 339
Cdd:pfam02463 468 KKSEDLLKETQLVK 481
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
19-337 |
9.22e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.81 E-value: 9.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 19 HEAERTEVLRGLQEERQAAELTR---SKQQETVTRLEQSLSEAMEALSREQEGARLQ---QREKEALEEerqaLTLRLEV 92
Cdd:COG3096 290 LRRELFGARRQLAEEQYRLVEMArelEELSARESDLEQDYQAASDHLNLVQTALRQQekiERYQEDLEE----LTERLEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 93 EQQQCRTLQEERDEARA-------------GQLSEH-RKLEALQ---VALQEERQAWIKQEHQL----------KERLQA 145
Cdd:COG3096 366 QEEVVEEAAEQLAEAEArleaaeeevdslkSQLADYqQALDVQQtraIQYQQAVQALEKARALCglpdltpenaEDYLAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 146 LQEEGQAQLEREKGNSQREAQAAwETQQQFALLQTEVRRLEGDLDTVRRERDALQLemslvQARYESQRIQMESELAVQL 225
Cdd:COG3096 446 FRAKEQQATEEVLELEQKLSVAD-AARRQFEKAYELVCKIAGEVERSQAWQTAREL-----LRRYRSQQALAQRLQQLRA 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 226 EQRVTERLAEAQENSLRQAASLRDHHRKQLqelsgQHQQELAAQLAQFKvemADREERQQQVAQDYELRLAREQARvrdl 305
Cdd:COG3096 520 QLAELEQRLRQQQNAERLLEEFCQRIGQQL-----DAAEELEELLAELE---AQLEELEEQAAEAVEQRSELRQQL---- 587
|
330 340 350
....*....|....*....|....*....|..
gi 26331630 306 ksgnQQLEEQRAELVERLQAMLQAHwEEANQL 337
Cdd:COG3096 588 ----EQLRARIKELAARAPAWLAAQ-DALERL 614
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
18-268 |
1.60e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.83 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 18 RHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQ-----REKEALEEERQALTLRLEV 92
Cdd:pfam17380 341 RMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeleaaRKVKILEEERQRKIQQQKV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 93 EQQQCRTLQEERDEARAGQLSEHRKLEALQVALQE-ERQAWIKQEHQlkerlqalQEEGQAQLEREKGNSQREAQAAWET 171
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEqERQQQVERLRQ--------QEEERKRKKLELEKEKRDRKRAEEQ 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 172 QQQfaLLQTEVRRLEGDLDTVRRERDALQLEMSLVQARY--ESQRIQMESELAVQLE----QRVTERLAEAQENSLRQAA 245
Cdd:pfam17380 493 RRK--ILEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEmeerRRIQEQMRKATEERSRLEA 570
|
250 260
....*....|....*....|...
gi 26331630 246 SLRDHHRKQLQELSGQHQQELAA 268
Cdd:pfam17380 571 MEREREMMRQIVESEKARAEYEA 593
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
73-325 |
3.19e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 3.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 73 QREKEALEEERQALTLRLEVEQQQCRTLQEERDEARagqlsehRKLEALQvALQEERQAWIKQEhQLKERLQALQEEgQA 152
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------ERREALQ-RLAEYSWDEIDVA-SAEREIAELEAE-LE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 153 QLErekgnsqreaqaawETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQ----------MESELA 222
Cdd:COG4913 679 RLD--------------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEldelqdrleaAEDLAR 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 223 VQLEQRVTERLAEA-QENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFK-----------VEMADREERQQQVAQD 290
Cdd:COG4913 745 LELRALLEERFAAAlGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpaetadldADLESLPEYLALLDRL 824
|
250 260 270
....*....|....*....|....*....|....*
gi 26331630 291 YELRLAREQARVRDLKsgNQQLEEQRAELVERLQA 325
Cdd:COG4913 825 EEDGLPEYEERFKELL--NENSIEFVADLLSKLRR 857
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
18-225 |
7.06e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.90 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 18 RHEAERTEVLRGLQEERQAAELTRSKQQETVtRLEQSLSEAMEALSREQEGARLQQR-EKEALEEERQALTLRLEVEQQQ 96
Cdd:pfam17380 395 RQELEAARKVKILEEERQRKIQQQKVEMEQI-RAEQEEARQREVRRLEEERAREMERvRLEEQERQQQVERLRQQEEERK 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 97 CRTLQEERDEaRAGQLSEHRKLEALQVALQEERQAWIKQ-------EHQLKERLQALQEEGQAQLEREKGNSQREAQAAW 169
Cdd:pfam17380 474 RKKLELEKEK-RDRKRAEEQRRKILEKELEERKQAMIEEerkrkllEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 26331630 170 ETQQQFALLQTEVRRLEgdldtvrrerdALQLEMSLVQARYESQRIQMESELAVQL 225
Cdd:pfam17380 553 RIQEQMRKATEERSRLE-----------AMEREREMMRQIVESEKARAEYEATTPI 597
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3-337 |
1.30e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.23 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 3 EQLDKTLARVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLE----QSLSEAMEALSREQEGARLQQREKEA 78
Cdd:pfam12128 279 EERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdqhgAFLDADIETAAADQEQLPSWQSELEN 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 79 LEEERQALT------------LRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQAL 146
Cdd:pfam12128 359 LEERLKALTgkhqdvtakynrRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 147 QEEGQAQLEREKGNsQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLE 226
Cdd:pfam12128 439 EYRLKSRLGELKLR-LNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEE 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 227 QRvtERLAEAQENSLRQAASLRDHHRKQLQELSgQHQQELA--AQLAQFKVEMADREERQQQVAQDYELRLAREQARVRD 304
Cdd:pfam12128 518 RQ--SALDELELQLFPQAGTLLHFLRKEAPDWE-QSIGKVIspELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPE 594
|
330 340 350
....*....|....*....|....*....|...
gi 26331630 305 LKSGNQQLEEQRAELVERLQAMLQAHWEEANQL 337
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
14-322 |
1.50e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 14 EGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSE---AMEALSREQEGARLQQREKEALEEERQALTLRL 90
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKKAAAAKKKADEAKK 1425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 91 EVEQ-QQCRTLQEERDEARAG-----QLSEHRKLEALQVALQEERQAwikQEHQLKERLQALQEEGQAQLEREKGNSQRE 164
Cdd:PTZ00121 1426 KAEEkKKADEAKKKAEEAKKAdeakkKAEEAKKAEEAKKKAEEAKKA---DEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 165 AQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSlvQARYESQRIQMESELAVQLEQRVTERLAEAQEN---SL 241
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDknmAL 1580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 242 RQAASLRDHHRKQLQELSGQHQQELA--------AQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLE 313
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKmkaeeakkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
....*....
gi 26331630 314 EQRAELVER 322
Cdd:PTZ00121 1661 IKAAEEAKK 1669
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
116-325 |
1.61e-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: 54.00 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 116 RKLEALQVALQEERQAWIKQEHQLKERLQALQeegqaQLEREKGNSQREAQaawETQQQFALLQTEVRRLEGDLDTVRRE 195
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLA-----ALERRIAALARRIR---ALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 196 RDALQLEMS-LVQARYESQRIQ-----MESELAVQLEQRVT--ERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQ--E 265
Cdd:COG4942 99 LEAQKEELAeLLRALYRLGRQPplallLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEleA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 266 LAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQA 325
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
21-325 |
1.79e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 21 AERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTL-RLEVEQQQCR- 98
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARALCGLpDLTPENAEDYl 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 99 -TLQEERDEARAGQLSEHRKLEALQVALQEERQAWikqehQLKERLQALQEEGQA-QLEREKGNSQREAQAAWETQQQFA 176
Cdd:COG3096 444 aAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-----ELVCKIAGEVERSQAwQTARELLRRYRSQQALAQRLQQLR 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 177 LLQTEVRRLEGDLDTVRRerdaLQLEMSLVQARYESQRIQMESELAVQLEQRvtERLAEAQENSLRQAASLR---DHHRK 253
Cdd:COG3096 519 AQLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAELEAQL--EELEEQAAEAVEQRSELRqqlEQLRA 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 254 QLQELSGQHQQELAAQLA------QFKVEMADREE----RQQQVAQDYELRLAREQARVRdlksgNQQLEEQraelVERL 323
Cdd:COG3096 593 RIKELAARAPAWLAAQDAlerlreQSGEALADSQEvtaaMQQLLEREREATVERDELAAR-----KQALESQ----IERL 663
|
..
gi 26331630 324 QA 325
Cdd:COG3096 664 SQ 665
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
67-345 |
3.21e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 67 EGARLQQREK--EALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEAlqvALQEERQAWIKQEHQLKERLQ 144
Cdd:pfam12128 242 EFTKLQQEFNtlESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDD---QWKEKRDELNGELSAADAAVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 145 ALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEvrrlegdLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQ 224
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSE-------LENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRD 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 225 LEqRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQ----------ELAAQLAQFKVEMAD----REERQQQVAQD 290
Cdd:pfam12128 392 IA-GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAgklefneeeyRLKSRLGELKLRLNQatatPELLLQLENFD 470
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26331630 291 YELRLAREQ-----ARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQL--LSTTLLPP 345
Cdd:pfam12128 471 ERIERAREEqeaanAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALdeLELQLFPQ 532
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
44-333 |
7.83e-07 |
|
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: 52.67 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 44 QQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQA-------LTLRLEVEQQQCRTLQEERDEARAGQLSEHR 116
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEEtenlaelIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 117 KLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNS----QREAQAAWETQQQ-------------FALLQ 179
Cdd:pfam02463 220 ELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEeklaQVLKENKEEEKEKklqeeelkllakeEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 180 TEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELS 259
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26331630 260 GQHQQELAAQLAQFKVEMADREERQQQV-AQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEE 333
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAqLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
33-237 |
8.58e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 33 ERQAAELTRSKQQETVTRLEQslseaMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARagQL 112
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKE-----LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE--KL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 113 SEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTV 192
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 26331630 193 RRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQ 237
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
30-330 |
8.86e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 30 LQEERQAAELTRSKQQETVTRLEQSLSEA---MEALSREQ-------EGARLQQR----EKEAL---------EEERQAL 86
Cdd:pfam12128 602 LRERLDKAEEALQSAREKQAAAEEQLVQAngeLEKASREEtfartalKNARLDLRrlfdEKQSEkdkknkalaERKDSAN 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 87 TLRLEVEQQQCRTLQEERD--EARAGQLSEHR--KLEALQVaLQEERQAwikQEHQLKERLQALQEEGQAQLEREKGNSQ 162
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAwlEEQKEQKREARteKQAYWQV-VEGALDA---QLALLKAAIAARRSGAKAELKALETWYK 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 163 REAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAvQLEQRVTE---RLAEAQEN 239
Cdd:pfam12128 758 RDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLS-NIERAISElqqQLARLIAD 836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 240 SLRQAASL---RDHHRKQLQELSGQHQ--QELAAQLAQFKVEmadreerqqQVAQDYELRLAREQARVRDLKSGNQQLEE 314
Cdd:pfam12128 837 TKLRRAKLemeRKASEKQQVRLSENLRglRCEMSKLATLKED---------ANSEQAQGSIGERLAQLEDLKLKRDYLSE 907
|
330
....*....|....*.
gi 26331630 315 QRAELVERLQAMLQAH 330
Cdd:pfam12128 908 SVKKYVEHFKNVIADH 923
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-199 |
9.83e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 9.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 11 RVVEGWNRHEAERTEVLRGLQEERQA-----------AELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEAL 79
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAeearieevmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 80 EEERQALTLRLEVEQQQCRTLQEER---------DEARAGQLSEHRKLEALQVALQEERQA-----WIKQEHQLKERLQA 145
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKkaeedkkkaEEAKKAEEDEKKAAEALKKEAEEAKKAeelkkKEAEEKKKAEELKK 1723
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 26331630 146 LQEEGQA---QLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDAL 199
Cdd:PTZ00121 1724 AEEENKIkaeEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
166-337 |
1.37e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 166 QAAWETQQQFALLQtEVRRLEGDLDTVRRERDALQLEMSLVQAryesQRIQMESELAVQLEQRVTERLAEAQEnSLRQAA 245
Cdd:COG4913 242 EALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRL----WFAQRRLELLEAELEELRAELARLEA-ELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 246 SLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQdyelRLAREQARVRDLKSGNQQLEEQRAELVERLQA 325
Cdd:COG4913 316 ARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERER----RRARLEALLAALGLPLPASAEEFAALRAEAAA 391
|
170
....*....|..
gi 26331630 326 MLQAHWEEANQL 337
Cdd:COG4913 392 LLEALEEELEAL 403
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
123-329 |
1.44e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 123 VALQEERQAWIKQEHQLKERLQALQEEgQAQLEREKGNSQREAQAAwetQQQFALLQTEVRRLEGDLDTVRRERDALQLE 202
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKE-LAALKKEEKALLKQLAAL---ERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 203 MSLVQARYESQRIQMESELAV--QLEQRVTERLAEAQENSLRQAASLR------DHHRKQLQELSGQHQ--QELAAQLAQ 272
Cdd:COG4942 92 IAELRAELEAQKEELAELLRAlyRLGRQPPLALLLSPEDFLDAVRRLQylkylaPARREQAEELRADLAelAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 273 FKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAEL---VERLQAMLQA 329
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIAR 231
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
27-339 |
2.70e-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: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 27 LRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDE 106
Cdd:pfam01576 133 IKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 107 ARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAwETQQQFALLQTEVRRLE 186
Cdd:pfam01576 213 LEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQIS-ELQEDLESERAARNKAE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 187 GDLDTVRRERDALQLEMSLVQARYESQRiqmesELAVQLEQRVTErLAEAQENSLR----QAASLRDHHRKQLQELSGQH 262
Cdd:pfam01576 292 KQRRDLGEELEALKTELEDTLDTTAAQQ-----ELRSKREQEVTE-LKKALEEETRsheaQLQEMRQKHTQALEELTEQL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 263 QQELAAQLAQFKVEMADREERQ---------QQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAmLQAHWEE 333
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENAelqaelrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK-LQSELES 444
|
....*.
gi 26331630 334 ANQLLS 339
Cdd:pfam01576 445 VSSLLN 450
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
122-325 |
3.95e-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: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 122 QVALQEERQAWIKQEhqLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQL 201
Cdd:TIGR02169 181 EVEENIERLDLIIDE--KRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 202 EMSLVQARYESQRIQMEsELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKqlQELSGQHQQELAAQLAQFKVEMadre 281
Cdd:TIGR02169 259 EISELEKRLEEIEQLLE-ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERS--IAEKERELEDAEERLAKLEAEI---- 331
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 26331630 282 ERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQA 325
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
31-322 |
6.89e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 31 QEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEA--- 107
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAakk 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 108 RAGQL----SEHRKLEALQVALQEERQA-WIKQEHQLKERLQAL----QEEGQAQLEREKGNSQREAQAAWETQQQFALL 178
Cdd:PTZ00121 1419 KADEAkkkaEEKKKADEAKKKAEEAKKAdEAKKKAEEAKKAEEAkkkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK 1498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 179 QTEVRRLE------GDLDTVRRERDALQL----------EMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQEN--- 239
Cdd:PTZ00121 1499 ADEAKKAAeakkkaDEAKKAEEAKKADEAkkaeeakkadEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDknm 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 240 SLRQAASLRDHHRKQLQELSGQHQQElaaqlAQFKVEMADREERQQQVAQdyELRLAREQARVRDLKSGNQQLEEQRAEL 319
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEE-----KKMKAEEAKKAEEAKIKAE--ELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
...
gi 26331630 320 VER 322
Cdd:PTZ00121 1652 LKK 1654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
37-228 |
7.73e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 7.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 37 AELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVE--QQQCRTLQEERDEARAGQLSE 114
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEllEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 115 HRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAW-------ETQQQFALLQTEVRRLEG 187
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAEAAALLE 394
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 26331630 188 DLDTVRRERDALQLEMSLVQARYESQRIQMESELAvQLEQR 228
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIA-SLERR 434
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
127-360 |
1.43e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 127 EERQAWIKQE-HQLKERLQALQEEGQAQLEREKGNSqreaqaaweTQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSL 205
Cdd:COG3206 174 RKALEFLEEQlPELRKELEEAEAALEEFRQKNGLVD---------LSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 206 VQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHH------RKQLQELSGQHQQELAAQLAQFKVEMAD 279
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdvialRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 280 REERQQQVAQdyelRLAREQARVRDLKSGNQQLE--EQRAELVERLQAMLQAHWEEANqlLSTTLLPPN------PQAPL 351
Cdd:COG3206 325 LQAREASLQA----QLAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEEAR--LAEALTVGNvrvidpAVVPL 398
|
....*....
gi 26331630 352 aEPSSPGPL 360
Cdd:COG3206 399 -KPVSPKKL 406
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
8-326 |
1.49e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.25 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 8 TLARVVEGWNRHEAERTEVLRGLQEERQaaELTRSKqqETVTRLEQSLSEAMEALSREQEGARLQQREkeaLEEERQAL- 86
Cdd:pfam01576 640 SLARALEEALEAKEELERTNKQLRAEME--DLVSSK--DDVGKNVHELERSKRALEQQVEEMKTQLEE---LEDELQATe 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 87 --TLRLEVEQQQCRTlQEERD-EARAGQLSEHRKLEALQValqeeRQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQR 163
Cdd:pfam01576 713 daKLRLEVNMQALKA-QFERDlQARDEQGEEKRRQLVKQV-----RELEAELEDERKQRAQAVAAKKKLELDLKELEAQI 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 164 EA--QAAWETQQQFALLQTEVRRLEGDLDTVRRERDALqlemsLVQAR--------YESQRIQMESELAVQLEQRVT--- 230
Cdd:pfam01576 787 DAanKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI-----LAQSKesekklknLEAELLQLQEDLAASERARRQaqq 861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 231 --ERLAEAQENSLRQAASLRDHHRkQLQELSGQHQQELaaQLAQFKVEM-ADREERQQQVAQDYELRLAREQARVRDLKS 307
Cdd:pfam01576 862 erDELADEIASGASGKSALQDEKR-RLEARIAQLEEEL--EEEQSNTELlNDRLRKSTLQVEQLTTELAAERSTSQKSES 938
|
330
....*....|....*....
gi 26331630 308 GNQQLEEQRAELVERLQAM 326
Cdd:pfam01576 939 ARQQLERQNKELKAKLQEM 957
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
22-338 |
1.94e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 22 ERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSR--EQEGARLQQREKEALEEERQALTLRLEVEQQQCRT 99
Cdd:COG4717 78 EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 100 LQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEgQAQLEREKGNSQRE---AQAAWETQQQFA 176
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-LAELEEELEEAQEEleeLEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 177 LLQTEVRRLE--------------------GDLDTVRRERDALQLEMSLVQARYESQRIQmeselAVQLEQRVTERLAEA 236
Cdd:COG4717 237 EAAALEERLKearlllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLARE-----KASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 237 QENSLRQAASLRDHHRKQL-QELSGQHQQELAAQLAQFKVEMADREERQQQVAQDyelrlAREQARVRDLKSGNQQLEEQ 315
Cdd:COG4717 312 ALEELEEEELEELLAALGLpPDLSPEELLELLDRIEELQELLREAEELEEELQLE-----ELEQEIAALLAEAGVEDEEE 386
|
330 340
....*....|....*....|....*
gi 26331630 316 RAELVERLQAM--LQAHWEEANQLL 338
Cdd:COG4717 387 LRAALEQAEEYqeLKEELEELEEQL 411
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
20-224 |
2.21e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 20 EAERTEVLRGLQEERQAAEltRSKQQETVTRLEQSLSEAMEALSREQEGAR-LQQREKEALEEERQALTLRLEVE----- 93
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAEE--DKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEEKKKAEELKKAEEenkik 1731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 94 -QQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAwikqEHQLKERLQALQEEGQAQLEREKGNSQREAQaawETQ 172
Cdd:PTZ00121 1732 aEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA----EEIRKEKEAVIEEELDEEDEKRRMEVDKKIK---DIF 1804
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 26331630 173 QQFALLQtevrrlEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQ 224
Cdd:PTZ00121 1805 DNFANII------EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2-299 |
2.37e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEaLEE 81
Cdd:TIGR00618 196 AELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEE-LRA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 82 ERQALTLRLEVEQQQCRTLQ--------EERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQ 153
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPlaahikavTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 154 LEREKGNSQrEAQAAWETQQQFALLQtEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERL 233
Cdd:TIGR00618 355 IHIRDAHEV-ATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26331630 234 AEAQensLRQAASLRDHHRKQLQELSGQ--HQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQ 299
Cdd:TIGR00618 433 QELQ---QRYAELCAAAITCTAQCEKLEkiHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL 497
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-316 |
2.38e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 9 LARVVEGWNR-HEAERTEVLRGLQEERQAAELTRS---KQQETVTRLEQSLSEAMEalsREQEGARLQQREKEAlEEERQ 84
Cdd:PTZ00121 1156 IARKAEDARKaEEARKAEDAKKAEAARKAEEVRKAeelRKAEDARKAEAARKAEEE---RKAEEARKAEDAKKA-EAVKK 1231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 85 ALTLRLEVEqqQCRTLQEERDEaragqlSEHRKLEALQVALQEERQAWIKQEHQLK-ERLQALQEEGQAQlEREKGNSQR 163
Cdd:PTZ00121 1232 AEEAKKDAE--EAKKAEEERNN------EEIRKFEEARMAHFARRQAAIKAEEARKaDELKKAEEKKKAD-EAKKAEEKK 1302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 164 EAQAAWETQQQfallQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMEselAVQLEQRVTERLAEAQENSLRQ 243
Cdd:PTZ00121 1303 KADEAKKKAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE---AAADEAEAAEEKAEAAEKKKEE 1375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26331630 244 AASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYElRLAREQARVRDLKsgnQQLEEQR 316
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK-KKAEEKKKADEAK---KKAEEAK 1444
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
20-334 |
2.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 20 EAERTEVLRGLQEERQAAELTRSKQQ---ETVTRLE---QSLSEAMEALSREQEGARLQQREK----EALEEERQALTLR 89
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAEslrEDADDLEeraEELREEAAELESELEEAREAVEDRreeiEELEEEIEELRER 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 90 LEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAwikqehqlKERLQALQEEGQA-QLEREKGNSQReAQAA 168
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARER--------VEEAEALLEAGKCpECGQPVEGSPH-VETI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 169 WETQQQFALLQTEVRRLEGDLDTVRRERDALQlemSLVQARYESQRIQMESELavqLEQRVTERLAEAQENSLRqAASLR 248
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAE---DLVEAEDRIERLEERRED---LEELIAERRETIEEKRER-AEELR 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 249 D------------HHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVA------QDYELRLAREQARVRDLKSGNQ 310
Cdd:PRK02224 544 EraaeleaeaeekREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRtllaaiADAEDEIERLREKREALAELND 623
|
330 340
....*....|....*....|....
gi 26331630 311 QLEEQRAELVERLQAMLQAHWEEA 334
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEAR 647
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
9-340 |
2.47e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.66 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 9 LARVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQE------TVTRLEQSLSEAMEALSREQEGAR----LQQREKEA 78
Cdd:TIGR00618 530 MQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEiqqsfsILTQCDNRSKEDIPNLQNITVRLQdlteKLSEAEDM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 79 LEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSE-HRKLEALQVALQEERQAWIkqehqlkeRLQALQEEGQAQLERE 157
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHAL--------SIRVLPKELLASRQLA 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 158 KGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRI---QMESELAVQLEQRVTERLA 234
Cdd:TIGR00618 682 LQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDalnQSLKELMHQARTVLKARTE 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 235 EAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQfkvEMADREERQQQVAQDYEL-RLAREQARVRDLKSGNQQLE 313
Cdd:TIGR00618 762 AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH---LLKTLEAEIGQEIPSDEDiLNLQCETLVQEEEQFLSRLE 838
|
330 340
....*....|....*....|....*..
gi 26331630 314 EQRAELVERLQamLQAHWEEANQLLST 340
Cdd:TIGR00618 839 EKSATLGEITH--QLLKYEECSKQLAQ 863
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
11-329 |
3.13e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 11 RVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEA-MEALSREQEGARLQQR----------EKEAL 79
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEArMAHFARRQAAIKAEEArkadelkkaeEKKKA 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 80 EEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEER---QAWIKQEHQLKERLQALQEEGQAQlER 156
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKkaaEAAKAEAEAAADEAEAAEEKAEAA-EK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 157 EKGNSQREAQAAWETQQQFALLQTEVRRLEGD---------LDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQ 227
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkadelkkAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 228 RVTErlAEAQENSLRQAASLR--DHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQdyELRLAREQARVRDL 305
Cdd:PTZ00121 1452 KAEE--AKKAEEAKKKAEEAKkaDEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKAD--EAKKAEEAKKADEA 1527
|
330 340
....*....|....*....|....*..
gi 26331630 306 KSGNQQL---EEQRAELVERLQAMLQA 329
Cdd:PTZ00121 1528 KKAEEAKkadEAKKAEEKKKADELKKA 1554
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2-324 |
3.30e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALeE 81
Cdd:TIGR00618 175 LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQ-E 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 82 ERQALTLRLEVEQQQCRTLQEErdEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEgQAQLEREKGNS 161
Cdd:TIGR00618 254 EQLKKQQLLKQLRARIEELRAQ--EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK-MRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 162 QREAQAAWETQQQFALLQTEVR---RLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQE 238
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSqeiHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 239 NSLRQAASLRDhHRKQLQELSGQH--QQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQR 316
Cdd:TIGR00618 411 TIDTRTSAFRD-LQGQLAHAKKQQelQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKK 489
|
....*...
gi 26331630 317 AELVERLQ 324
Cdd:TIGR00618 490 AVVLARLL 497
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
128-369 |
4.07e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.66 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 128 ERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVR---RLEGDLDTVRRERDALQLEms 204
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERmamERERELERIRQEERKRELE-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 205 lvqaRYESQRIQMESELAVQLEQRVTERlaeaQENSLRQAASLRDHHRKQLQElsGQHQQELAAQLAQFKVEMADREERQ 284
Cdd:pfam17380 364 ----RIRQEEIAMEISRMRELERLQMER----QQKNERVRQELEAARKVKILE--EERQRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 285 QQVAQDYELRLAREQARVR-DLKSGNQQLEEQRAELVERLQAML--------QAHWEEANQLLSTTLLPPNPQAPLAEPS 355
Cdd:pfam17380 434 QREVRRLEEERAREMERVRlEEQERQQQVERLRQQEEERKRKKLelekekrdRKRAEEQRRKILEKELEERKQAMIEEER 513
|
250
....*....|....
gi 26331630 356 SPGPLEPEKGERRT 369
Cdd:pfam17380 514 KRKLLEKEMEERQK 527
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
169-337 |
4.11e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 169 WETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYES-QRIQMESELAVQLEQ------RVTERLAEAQENS- 240
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlQRLAEYSWDEIDVASaereiaELEAELERLDASSd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 241 -LRQAASLRDHHRKQLQELSGQhQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVR---DLKSGNQQLEEQR 316
Cdd:COG4913 686 dLAALEEQLEELEAELEELEEE-LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRallEERFAAALGDAVE 764
|
170 180
....*....|....*....|.
gi 26331630 317 AELVERLQAMLQAHWEEANQL 337
Cdd:COG4913 765 RELRENLEERIDALRARLNRA 785
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
25-483 |
4.51e-05 |
|
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: 47.04 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 25 EVLRGLQEERQAAELTRSKQQETVTRLEQSLSEamealsreqegarlQQREKEALEEERQALTLRLEVEQQQCRTLQEER 104
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSERTVSDLTASLQE--------------KERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 105 DEARAGQlsehRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQ--AQLEREKGNSQREAQAAWETQQQFALLQ--- 179
Cdd:pfam15921 541 DHLRNVQ----TECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRtaGAMQVEKAQLEKEINDRRLELQEFKILKdkk 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 180 -TEVRRLEGDLDTVRRERdalqleMSLVQAryESQRIQMESELAVQLEQRVTE-RLAEAQENSLRQAAS-LRDHHRKQLQ 256
Cdd:pfam15921 617 dAKIRELEARVSDLELEK------VKLVNA--GSERLRAVKDIKQERDQLLNEvKTSRNELNSLSEDYEvLKRNFRNKSE 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 257 EL-SGQHQQELAAQLAQFKVE--------MADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAElVERLQAML 327
Cdd:pfam15921 689 EMeTTTNKLKMQLKSAQSELEqtrntlksMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN-ANKEKHFL 767
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 328 QAHWEEANQLLSTTLLPPNPQAplaepsspGPLEPEKGERRTW--AMPPMAVALKPVLQQSRE----VKGDVPGAPSVLC 401
Cdd:pfam15921 768 KEEKNKLSQELSTVATEKNKMA--------GELEVLRSQERRLkeKVANMEVALDKASLQFAEcqdiIQRQEQESVRLKL 839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 402 STSPDLSLLLGPPFQNQNSFQP--LEPKPDVTPPTAGPFSALEA-FTDDHRAERPFPEEDPGSDgdarlppasqlegLKN 478
Cdd:pfam15921 840 QHTLDVKELQGPGYTSNSSMKPrlLQPASFTRTHSNVPSSQSTAsFLSHHSRKTNALKEDPTRD-------------LKQ 906
|
....*
gi 26331630 479 FLQQL 483
Cdd:pfam15921 907 LLQEL 911
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
20-336 |
5.76e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 20 EAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARlqqrekeALEEERQALTLRlevEQQQCRT 99
Cdd:PTZ00121 1126 DARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAK-------KAEAARKAEEVR---KAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 100 LQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERlqalqEEGQAQLEREKGNSQ----REAQAAWETQQQF 175
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKD-----AEEAKKAEEERNNEEirkfEEARMAHFARRQA 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 176 ALLQTEVRRLEgDLDTVRRERDALQLEMSLVQARYESQRIQMEselavqlEQRVTERLAEAQENSLRQAASLRD--HHRK 253
Cdd:PTZ00121 1271 AIKAEEARKAD-ELKKAEEKKKADEAKKAEEKKKADEAKKKAE-------EAKKADEAKKKAEEAKKKADAAKKkaEEAK 1342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 254 QLQELSGQHQQELAAQL--AQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAhw 331
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAeaAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-- 1420
|
....*
gi 26331630 332 EEANQ 336
Cdd:PTZ00121 1421 DEAKK 1425
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
59-328 |
5.99e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 59 MEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQ-----EERDEARAGQLSEHRKLEAlQVALQEER---- 129
Cdd:PRK10246 557 TKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQpwldaQEEHERQLRLLSQRHELQG-QIAAHNQQiiqy 635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 130 -QAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAA-WETQQ-QFALLQTEVRRLEGDLDTVRRERDA-------- 198
Cdd:PRK10246 636 qQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQsWQQRQnELTALQNRIQQLTPLLETLPQSDDLphseetva 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 199 --------------------LQLEMSLVQARYESQRIQMESELAVQLEQRVTERLA----EAQENSLRQAASLRDHHRKQ 254
Cdd:PRK10246 716 ldnwrqvheqclslhsqlqtLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQAFLAalldEETLTQLEQLKQNLENQRQQ 795
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26331630 255 LQELSGQHQQELAAQLAQ---FKVEMADREERQQQVAQ-DYELRL-AREQARVRdlksgnQQLeEQRAELVERLQAMLQ 328
Cdd:PRK10246 796 AQTLVTQTAQALAQHQQHrpdGLDLTVTVEQIQQELAQlAQQLREnTTRQGEIR------QQL-KQDADNRQQQQALMQ 867
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
27-213 |
7.11e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 27 LRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTL------ 100
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyr 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 101 -----------------QEERDEARAGQLSEHRK--LEALQVALQE--ERQAWIKQEHQLKERLQALQEEGQAQLEREKg 159
Cdd:COG4942 116 lgrqpplalllspedflDAVRRLQYLKYLAPARReqAEELRADLAElaALRAELEAERAELEALLAELEEERAALEALK- 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 26331630 160 nSQREAQAAwETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQ 213
Cdd:COG4942 195 -AERQKLLA-RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
18-342 |
7.17e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 18 RHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQC 97
Cdd:COG4717 115 REELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 98 RTLQEERDEARAGQLSEHRKLEALQVALQEERQAW--IKQEHQLKERLQALQEEGQ------------AQLEREKGNSQR 163
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELeqLENELEAAALEERLKEARLllliaaallallGLGGSLLSLILT 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 164 EAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEqRVTERLAEAQEnsLRQ 243
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE-ELLELLDRIEE--LQE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 244 AASLRDHHRKQLQELsgQHQQELAAQLAQFKVEmaDREERQQQVAQDYELRlaREQARVRDLKsgnQQLEEQRAELVERL 323
Cdd:COG4717 352 LLREAEELEEELQLE--ELEQEIAALLAEAGVE--DEEELRAALEQAEEYQ--ELKEELEELE---EQLEELLGELEELL 422
|
330
....*....|....*....
gi 26331630 324 QAMLQAHWEEANQLLSTTL 342
Cdd:COG4717 423 EALDEEELEEELEELEEEL 441
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
147-378 |
7.81e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 7.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 147 QEEGQAQLEREKGNSQREAQAAwetQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLE 226
Cdd:COG3883 21 KQKELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 227 QRVT----ERLAEAQENS--LRQAASLRDHHRKQLQELsgQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQA 300
Cdd:COG3883 98 SGGSvsylDVLLGSESFSdfLDRLSALSKIADADADLL--EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26331630 301 RVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQLLSTTLLPPNPQAPLAEPSSPGPLEPEKGERRTWAMPPMAVA 378
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAG 253
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
50-336 |
9.82e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 50 RLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEER 129
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEED 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 130 QAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTE-VRRLEGDLDTVRRERDALQLEMSLVQA 208
Cdd:pfam13868 115 QAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAErEEEREAEREEIEEEKEREIARLRAQQE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 209 RYESQRIQMESELAV----QLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQ 284
Cdd:pfam13868 195 KAQDEKAERDELRAKlyqeEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDE 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 26331630 285 QQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQ 336
Cdd:pfam13868 275 EIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAE 326
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
10-313 |
1.01e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 10 ARVVEgwnRHEAERTEvLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEA--------------LSREQEGARLQQRE 75
Cdd:PRK10246 187 AMVFE---QHKSARTE-LEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQlltaqqqqqqslnwLTRLDELQQEASRR 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 76 KEALEEERQALT------LRLEVEQ--QQCRTLQEERDEARAGQLSEHRKLEALQVALQE--ERQAWIKQ--EHQLKERL 143
Cdd:PRK10246 263 QQALQQALAAEEkaqpqlAALSLAQpaRQLRPHWERIQEQSAALAHTRQQIEEVNTRLQStmALRARIRHhaAKQSAELQ 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 144 QALQEEGQAQLEREKGNSQREAQAAWETQ-QQFALLQTEVRRLEGDLDTVRRERDALQlemslvqaryESQRIQMESELA 222
Cdd:PRK10246 343 AQQQSLNTWLAEHDRFRQWNNELAGWRAQfSQQTSDREQLRQWQQQLTHAEQKLNALP----------AITLTLTADEVA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 223 VQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYElrLAREQARV 302
Cdd:PRK10246 413 AALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT--ICEQEARI 490
|
330
....*....|.
gi 26331630 303 RDLKSGNQQLE 313
Cdd:PRK10246 491 KDLEAQRAQLQ 501
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
29-337 |
1.16e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 29 GLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGArlQQREKEALEEER---------QALTLRLEVEQQQCRT 99
Cdd:pfam12128 398 KLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEE--EYRLKSRLGELKlrlnqatatPELLLQLENFDERIER 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 100 LQEERDEARAGQLSEHRKLEALQvALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQ---REAQAAWEtqQQFA 176
Cdd:pfam12128 476 AREEQEAANAEVERLQSELRQAR-KRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLhflRKEAPDWE--QSIG 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 177 LLQTEVRRLEGDLDTVRRERDALQlEMSLVQARYESQRIQMESelAVQLEQRVTERLAEAQEnSLRQAASLRDHHRKQLQ 256
Cdd:pfam12128 553 KVISPELLHRTDLDPEVWDGSVGG-ELNLYGVKLDLKRIDVPE--WAASEEELRERLDKAEE-ALQSAREKQAAAEEQLV 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 257 ELSGQ-HQQELAAQLAQFKVEMAdREERQQQVAQDYELRLAREQARVRDLKSGNQQ---LEEQRAELVERLQAMLQAHWE 332
Cdd:pfam12128 629 QANGElEKASREETFARTALKNA-RLDLRRLFDEKQSEKDKKNKALAERKDSANERlnsLEAQLKQLDKKHQAWLEEQKE 707
|
....*
gi 26331630 333 EANQL 337
Cdd:pfam12128 708 QKREA 712
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
30-325 |
1.17e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 30 LQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARA 109
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 110 ----------GQ-LSEHRKLEAL-----QVALQEERQAWIKQEHQ-LKERLQALQEEGQAQLEREKGNSQREAqaaweTQ 172
Cdd:PRK02224 448 lleagkcpecGQpVEGSPHVETIeedreRVEELEAELEDLEEEVEeVEERLERAEDLVEAEDRIERLEERRED-----LE 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 173 QQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAV--QLEQRVTErLAEAQE--NSLRQAASLR 248
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEvaELNSKLAE-LKERIEslERIRTLLAAI 601
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26331630 249 DHHRKQLQELSGQHQQeLAAQLAQFKVEMADREERQQQVAQDYelrlarEQARVRDLKSGNQQLEEQRAELVERLQA 325
Cdd:PRK02224 602 ADAEDEIERLREKREA-LAELNDERRERLAEKRERKRELEAEF------DEARIEEAREDKERAEEYLEQVEEKLDE 671
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
31-327 |
1.21e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 31 QEERQAAELTRSKQQETVTRLEQSLSEAM-EALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDeaRA 109
Cdd:pfam02029 9 RERRRRAREERRRQKEEEEPSGQVTESVEpNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALE--RQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 110 GQLSEHRKLEALQVALQEERqawikqehqlKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDL 189
Cdd:pfam02029 87 KEFDPTIADEKESVAERKEN----------NEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 190 DTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTE-----------------------------------RLA 234
Cdd:pfam02029 157 EEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLdqkrghpevksqngeeevtklkvttkrrqgglsqsQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 235 EAQENSLRQAASLRDHHRKQLQELSG-------QHQQELAAQLAQFKVEMADR----EERQQQVAQDYELRLAREQARVR 303
Cdd:pfam02029 237 EEEAEVFLEAEQKLEELRRRRQEKESeefeklrQKQQEAELELEELKKKREERrkllEEEEQRRKQEEAERKLREEEEKR 316
|
330 340
....*....|....*....|....
gi 26331630 304 DLKsgnQQLEEQRAELVERLQAML 327
Cdd:pfam02029 317 RMK---EEIERRRAEAAEKRQKLP 337
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
20-282 |
1.33e-04 |
|
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: 45.42 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 20 EAERTEVLRGLQEERQAAELTRskqQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRT 99
Cdd:TIGR00606 289 ELKMEKVFQGTDEQLNDLYHNH---QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 100 LQEERDEaragqLSEHRKLEALQVALQEERQawIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAwetqqqfallQ 179
Cdd:TIGR00606 366 RDSLIQS-----LATRLELDGFERGPFSERQ--IKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQ----------A 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 180 TEVR-RLEGDLDTVRRERDALQLEMS-LVQARYESQRIQMESELAVQLEQRVTERLAE---AQENSLRQAASLRDHHRKQ 254
Cdd:TIGR00606 429 DEIRdEKKGLGRTIELKKEILEKKQEeLKFVIKELQQLEGSSDRILELDQELRKAERElskAEKNSLTETLKKEVKSLQN 508
|
250 260
....*....|....*....|....*...
gi 26331630 255 LQELSGQHQQELAAQLAQFKVEMADREE 282
Cdd:TIGR00606 509 EKADLDRKLRKLDQEMEQLNHHTTTRTQ 536
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
20-337 |
1.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 20 EAERTEVLRGLQEERQAAEltRSKQQETVTRLEQSlSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRT 99
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEE--KKKADEAKKKAEEA-KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 100 LQEERDEARAGQL---SEHRKLEALQVALQEERQA--WIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQ 174
Cdd:PTZ00121 1359 AEAAEEKAEAAEKkkeEAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 175 FAllqTEVRRLEGDLDTVRRERDALQLEMSLVQARY--ESQRIQMESELAVQLEQRVTERLAEAQEnsLRQAAslrdHHR 252
Cdd:PTZ00121 1439 KA---EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAA----EAK 1509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 253 KQLQELSGQHQQELAAQLAQF-KVEMADREERQQQVAQDYELRLAREQARVRDLKsgnqQLEEQRAELVERLQAMLQAhw 331
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAeEAKKADEAKKAEEKKKADELKKAEELKKAEEKK----KAEEAKKAEEDKNMALRKA-- 1583
|
....*.
gi 26331630 332 EEANQL 337
Cdd:PTZ00121 1584 EEAKKA 1589
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
21-326 |
1.99e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 21 AERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTL 100
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 101 QEERDEaragqlsEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQT 180
Cdd:pfam01576 319 QELRSK-------REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 181 EVRRLEGDLDTVRRERDALQLEMSLVQARY---ESQRIQMESELA-VQLE-QRVTERLAEAQENSLRQAASLrDHHRKQL 255
Cdd:pfam01576 392 ELRTLQQAKQDSEHKRKKLEGQLQELQARLsesERQRAELAEKLSkLQSElESVSSLLNEAEGKNIKLSKDV-SSLESQL 470
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26331630 256 QELSGQHQQELAAQLA---QFKVEMADREERQQQVAQDYELRLAREqarvRDLKSGNQQLEEQRAELVERLQAM 326
Cdd:pfam01576 471 QDTQELLQEETRQKLNlstRLRQLEDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKKKLEEDAGTL 540
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
60-182 |
2.23e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 60 EALSReqegARLQQREK-EALEEERQALTlRLEVEQQQCRTLQEERDEARAGQLSEhrKLEALQVALQEERQAWiKQEHQ 138
Cdd:COG0542 397 EAAAR----VRMEIDSKpEELDELERRLE-QLEIEKEALKKEQDEASFERLAELRD--ELAELEEELEALKARW-EAEKE 468
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 26331630 139 LKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEV 182
Cdd:COG0542 469 LIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
24-222 |
2.57e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 24 TEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKE--ALEEERQALTLRLEVEQQQCRTLQ 101
Cdd:COG3206 218 LQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQlaELEAELAELSARYTPNHPDVIALR 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 102 EERDEARAGQLSEhrkLEALQVALQEERQAWIKQEHQLKERLQALQEEgqaqlerekgnsqreaqaawetQQQFALLQTE 181
Cdd:COG3206 298 AQIAALRAQLQQE---AQRILASLEAELEALQAREASLQAQLAQLEAR----------------------LAELPELEAE 352
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 26331630 182 VRRLEgdldtvrRERDALQLEMSLVQARYESQRIQMESELA 222
Cdd:COG3206 353 LRRLE-------REVEVARELYESLLQRLEEARLAEALTVG 386
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-238 |
2.64e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQR----EKE 77
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAkleaEID 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 78 ALEEERQALTLRLEVEQQQCRTLQEERDEARAgqlsehrKLEALQVALQEER---QAWIKQEHQLKERLQALQEEgqaqL 154
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVDkefAETRDELKDYREKLEKLKRE----I 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 155 EREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESE----LAVQLE-QRV 229
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYeqelYDLKEEyDRV 481
|
....*....
gi 26331630 230 TERLAEAQE 238
Cdd:TIGR02169 482 EKELSKLQR 490
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
12-174 |
2.75e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.64 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 12 VVEGWNRHE-----AERTEVLRGLQEERQAAELtRSKQQETVTRLeqslseamealsREQEGARLQQRE--KEALEEERQ 84
Cdd:PRK09510 60 VVEQYNRQQqqqksAKRAEEQRKKKEQQQAEEL-QQKQAAEQERL------------KQLEKERLAAQEqkKQAEEAAKQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 85 ALTLRLEVEQQQCRTLQEER--DEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQ 162
Cdd:PRK09510 127 AALKQKQAEEAAAKAAAAAKakAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAE 206
|
170
....*....|..
gi 26331630 163 REAQAAWETQQQ 174
Cdd:PRK09510 207 AKKKAAAEAKKK 218
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
3-317 |
3.04e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 3 EQLDKTLARVVEGWNRHEaERTEVLRGLQEERQAAELTRSKQQETVTRLEQSlSEAMEALSREQEGA-----RLQQREKE 77
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLK-SRLGELKLRLNQATATPELLLQLENFDERIERA-REEQEAANAEVERLqselrQARKRRDQ 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 78 ALEEERQAlTLRLEVEQQQCRTLQEERDeARAGQLSEHRKLEA--------------------LQVALQEERQAWIKQEH 137
Cdd:pfam12128 504 ASEALRQA-SRRLEERQSALDELELQLF-PQAGTLLHFLRKEApdweqsigkvispellhrtdLDPEVWDGSVGGELNLY 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 138 QLKERLQALQEEGQAQLEREkgnsQREAQAAWETQQQFAllQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRI-- 215
Cdd:pfam12128 582 GVKLDLKRIDVPEWAASEEE----LRERLDKAEEALQSA--REKQAAAEEQLVQANGELEKASREETFARTALKNARLdl 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 216 -----QMESElAVQLEQRVTERLAEAQEnSLRQAAslrdhhrKQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQD 290
Cdd:pfam12128 656 rrlfdEKQSE-KDKKNKALAERKDSANE-RLNSLE-------AQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
|
330 340 350
....*....|....*....|....*....|.
gi 26331630 291 YELRLAR----EQARVRDLKSGNQQLEEQRA 317
Cdd:pfam12128 727 LDAQLALlkaaIAARRSGAKAELKALETWYK 757
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
74-323 |
3.17e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 74 REK--EALEEERQALTLR---LEVEQQQCRTLQEERDEARAGQLS----------------EHRKLEALQVALQEERQAW 132
Cdd:COG3096 783 REKrlEELRAERDELAEQyakASFDVQKLQRLHQAFSQFVGGHLAvafapdpeaelaalrqRRSELERELAQHRAQEQQL 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 133 IKQEHQLKERLQALQE-EGQAQLEREKGNSQR------EAQAAWETQQQFALLQTEVRRLEGDLDTVRR---ERDALQLE 202
Cdd:COG3096 863 RQQLDQLKEQLQLLNKlLPQANLLADETLADRleelreELDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeQFEQLQAD 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 203 msLVQARYESQRIQMESELAVQLEQRVT--------ERLAEAQENS------LRQAASLRDHHRKQLQELSGQHQQELAA 268
Cdd:COG3096 943 --YLQAKEQQRRLKQQIFALSEVVQRRPhfsyedavGLLGENSDLNeklrarLEQAEEARREAREQLRQAQAQYSQYNQV 1020
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26331630 269 -------------QLAQFKVEM--------ADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERL 323
Cdd:COG3096 1021 laslkssrdakqqTLQELEQELeelgvqadAEAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRL 1096
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
17-261 |
3.54e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.05 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 17 NRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLE-----QSLSEAMEALSREQEGarlqQREKEALEEERQALTL--- 88
Cdd:NF012221 1548 SKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAaisgsQSQLESTDQNALETNG----QAQRDAILEESRAVTKelt 1623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 89 ----RLEVEQQQCRTLQEERDEARAG-----------QLSEHRKLeaLQVALQEERQAWIKQEHQLKERLqALQEEGQAQ 153
Cdd:NF012221 1624 tlaqGLDALDSQATYAGESGDQWRNPfagglldrvqeQLDDAKKI--SGKQLADAKQRHVDNQQKVKDAV-AKSEAGVAQ 1700
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 154 LEREKGNSQREAQAAWEtqqqfallQTEVRRLEGDldtvRRERDALQLEMslvQARYESQRIQMESELAVQLEQRVTERl 233
Cdd:NF012221 1701 GEQNQANAEQDIDDAKA--------DAEKRKDDAL----AKQNEAQQAES---DANAAANDAQSRGEQDASAAENKANQ- 1764
|
250 260
....*....|....*....|....*....
gi 26331630 234 AEAQENSLRQAASLR-DHHRKQLQELSGQ 261
Cdd:NF012221 1765 AQADAKGAKQDESDKpNRQGAAGSGLSGK 1793
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
20-279 |
3.59e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 20 EAERTEVLRGLQEERQAAELTRSKQQETVTRLEQ-------SLSEAMEALS---------------REQEGARLQQREKE 77
Cdd:PRK10246 604 AQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQQqieqrqqQLLTALAGYAltlpqedeeaswlatRQQEAQSWQQRQNE 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 78 --ALEEERQALTLRLEVEQQQcrtlQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLE 155
Cdd:PRK10246 684 ltALQNRIQQLTPLLETLPQS----DDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQ 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 156 REKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRrerdALQLEMSLVQARYESQRIQMESELAV--QLEQRVTERL 233
Cdd:PRK10246 760 ASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQ----TLVTQTAQALAQHQQHRPDGLDLTVTveQIQQELAQLA 835
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 26331630 234 AEAQENSLRQAASlrdhhRKQLQ--ELSGQHQQELAAQLAQFKVEMAD 279
Cdd:PRK10246 836 QQLRENTTRQGEI-----RQQLKqdADNRQQQQALMQQIAQATQQVED 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-339 |
3.68e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEGWNR---HEAERTEVLRGLQEERQAAELTRSKQqETVTRLEQSLSEAMEALSREQEGARLQQREKEA 78
Cdd:PRK03918 178 IERLEKFIKRTENIEELikeKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 79 LEEERQALTLRLEVEQQQCRTLQEerdeaRAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREK 158
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEE-----KVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 159 GNSQREAQAAwETQQQFALLQTEVRRLEGDLDTVRRERdALQLEMSLVQAR---YESQRIQMESELAVQLEQRVTERLAE 235
Cdd:PRK03918 332 ELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRltgLTPEKLEKELEELEKAKEEIEEEISK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 236 --AQENSLRQAASLRDHHRKQLQ-----------ELSGQHQQELAAQ-------LAQFKVEMADREERQQQVAQDYELRL 295
Cdd:PRK03918 410 itARIGELKKEIKELKKAIEELKkakgkcpvcgrELTEEHRKELLEEytaelkrIEKELKEIEEKERKLRKELRELEKVL 489
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 26331630 296 AREQaRVRDLKSGNQQLEEQRAELVERLQAMLQAHWEEANQLLS 339
Cdd:PRK03918 490 KKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
143-325 |
3.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 143 LQALQEEgQAQLEREKG----NSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQME 218
Cdd:COG4717 48 LERLEKE-ADELFKPQGrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 219 SELAVQLEQRVTERLAEAQE--NSLRQAASLRDHHRKQLQELSGQH---QQELAAQLAQFKVEMADREERQQQVAQDYEL 293
Cdd:COG4717 127 LLPLYQELEALEAELAELPErlEELEERLEELRELEEELEELEAELaelQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190
....*....|....*....|....*....|..
gi 26331630 294 RLAREQARVRDLKSGNQQLEEQRAELVERLQA 325
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
19-275 |
3.86e-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: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 19 HEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQqqCR 98
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ--CQ 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 99 TLQEErdearagqlsEHRKLEALQVALQEERQAWIKQEHQLKERLQALQE-EGQAQLEREKGNSQREAQAAWETQQQFAL 177
Cdd:TIGR00618 704 TLLRE----------LETHIEEYDREFNEIENASSSLGSDLAAREDALNQsLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 178 LQT--EVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERlaEAQENSLRQAASLRDHHRKQL 255
Cdd:TIGR00618 774 LQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE--EQFLSRLEEKSATLGEITHQL 851
|
250 260
....*....|....*....|
gi 26331630 256 QELSGQHQQELAAQLAQFKV 275
Cdd:TIGR00618 852 LKYEECSKQLAQLTQEQAKI 871
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
50-152 |
3.89e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 50 RLEQ-SLSEAMEALSREQEgaRLQqREKEALEEERQALTL-RLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQvALQE 127
Cdd:COG0542 403 RMEIdSKPEELDELERRLE--QLE-IEKEALKKEQDEASFeRLAELRDELAELEEELEALKARWEAEKELIEEIQ-ELKE 478
|
90 100
....*....|....*....|....*
gi 26331630 128 ERQAWIKQEHQLKERLQALQEEGQA 152
Cdd:COG0542 479 ELEQRYGKIPELEKELAELEEELAE 503
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
343-537 |
4.54e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 343 LPPNPQAPLAEPSSPGPLEPEKGERRTWAMPPmavalkpvlqqsREVKGDVPGAPSVlcSTSPDLSLLLGPPfqnQNSFQ 422
Cdd:PHA03247 2617 LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPP------------PERPRDDPAPGRV--SRPRRARRLGRAA---QASSP 2679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 423 PLEPKPDVTPPTAGPfsaLEAFTDDHRAERPfPEEDPGSDGDAR-LPPASQLEGLKNFLQQLLETAPQSNGNPSADLLLP 501
Cdd:PHA03247 2680 PQRPRRRAARPTVGS---LTSLADPPPPPPT-PEPAPHALVSATpLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPA 2755
|
170 180 190
....*....|....*....|....*....|....*.
gi 26331630 502 KAGSRAVSSWEEAPQVPRLPPPVHKTKVPLAMASSL 537
Cdd:PHA03247 2756 RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
34-336 |
4.60e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 34 RQAAEltRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEerdEARAGQLS 113
Cdd:COG3096 275 RHANE--RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQT---ALRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 114 EHRK--LEALQVALqEERQAWIKQEHQLKERLQALQEEGQAQLEREKgnSQ-REAQAAWETQQQFAL-LQTEVRRLEgdl 189
Cdd:COG3096 350 ERYQedLEELTERL-EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLK--SQlADYQQALDVQQTRAIqYQQAVQALE--- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 190 dTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASL---------RDHHRKQLQELSG 260
Cdd:COG3096 424 -KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELvckiageveRSQAWQTARELLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 261 QH--QQELAAQLAQFKVEMAD---REERQQQV---AQDYELRLAREQARVRDLKSGNQQLEEQRAELVERL------QAM 326
Cdd:COG3096 503 RYrsQQALAQRLQQLRAQLAEleqRLRQQQNAerlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAaeaveqRSE 582
|
330
....*....|
gi 26331630 327 LQAHWEEANQ 336
Cdd:COG3096 583 LRQQLEQLRA 592
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
27-323 |
5.10e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 5.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 27 LRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDE 106
Cdd:COG4372 54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 107 ARAgqlsEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLE 186
Cdd:COG4372 134 LEA----QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 187 GDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQEL 266
Cdd:COG4372 210 ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALE 289
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 26331630 267 AAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERL 323
Cdd:COG4372 290 EAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
29-212 |
5.45e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 29 GLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARlqqrEKEALEEERQALTLRLEvEQQQCRTLQEERDEAR 108
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE----EVAELNSKLAELKERIE-SLERIRTLLAAIADAE 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 109 agqlsehrklEALQvALQEERQAWIKQEHQLKERLQALQEEgQAQLEREKGNSQREaqaawETQQQFALLQTEVRRLEGD 188
Cdd:PRK02224 606 ----------DEIE-RLREKREALAELNDERRERLAEKRER-KRELEAEFDEARIE-----EAREDKERAEEYLEQVEEK 668
|
170 180
....*....|....*....|....
gi 26331630 189 LDTVRRERDALQLEMSLVQARYES 212
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELEE 692
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
20-314 |
7.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 20 EAERTEVLRGLQEERQA-----AELTRskqqetvtRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQ 94
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAeelkkAEEKK--------KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 95 QQCRTLQEERDEARAGQLSEHRKLEALQVALQEErqawikQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQ 174
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA------EEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 175 fallQTEVRRLEGDLDtvRRERDALQLEmSLVQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLR--DHHR 252
Cdd:PTZ00121 1684 ----EEDEKKAAEALK--KEAEEAKKAE-ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkdEEEK 1756
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26331630 253 KQLQELsgQHQQELAAQLAQFKVEMADREErqqqVAQDYELRLAREQARVRDLKSGNQQLEE 314
Cdd:PTZ00121 1757 KKIAHL--KKEEEKKAEEIRKEKEAVIEEE----LDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-149 |
7.86e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 27 LRGLQEERQAAELTRS---KQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEE 103
Cdd:COG4913 670 IAELEAELERLDASSDdlaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 26331630 104 RDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEE 149
Cdd:COG4913 750 LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| FUSC |
pfam04632 |
Fusaric acid resistance protein family; This family includes a conserved region found in two ... |
176-330 |
8.49e-04 |
|
Fusaric acid resistance protein family; This family includes a conserved region found in two proteins associated with fusaric acid resistance, from Burkholderia cepacia and Klebsiella oxytoca. These proteins are likely to be membrane transporter proteins.
Pssm-ID: 428044 [Multi-domain] Cd Length: 655 Bit Score: 42.66 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 176 ALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAeaqenslrQAASLRDHHRkQL 255
Cdd:pfam04632 174 AALAGAPGAEAFEAARLRLAADILALEALRSHAAFESPRGRARARALRRLLARMLALLP--------RLRSLARLLA-RL 244
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26331630 256 QELSGQHQQELAAQLAqfkvEMADREERQQQVAQDYELRLAREQAR--VRDLKSGNQQLEEQRAELVERLQAMLQAH 330
Cdd:pfam04632 245 RTEGAGTVPELAALLD----ELAAWEAALAAEALQAALAALRARLRalRPALPLDFDTAAELLARLADLLAELAEAL 317
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
33-314 |
9.61e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.19 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 33 ERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLqeERDEARAGQL 112
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL--EEDIKTLTQR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 113 SEHRKLEALQVALQEERQ-AWIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDT 191
Cdd:pfam07888 145 VLERETELERMKERAKKAgAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTT 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 192 VRR---ERDALQLEMSLVQARYESqriqmeselavqleqrvTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQeLAA 268
Cdd:pfam07888 225 AHRkeaENEALLEELRSLQERLNA-----------------SERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQ-LTL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 26331630 269 QLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEE 314
Cdd:pfam07888 287 QLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-296 |
9.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 83 RQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEgQAQLEREKgNSQ 162
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE-LEELREEL-EKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 163 REAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDAL-QLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQENSL 241
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELrELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 26331630 242 RQAASLRDHHRKQLQELSGQHQQeLAAQLAQFKVEMADREERQQQVAQDYELRLA 296
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEE-LEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
30-227 |
1.13e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 30 LQEERQAAELTRSKQQETVTRLEQSLSEAMEALS--REQEG---------------ARLQQREKEALEEERQALTLRLEV 92
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEefRQKNGlvdlseeaklllqqlSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 93 EQQQCRTLQEERDEARAGQLSEHR-KLEALQVALQEERQAWiKQEH----QLKERLQALQEEGQAQLEREKGNSQREAQA 167
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLRaQLAELEAELAELSARY-TPNHpdviALRAQIAALRAQLQQEAQRILASLEAELEA 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26331630 168 AwetQQQFALLQTEVRRLEGDLDT---VRRERDALQLEMSLVQARYES--QRIQmESELAVQLEQ 227
Cdd:COG3206 325 L---QAREASLQAQLAQLEARLAElpeLEAELRRLEREVEVARELYESllQRLE-EARLAEALTV 385
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
96-325 |
1.29e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 96 QCRTLQEERDEARAGQLSEHRKLEALQVALQE-ERQAWIKQEHQLKERLQAL-QEEGQAQLEREKGNSQREAQAAW---- 169
Cdd:PRK02224 160 QLGKLEEYRERASDARLGVERVLSDQRGSLDQlKAQIEEKEEKDLHERLNGLeSELAELDEEIERYEEQREQARETrdea 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 170 --------ETQQQFALLQTEVRRLEGDLDTVRRERDALqlemslvqaryeSQRIQMESELAVQLEQRVTERLAEAQENSL 241
Cdd:PRK02224 240 devleeheERREELETLEAEIEDLRETIAETEREREEL------------AEEVRDLRERLEELEEERDDLLAEAGLDDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 242 RQAASLrdhhrkqlqelsgQHQQELAAQlaqfKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVE 321
Cdd:PRK02224 308 DAEAVE-------------ARREELEDR----DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELES 370
|
....
gi 26331630 322 RLQA 325
Cdd:PRK02224 371 ELEE 374
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
73-339 |
1.40e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 73 QREKEALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALqEEGQA 152
Cdd:pfam15921 418 RRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL-ESSER 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 153 QLEREKGNSQREAQAAWETQQQFALLQTEVRRLEGDLDTVRRERDALQlemsLVQARYESQRIQMESelavqlEQRVTER 232
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR----NVQTECEALKLQMAE------KDKVIEI 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 233 LAEAQENslrqaaslrdhhrkqLQELSGQHQQELAAQL---AQFKVEMADREERqqqvAQDYELRLAREQARVRDLKSGN 309
Cdd:pfam15921 567 LRQQIEN---------------MTQLVGQHGRTAGAMQvekAQLEKEINDRRLE----LQEFKILKDKKDAKIRELEARV 627
|
250 260 270
....*....|....*....|....*....|....
gi 26331630 310 QQLEEQRAELV----ERLQAMLQAHwEEANQLLS 339
Cdd:pfam15921 628 SDLELEKVKLVnagsERLRAVKDIK-QERDQLLN 660
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
23-317 |
1.43e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 41.86 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 23 RTEVLRGLQE--ERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGarLQQREKEA--------------LEEERQAL 86
Cdd:pfam15818 6 KTSLLEALEElrMRREAETQYEEQIGKIIVETQELKWQKETLQNQKET--LAKQHKEAmavfkkqlqmkmcaLEEEKGKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 87 TLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAwiKQEHQLK----ERLQA-------LQEEGQAQLE 155
Cdd:pfam15818 84 QLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLA--KEDHHKQlneiEKYYAtitgqfgLVKENHGKLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 156 RekgNSQREAQ-----AAWETQQQFAL--LQTEVRRLEGDL------DTVRRERDALQLEMSLVQARYESQRIQMESEla 222
Cdd:pfam15818 162 Q---NVQEAIQlnkrlSALNKKQESEIcsLKKELKKVTSDLikskvtCQYKMGEENINLTIKEQKFQELQERLNMELE-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 223 vqLEQRVTERLAEAQEnslrqaaslrdhhRKQLQELSGQHQQELAAQLAQFKVEMADR----EERQQQVAQDYELRlaRE 298
Cdd:pfam15818 237 --LNKKINEEITHIQE-------------EKQDIIISFQHMQQLLQQQTQANTEMEAElkalKENNQTLERDNELQ--RE 299
|
330
....*....|....*....
gi 26331630 299 QARVRDLKSGNQQLEEQRA 317
Cdd:pfam15818 300 KVKENEEKFLNLQNEHEKA 318
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
178-333 |
1.47e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 178 LQTEVRRLEGDLDTVRRERDALQLEmsLVQARYESQRIQMESELAVQLEQRVTERLAEAQENslRQAASLR---DHHRKQ 254
Cdd:COG1579 29 LPAELAELEDELAALEARLEAAKTE--LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN--KEYEALQkeiESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26331630 255 LQELSgQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAMLQAHWEE 333
Cdd:COG1579 105 ISDLE-DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALYER 182
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
39-165 |
1.54e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 39 LTRSKQQETVTRLEQSLSEA-MEALSREQEgARLQQRE---KEALEEERQALTLRLEVEQQQCRTLQEERdearagQLSE 114
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAkKEAEAIKKE-ALLEAKEeihKLRNEFEKELRERRNELQKLEKRLLQKEE------NLDR 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 26331630 115 H-RKLEALQVALQEERQAWIKQEHQLKER---LQALQEEGQAQLEREKGNSQREA 165
Cdd:PRK12704 101 KlELLEKREEELEKKEKELEQKQQELEKKeeeLEELIEEQLQELERISGLTAEEA 155
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
30-323 |
1.54e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 30 LQEERQAAELTRSKQQE---------TVTRLEQSLSEAMEALSreQEGARLQ-QREKEALEEERQALTLRLEVEQQQCRT 99
Cdd:PRK10929 112 LQVSSQLLEKSRQAQQEqdrareisdSLSQLPQQQTEARRQLN--EIERRLQtLGTPNTPLAQAQLTALQAESAALKALV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 100 lqeerDEARAGQLSEHRKLE--ALQVALQEerqawiKQEHQLKERLQALQEEGQAQlerekgnSQREAQAAWETQQQFAl 177
Cdd:PRK10929 190 -----DELELAQLSANNRQElaRLRSELAK------KRSQQLDAYLQALRNQLNSQ-------RQREAERALESTELLA- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 178 lqtevrRLEGDLDTVRRERdaLQLEMSLVQARyeSQRIQMESELAVQleqrvtERLAEAQENSLRQAASLRdhhRKQLQE 257
Cdd:PRK10929 251 ------EQSGDLPKSIVAQ--FKINRELSQAL--NQQAQRMDLIASQ------QRQAASQTLQVRQALNTL---REQSQW 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 258 LSGQ------------------HQQELAAQLAQFKV------EMADREERQQQVAQDYELRLAREQARVRDlksgnQQLE 313
Cdd:PRK10929 312 LGVSnalgealraqvarlpempKPQQLDTEMAQLRVqrlryeDLLNKQPQLRQIRQADGQPLTAEQNRILD-----AQLR 386
|
330
....*....|
gi 26331630 314 EQRaELVERL 323
Cdd:PRK10929 387 TQR-ELLNSL 395
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-298 |
1.76e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEE 81
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 82 ERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWI------------------------KQEH 137
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarekaslgkeAEEL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 138 QLKERLQALQEEGQAQLEREKG----NSQREAQAAWETQQQFALLQTEVRRLEGDLDTVR-------------------- 193
Cdd:COG4717 308 QALPALEELEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELEEELQLEEleqeiaallaeagvedeeel 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 194 -------RERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQENsLRQAASLRDHHRKQLQELSGQHQQ-E 265
Cdd:COG4717 388 raaleqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE-LEELEEELEELREELAELEAELEQlE 466
|
330 340 350
....*....|....*....|....*....|....
gi 26331630 266 LAAQLAQFKVEMADREERQQQVAQDY-ELRLARE 298
Cdd:COG4717 467 EDGELAELLQELEELKAELRELAEEWaALKLALE 500
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
339-554 |
1.85e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 339 STTLLPPNPQAPLAEPSSPGPLEPEKgERRTWAMPPMAVALKPVLQQSrevkgdvpgAPSVLCSTSPDLSLLLGPPFQNQ 418
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSL-PLGGSVAPGGDVRRRPPSRSP---------AAKPAAPARPPVRRLARPAVSRS 2894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 419 NSFQPLEPKPDVTPPTAGPFSALEAFTDDHRAERPFPEEDPGSDGDARLPPasqleglknflqqllETAPQSNGNPSADL 498
Cdd:PHA03247 2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAP---------------TTDPAGAGEPSGAV 2959
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 26331630 499 LLPKAGsrAVSSWEEAPQVPRLPPPVHKTKVPLAMASSLfRVHGLPSTNLQGSGLS 554
Cdd:PHA03247 2960 PQPWLG--ALVPGRVAVPRFRVPQPAPSREAPASSTPPL-TGHSLSRVSSWASSLA 3012
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
42-325 |
2.00e-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: 41.31 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 42 SKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCrtlqEERDEARAGQLSEHRKLEAL 121
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELC----AEAEEMRARLAARKQELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 122 QVALQ---EERQAWIKQEHQLKERLQALQEEGQAQLEREKGNSQReaqaaweTQQQFALLQTEVRRLEGDLDTVRRERDA 198
Cdd:pfam01576 77 LHELEsrlEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQK-------LQLEKVTTEAKIKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 199 LQLEMSLVQARY---------ESQRIQMESELAVQLEQRVTErLAEAQENSLRQAASLRDHHRKQLQELSGQHQQ--ELA 267
Cdd:pfam01576 150 LSKERKLLEERIseftsnlaeEEEKAKSLSKLKNKHEAMISD-LEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaELQ 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 26331630 268 AQLAQFKVEMADREERqqqvAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQA 325
Cdd:pfam01576 229 AQIAELRAQLAKKEEE----LQAALARLEEETAQKNNALKKIRELEAQISELQEDLES 282
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
178-324 |
2.83e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 178 LQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRI-QMESELAVQLEQRVTERLAEAQenslRQAASLRD--HHRKQ 254
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAIsRQDYDGATAQLRAAQAAVKAAQ----AQLAQAQIdlARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 255 LQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQ 324
Cdd:pfam00529 132 LAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELK 201
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
53-203 |
3.07e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 53 QSLSEAMEALSREQEGARLQQREKEALEEERQaltlrLEVEQQQCRTLQEERDEaragqlsehrkLEALQVALQEERqaw 132
Cdd:COG2433 376 LSIEEALEELIEKELPEEEPEAEREKEHEERE-----LTEEEEEIRRLEEQVER-----------LEAEVEELEAEL--- 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26331630 133 ikqeHQLKERLQALQEEgqaqLEREKGNSQREAqaawETQQQFALLQTEVRRLEGDLDTVRRERDALQLEM 203
Cdd:COG2433 437 ----EEKDERIERLERE----LSEARSEERREI----RKDREISRLDREIERLERELEEERERIEELKRKL 495
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
27-261 |
3.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 27 LRGLQEERQAAEltrSKQQETVTRLEQSLSEAMEALSREQEGARLQQR---EKEALEEERQALTLRLEVEQQQcrtLQEE 103
Cdd:PRK04863 440 AEDWLEEFQAKE---QEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagEVSRSEAWDVARELLRRLREQR---HLAE 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 104 RDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQ---LKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQFALLQT 180
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKnldDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 181 EVRRLEgdldtvRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQENslrqaaslRDHHRKQLQELSG 260
Cdd:PRK04863 594 RIQRLA------ARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE--------RDELAARKQALDE 659
|
.
gi 26331630 261 Q 261
Cdd:PRK04863 660 E 660
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
19-306 |
3.25e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.29 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 19 HEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSE-----AMEALSREQEGARLQQREKEALEEERQALTLRLEVE 93
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEreqkrQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 94 QQ-------QCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKgNSQREAQ 166
Cdd:pfam13868 126 RQlreeideFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQ-DEKAERD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 167 AAWETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLvQARYESQRIQMESELAVQLEQRVTERLAEAQENSLRQAAs 246
Cdd:pfam13868 205 ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE-QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAE- 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 247 lrdhhrkQLQELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLK 306
Cdd:pfam13868 283 -------KRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEER 335
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
10-250 |
3.47e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 10 ARVVEGWNRHEAERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLR 89
Cdd:pfam02463 278 EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 90 LEVEQQQCRTL--QEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLqALQEEGQAQLEREKGNSQREAQa 167
Cdd:pfam02463 358 EEELEKLQEKLeqLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL-ARQLEDLLKEEKKEELEILEEE- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 168 awETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQA---RYESQRIQMESELAVQLEQRVTERLAEAQENSLRQA 244
Cdd:pfam02463 436 --EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLketQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLL 513
|
....*.
gi 26331630 245 ASLRDH 250
Cdd:pfam02463 514 ALIKDG 519
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2-145 |
3.74e-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: 39.52 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEgwnRHEAERTEvLRGLQEERQAAELTRSKQQETVTRLEQSLSEA-----MEALSREQEgarLQQREK 76
Cdd:COG1579 33 LAELEDELAALEA---RLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeYEALQKEIE---SLKRRI 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26331630 77 EALEEERQALTLRLEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEERQAWIKQEHQLKERLQA 145
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
18-306 |
4.08e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 18 RHEAERTEVLRGLQEERQAAELTRSKQQETVTRL----EQSLSEAMEALSREQEgARLQQREKEALEEErqaltLRLEVE 93
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALglppDLSPEELLELLDRIEE-LQELLREAEELEEE-----LQLEEL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 94 QQQCRTLqeerdearagqlsehrkLEALQVALQEERQAWIKQeHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQ- 172
Cdd:COG4717 369 EQEIAAL-----------------LAEAGVEDEEELRAALEQ-AEEYQELKEELEELEEQLEELLGELEELLEALDEEEl 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 173 -QQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESElavQLEQRVTERLAEAQenSLRQAASLRDHH 251
Cdd:COG4717 431 eEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE---ELKAELRELAEEWA--ALKLALELLEEA 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 26331630 252 RKQLQElsgQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLK 306
Cdd:COG4717 506 REEYRE---ERLPPVLERASEYFSRLTDGRYRLIRIDEDLSLKVDTEDGRTRPVE 557
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
43-167 |
4.65e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 43 KQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQcrtlqeeRDEARAGQLSEHRKLEALQ 122
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQ-------REEERLVQKEEQLDARAEK 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 26331630 123 VALQEERQawIKQEHQLKERLQALQEEGQ---AQLEREKGNSQREAQA 167
Cdd:PRK12705 100 LDNLENQL--EEREKALSARELELEELEKqldNELYRVAGLTPEQARK 145
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
69-148 |
5.12e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 69 ARLQQREKEALEEERQALTLRLEVE------QQQCRTLQEERDEARAGQLSEHR------KLEALQV-----ALQEERQA 131
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEklkeelEEKKEKLQEEEDKLLEEAEKEAQqaikeaKKEADEIikelrQLQKGGYA 602
|
90
....*....|....*..
gi 26331630 132 WIKqEHQLKERLQALQE 148
Cdd:PRK00409 603 SVK-AHELIEARKRLNK 618
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
23-290 |
5.70e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.94 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 23 RTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSR----EQEGARLQQREK----EALEEERQALTLRLEVEQ 94
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIkkatESLEEQLAAAEAeqelEESKRETETGIQNLTAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 95 QQCRTLQEERDEARAGQLSEHRKLEALqvalqEERQAWIKQEHQLKERL-QALQEEGQAQLEREKGNSQREAQAAWETQQ 173
Cdd:COG5185 346 EQGQESLTENLEAIKEEIENIVGEVEL-----SKSSEELDSFKDTIESTkESLDEIPQNQRGYAQEILATLEDTLKAADR 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 174 QFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQMESELAVQLEQRVTERLAEAQE--NSL-RQAASLRDH 250
Cdd:COG5185 421 QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEelTQIeSRVSTLKAT 500
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 26331630 251 HRKQLQELSGQHQ---QELAAQLAQFKVEMADREERQQQVAQD 290
Cdd:COG5185 501 LEKLRAKLERQLEgvrSKLDQVAESLKDFMRARGYAHILALEN 543
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
50-141 |
6.57e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 50 RLEQsLSEAMEALSREQEGA---RLQQREKE--ALEEERQALTLRLEVEQQQCRTLQEERDEARAgqlsEHRKLEALQVA 124
Cdd:COG0542 419 RLEQ-LEIEKEALKKEQDEAsfeRLAELRDElaELEEELEALKARWEAEKELIEEIQELKEELEQ----RYGKIPELEKE 493
|
90
....*....|....*..
gi 26331630 125 LQEERQAWIKQEHQLKE 141
Cdd:COG0542 494 LAELEEELAELAPLLRE 510
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
18-174 |
6.95e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.13 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 18 RHEAERTEVLRGLQEERQAAELTRSKQQEtvtRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQC 97
Cdd:pfam13868 120 EKLEKQRQLREEIDEFNEEQAEWKELEKE---EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKA 196
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26331630 98 RTLQEERDEARAGQLSEHRKLEALQVALQEERQAwIKQEHQLKERLQALQEEGQAQLEREKGNSQREAQAAWETQQQ 174
Cdd:pfam13868 197 QDEKAERDELRAKLYQEEQERKERQKEREEAEKK-ARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAE 272
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
34-318 |
7.24e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 39.25 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 34 RQAAELTRSKQQETVTRLEQSLseaMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQcrtlQEERDEARAGQLS 113
Cdd:pfam15558 7 RKIAALMLARHKEEQRMRELQQ---QAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAE----KEQRKARLGREER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 114 EHRKLEALQVALQEERQAWI--KQEHQLKERLQALQEEG------QAQLEREKGNSQREAQAAWETQQQFALLQTEVRRL 185
Cdd:pfam15558 80 RRADRREKQVIEKESRWREQaeDQENQRQEKLERARQEAeqrkqcQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 186 EGDLDTVRRERDALQLEMSLVQAR---YESQRIQMESELAVQLEQRVT------ERLAEAQENSLRQAASLRDHHRKQLQ 256
Cdd:pfam15558 160 LKEREEQKKVQENNLSELLNHQARkvlVDCQAKAEELLRRLSLEQSLQrsqenyEQLVEERHRELREKAQKEEEQFQRAK 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26331630 257 ELSGQHQQELAAQLAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAE 318
Cdd:pfam15558 240 WRAEEKEEERQEHKEALAELADRKIQQARQVAHKTVQDKAQRARELNLEREKNHHILKLKVE 301
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
94-277 |
7.37e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 38.27 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 94 QQQCRTLQEERDEAR---AGQLSEHRKLEALQVALQEERQAWikqEHQLKERLQALQEE-GQAQLEREKGNsqrEAQAAw 169
Cdd:COG1842 29 DQAIRDMEEDLVEARqalAQVIANQKRLERQLEELEAEAEKW---EEKARLALEKGREDlAREALERKAEL---EAQAE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 170 ETQQQFALLQTEVRRLEGDLDTVRRERDALQLEMSLVQARYESQRIQ---------MESELAV----QLEQRVTERLAEA 236
Cdd:COG1842 102 ALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQekvnealsgIDSDDATsaleRMEEKIEEMEARA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 26331630 237 QE-NSLRQAASLRDhhrkQLQELSGQHqqELAAQLAQFKVEM 277
Cdd:COG1842 182 EAaAELAAGDSLDD----ELAELEADS--EVEDELAALKAKM 217
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
116-231 |
7.47e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 116 RKLEALQVALQEERQAWIK-QEHQLKERLQALQEEgQAQLEREkgnsQREAQAAWETQQQfalLQTEVRRLEGDLDTVRR 194
Cdd:COG0542 414 DELERRLEQLEIEKEALKKeQDEASFERLAELRDE-LAELEEE----LEALKARWEAEKE---LIEEIQELKEELEQRYG 485
|
90 100 110
....*....|....*....|....*....|....*..
gi 26331630 195 ERDALQLEMSLVQARyesqriqmESELAVQLEQRVTE 231
Cdd:COG0542 486 KIPELEKELAELEEE--------LAELAPLLREEVTE 514
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
50-149 |
7.52e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.42 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 50 RLEQSLSEAmEALSREQEGARLQ-QREKEALEEERQALTLRLEVEQQQcrTLQEERDEArAGQLSEHRKLEALQVALQEE 128
Cdd:PRK00409 531 ELEQKAEEA-EALLKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEAQQ--AIKEAKKEA-DEIIKELRQLQKGGYASVKA 606
|
90 100
....*....|....*....|..
gi 26331630 129 RQawIKQEH-QLKERLQALQEE 149
Cdd:PRK00409 607 HE--LIEARkRLNKANEKKEKK 626
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
30-327 |
8.15e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 30 LQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQREKEALEEERQALTLRLEVEQQQCRTLQEERDEARA 109
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 110 gqlsEHRKLEALQVALQEERQAWIKQEHQLKERLQALQEEGQAQLEREKgnsqreaqaawETQQQFALLQTEVRRLEGDL 189
Cdd:COG4372 109 ----EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK-----------ELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 190 DTVRRERDALQLEMSLVQARyesQRIQMESELAVQLEQRVTERLAEAQENSLRQAASLRDHHRKQLQELSGQHQQELAAQ 269
Cdd:COG4372 174 QALSEAEAEQALDELLKEAN---RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 26331630 270 LAQFKVEMADREERQQQVAQDYELRLAREQARVRDLKSGNQQLEEQRAELVERLQAML 327
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-128 |
9.88e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26331630 2 IEQLDKTLARVVEGWNRHEA------ERTEVLRGLQEERQAAELTRSKQQETVTRLEQSLSEAMEALSREQEGARLQQRE 75
Cdd:COG4913 670 IAELEAELERLDASSDDLAAleeqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA 749
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 26331630 76 keALEEERQALTLRlEVEQQQCRTLQEERDEARAGQLSEHRKLEALQVALQEE 128
Cdd:COG4913 750 --LLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| |
