|
Name |
Accession |
Description |
Interval |
E-value |
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
246-425 |
1.93e-32 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 131.72 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 246 QLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA--PAVS 323
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEqpPAGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 324 SEVE------LQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRL------------- 384
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 325511392 385 --------QQLAEPQSDLEELKHEN---KSALQLEQQVK-ELQEKLGQVMETL 425
Cdd:pfam15070 161 lsqnrelkEQLAELQNGFVKLTNENmelTSALQSEQHVKkELAKKLGQLQEEL 213
|
|
| GM130_C |
pfam19046 |
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ... |
586-631 |
2.09e-22 |
|
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.
Pssm-ID: 465957 Cd Length: 46 Bit Score: 90.13 E-value: 2.09e-22
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 325511392 586 SSQDNPTAQPVVQLLGEMQDHQEHPGLGSNCCVPCFCWAWLPRRRR 631
Cdd:pfam19046 1 SPPENPTAQQIMQLLPEIQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-468 |
4.44e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 106 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKD 185
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 186 LAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQI 265
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEEL------------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 266 KGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapAVSSEVELQDLRKELERVAGELQAQ 345
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 346 VENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK--HENKSALQLEQQVKELQEKLGQVME 423
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadYEGFLEGVKAALLLAGLRGLAGAVA 527
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 325511392 424 TLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVEKLELG 468
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-467 |
7.02e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 106 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANnEKQKAERELE-----GQIQRLNTEKKKLNTDLYHMkhslryfE 180
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELElallvLRLEELREELEELQEELKEA-------E 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 181 EESKDLAGRLQRSSQRIGELEwslcavaatqkkkpDGFSSRSKALLKRQ--LEQSIREQILLKGHVTQLKESLKEVQLER 258
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELR--------------LEVSELEEEIEELQkeLYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 259 DQYAEQIkgerAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavsSEVELQDLRKELERV 338
Cdd:TIGR02168 319 EELEAQL----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----------LESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 339 AGEL-----QAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAL-QLEQQVK 412
Cdd:TIGR02168 385 RSKVaqlelQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELeRLEEALE 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 325511392 413 ELQEKLGQVMETLTSAEKEPEAAvpasgtGGESSGLMDLLEEKADLREHVEKLEL 467
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQL------QARLDSLERLQENLEGFSEGVKALLK 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-466 |
1.23e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 120 IKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQRSSQRIGE 199
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 200 LEWSLcAVAATQKKKPDGFSSRSKAL----------LKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGER 269
Cdd:TIGR02168 759 LEAEI-EELEERLEEAEEELAEAEAEieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 270 AQW---QQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAeplppdapavSSEVELQDLRKELERVAGELQaqv 346
Cdd:TIGR02168 838 RRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA----------SLEEALALLRSELEELSEELR--- 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 347 ENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEE--LKHENK---SALQLEQQVKELQEKLGQV 421
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaEALENKiedDEEEARRRLKRLENKIKEL 984
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 325511392 422 METLTSAEKEPEAavpasgtggESSGLMDLLEEKADLREHVEKLE 466
Cdd:TIGR02168 985 GPVNLAAIEEYEE---------LKERYDFLTAQKEDLTEAKETLE 1020
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-466 |
6.29e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 112 KISRLNDTIKS---LKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTdlyhMKHSLRYFEEESKDLAG 188
Cdd:PRK03918 177 RIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 189 RLQRSSQRIGELEWSLcavaATQKKKPDGFSSRSKALlkRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGE 268
Cdd:PRK03918 253 SKRKLEEKIRELEERI----EELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 269 RAQWQQRmRKMSQEVCTLKEEKKHDTHRVEELERS-------------LSRLKNQMAEPLPPDAPAVSSEV-----ELQD 330
Cdd:PRK03918 327 EERIKEL-EEKEERLEELKKKLKELEKRLEELEERhelyeeakakkeeLERLKKRLTGLTPEKLEKELEELekakeEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 331 LRKELERVAGELQAQV-ENNQCISLLNR--------GQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHEN 401
Cdd:PRK03918 406 EISKITARIGELKKEIkELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 325511392 402 KSALQLE----------QQVKELQEKLGQV-METLTSAEKEPEAAVPAS-GTGGESSGLMDLLEEKADLREHVEKLE 466
Cdd:PRK03918 486 EKVLKKEseliklkelaEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLiKLKGEIKSLKKELEKLEELKKKLAELE 562
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
120-431 |
1.49e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 120 IKSLKQQKKQ----VEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLyhmkhslRYFEEESKDLAGRLQRSSQ 195
Cdd:COG1196 202 LEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 196 RIGELEWslcAVAATQKKKpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIkgerAQWQQR 275
Cdd:COG1196 275 ELEELEL---ELEEAQAEE---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 276 MRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavssevELQDLRKELERVAGELQAQVENNQCISLL 355
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-------------AEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 325511392 356 NRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQVKELQEKLGQVMETLTSAEKE 431
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
101-489 |
4.79e-05 |
|
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: 46.50 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 101 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHmkhsLRYFE 180
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----YLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 181 EESKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSKalLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQ 260
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESS------KQEIEKEEEKLAQVLK--ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 261 YAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELErvAG 340
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES--ER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 341 ELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKhENKSALQLEQQVKELQEKLGQ 420
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325511392 421 VMETLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVE--KLELGFIQYRRERCHQKVHRLLTEPG 489
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglKVLLALIKDGVGGRIISAHGRLGDLG 535
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
100-348 |
4.31e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 100 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQ-------VEHQLEEEKKANNEKQKAE--RELEGQIQRLNTEKKKLNTDLY 170
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKlrkelreLEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEEY 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 171 H-MKHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPD--------GFSSRSKALLK-RQLEQSIREQILL 240
Cdd:PRK03918 528 EkLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllkeleelGFESVEELEERlKELEPFYNEYLEL 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 241 KGHVTQLKESLKEVQLERDQyAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHR-----VEELERSLSRLKNQMAepl 315
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEE-LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELE--- 683
|
250 260 270
....*....|....*....|....*....|...
gi 325511392 316 ppdapavssevELQDLRKELERVAGELQAQVEN 348
Cdd:PRK03918 684 -----------ELEKRREEIKKTLEKLKEELEE 705
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
99-201 |
1.15e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 41.57 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 99 CQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNtdlyhmkhslRY 178
Cdd:smart00435 265 CNHQRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKK----------KE 334
|
90 100
....*....|....*....|...
gi 325511392 179 FEEESKDLAgRLQRSSQRIGELE 201
Cdd:smart00435 335 KKKEEKKKK-QIERLEERIEKLE 356
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
246-425 |
1.93e-32 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 131.72 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 246 QLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA--PAVS 323
Cdd:pfam15070 1 QLMESLKQLQTERDQYAENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEqpPAGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 324 SEVE------LQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRL------------- 384
Cdd:pfam15070 81 SEEEqrlqeeAEQLQKELEALAGQLQAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILedmqsdratisra 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 325511392 385 --------QQLAEPQSDLEELKHEN---KSALQLEQQVK-ELQEKLGQVMETL 425
Cdd:pfam15070 161 lsqnrelkEQLAELQNGFVKLTNENmelTSALQSEQHVKkELAKKLGQLQEEL 213
|
|
| GM130_C |
pfam19046 |
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 ... |
586-631 |
2.09e-22 |
|
GM130 C-terminal binding motif; This entry represents the C-terminal motif from the GM130 protein that is bound by the GRASP65 PDZ domain pfam04495.
Pssm-ID: 465957 Cd Length: 46 Bit Score: 90.13 E-value: 2.09e-22
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 325511392 586 SSQDNPTAQPVVQLLGEMQDHQEHPGLGSNCCVPCFCWAWLPRRRR 631
Cdd:pfam19046 1 SPPENPTAQQIMQLLPEIQNPQEHPGLGSNPCIPFFYRADENDEVK 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
106-468 |
4.44e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 106 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKD 185
Cdd:COG1196 227 AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 186 LAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQI 265
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEEL------------EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 266 KGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapAVSSEVELQDLRKELERVAGELQAQ 345
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-------LEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 346 VENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK--HENKSALQLEQQVKELQEKLGQVME 423
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEadYEGFLEGVKAALLLAGLRGLAGAVA 527
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 325511392 424 TLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVEKLELG 468
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
92-313 |
1.15e-10 |
|
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: 63.63 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 92 LHARQSPCQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYH 171
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 172 MKHSLryfEEESKDLAGRLqRSSQRIGELEWSLCAVAAtqkKKPDGFSSRSKAL--LKRQLEQSIREQILLKGHVTQLKE 249
Cdd:COG4942 95 LRAEL---EAQKEELAELL-RALYRLGRQPPLALLLSP---EDFLDAVRRLQYLkyLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 325511392 250 SLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAE 313
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
106-467 |
7.02e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 106 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANnEKQKAERELE-----GQIQRLNTEKKKLNTDLYHMkhslryfE 180
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELElallvLRLEELREELEELQEELKEA-------E 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 181 EESKDLAGRLQRSSQRIGELEwslcavaatqkkkpDGFSSRSKALLKRQ--LEQSIREQILLKGHVTQLKESLKEVQLER 258
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELR--------------LEVSELEEEIEELQkeLYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 259 DQYAEQIkgerAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavsSEVELQDLRKELERV 338
Cdd:TIGR02168 319 EELEAQL----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----------LESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 339 AGEL-----QAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAL-QLEQQVK 412
Cdd:TIGR02168 385 RSKVaqlelQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELeRLEEALE 464
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 325511392 413 ELQEKLGQVMETLTSAEKEPEAAvpasgtGGESSGLMDLLEEKADLREHVEKLEL 467
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQL------QARLDSLERLQENLEGFSEGVKALLK 513
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
120-466 |
1.23e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 120 IKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQRSSQRIGE 199
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 200 LEWSLcAVAATQKKKPDGFSSRSKAL----------LKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGER 269
Cdd:TIGR02168 759 LEAEI-EELEERLEEAEEELAEAEAEieeleaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 270 AQW---QQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAeplppdapavSSEVELQDLRKELERVAGELQaqv 346
Cdd:TIGR02168 838 RRLedlEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA----------SLEEALALLRSELEELSEELR--- 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 347 ENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEE--LKHENK---SALQLEQQVKELQEKLGQV 421
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeaEALENKiedDEEEARRRLKRLENKIKEL 984
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 325511392 422 METLTSAEKEPEAavpasgtggESSGLMDLLEEKADLREHVEKLE 466
Cdd:TIGR02168 985 GPVNLAAIEEYEE---------LKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-435 |
8.80e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 8.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 112 KISRLNDTIKSLKQQKKQVE---HQLEEEKKANNEKQKAE-RELEGQIQRLNTEKKKLNTDLYHMkhslryfEEESKDLA 187
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRrerEKAERYQALLKEKREYEgYELLKEKEALERQKEAIERQLASL-------EEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 188 GRLQRSSQRIGELEWSLCAVAATQKKKPDGFSSRSK---ALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQY--- 261
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKekiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlae 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 262 AEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKnqmaeplppdapavsseVELQDLRKELERVAGE 341
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR-----------------DELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 342 LQAqvennqcislLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQ-----------LEQQ 410
Cdd:TIGR02169 401 INE----------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWkleqlaadlskYEQE 470
|
330 340
....*....|....*....|....*
gi 325511392 411 VKELQEKLGQVMETLTSAEKEPEAA 435
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-466 |
3.58e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 112 KISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQ 191
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 192 RSSQRIGELEWSLCAVAAtQKKKPDGFSSRSKALLKRQLEQSIREQIL-LKGHVTQLKESLKEVQLERdQYAEQikgERA 270
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEE-ALNDLEARLSHSRIPEIQAELSKLEEEVSrIEARLREIEQKLNRLTLEK-EYLEK---EIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 271 QWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavsSEVELQDLRKELERVAGELQAQVENNQ 350
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD----------LESRLGDLKKERDELEAQLRELERKIE 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 351 CIsllnrgqKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQVKELQEKLGQVMETLTSAEK 430
Cdd:TIGR02169 907 EL-------EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
330 340 350
....*....|....*....|....*....|....*.
gi 325511392 431 EPEAAVPASGTGGESsgLMDLLEEKADLREHVEKLE 466
Cdd:TIGR02169 980 EYEEVLKRLDELKEK--RAKLEEERKAILERIEEYE 1013
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-466 |
6.29e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 112 KISRLNDTIKS---LKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTdlyhMKHSLRYFEEESKDLAG 188
Cdd:PRK03918 177 RIERLEKFIKRtenIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE----LKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 189 RLQRSSQRIGELEWSLcavaATQKKKPDGFSSRSKALlkRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGE 268
Cdd:PRK03918 253 SKRKLEEKIRELEERI----EELKKEIEELEEKVKEL--KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 269 RAQWQQRmRKMSQEVCTLKEEKKHDTHRVEELERS-------------LSRLKNQMAEPLPPDAPAVSSEV-----ELQD 330
Cdd:PRK03918 327 EERIKEL-EEKEERLEELKKKLKELEKRLEELEERhelyeeakakkeeLERLKKRLTGLTPEKLEKELEELekakeEIEE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 331 LRKELERVAGELQAQV-ENNQCISLLNR--------GQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHEN 401
Cdd:PRK03918 406 EISKITARIGELKKEIkELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 325511392 402 KSALQLE----------QQVKELQEKLGQV-METLTSAEKEPEAAVPAS-GTGGESSGLMDLLEEKADLREHVEKLE 466
Cdd:PRK03918 486 EKVLKKEseliklkelaEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLiKLKGEIKSLKKELEKLEELKKKLAELE 562
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-336 |
1.94e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 100 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYF 179
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 180 EEESKDLAGRLQRSSQRIGELEwslcAVAATQKKKPDGFSSRSKALLKRQLEQSIREQILLK--GHVTQLKESLKEVQLE 257
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAE----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEaeEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 325511392 258 RDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELE 336
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
112-417 |
5.06e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.63 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 112 KISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQ 191
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIK 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 192 RSSQRIGELEWSLCAVAATQKKKPDGFSSRSKAllKRQLEQSIREqilLKGHVTQLKESLKEVQLErdqyAEQIKGERAQ 271
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ--DSVKELIIKN---LDNTRESLETQLKVLSRS----INKIKQNLEQ 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 272 WQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapaVSSEV-----ELQDLRKELERVAGELQAQV 346
Cdd:TIGR04523 487 KQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK--------LESEKkekesKISDLEDELNKDDFELKKEN 558
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 325511392 347 ------ENNQCISLLNRGQKerlreqeerlqEQQERLREREKRLQQLAEPQSDL-EELKHENKSALQLEQQVKELQEK 417
Cdd:TIGR04523 559 lekeidEKNKEIEELKQTQK-----------SLKKKQEEKQELIDQKEKEKKDLiKEIEEKEKKISSLEKELEKAKKE 625
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-337 |
1.07e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 112 KISRLNDTIKSLKQQKKQVEHQLEEEKKANNEkQKAERE-LEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRL 190
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAE-AEAEIEeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 191 QRSSQRIGELEWSLCAVAATQKKKPDGFSSRSKALlkRQLEQSIREQIllkghvTQLKESLKEVQlERDQYAEQIKGERA 270
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEI--EELEELIEELE------SELEALLNERA-SLEEALALLRSELE 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 271 QWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKN-----------------QMAEPLPPDAPAVSSEVE--LQDL 331
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVridnlqerlseeysltlEEAEALENKIEDDEEEARrrLKRL 977
|
....*.
gi 325511392 332 RKELER 337
Cdd:TIGR02168 978 ENKIKE 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
106-466 |
1.08e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 106 LNSRSIKISRLN-----DTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFE 180
Cdd:TIGR04523 290 LNQLKSEISDLNnqkeqDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 181 EESKDLAGRLQRSSQRIGELEWSlcavaatqkkkpdgfssrskallKRQLEQSIREQillKGHVTQLKESLKEVQLERDQ 260
Cdd:TIGR04523 370 NEIEKLKKENQSYKQEIKNLESQ-----------------------INDLESKIQNQ---EKLNQQKDEQIKKLQQEKEL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 261 YAEQIKGERAQwqqrMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLppdAPAVSSEVELQDLRKELERVAG 340
Cdd:TIGR04523 424 LEKEIERLKET----IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS---RSINKIKQNLEQKQKELKSKEK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 341 ELQAQVENNqciSLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSAlQLEQQVKELQEKLGQ 420
Cdd:TIGR04523 497 ELKKLNEEK---KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKE-NLEKEIDEKNKEIEE 572
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 325511392 421 VMETLTSAEKEPEaavpasgtggESSGLMDLLE-EKADLREHVEKLE 466
Cdd:TIGR04523 573 LKQTQKSLKKKQE----------EKQELIDQKEkEKKDLIKEIEEKE 609
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
96-431 |
1.27e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 96 QSPCQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKK-LNTDLyhmKH 174
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdWNKEL---KS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 175 SLRYFEEESKDLAGRLQRSSQRIGELEWSlcaVAATQKKKPDGFSSRSKalLKRQLEQSIREQILLKGHVTQLKESLKEV 254
Cdd:TIGR04523 315 ELKNQEKKLEEIQNQISQNNKIISQLNEQ---ISQLKKELTNSESENSE--KQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 255 QLER---DQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAeplppdapavssevELQDL 331
Cdd:TIGR04523 390 ESQIndlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS--------------VKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 332 RKELERVAGELQAQvennqcISLLNRGQKERLREQEERLqeqqerlrerekrlQQLAEPQSDLEELKHENKsalQLEQQV 411
Cdd:TIGR04523 456 IKNLDNTRESLETQ------LKVLSRSINKIKQNLEQKQ--------------KELKSKEKELKKLNEEKK---ELEEKV 512
|
330 340
....*....|....*....|
gi 325511392 412 KELQEKLGQVMETLTSAEKE 431
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESE 532
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
120-431 |
1.49e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 120 IKSLKQQKKQ----VEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLyhmkhslRYFEEESKDLAGRLQRSSQ 195
Cdd:COG1196 202 LEPLERQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAEL-------EELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 196 RIGELEWslcAVAATQKKKpdgfssrskALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIkgerAQWQQR 275
Cdd:COG1196 275 ELEELEL---ELEEAQAEE---------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL----EELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 276 MRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEplppdapavssevELQDLRKELERVAGELQAQVENNQCISLL 355
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-------------AEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 325511392 356 NRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQVKELQEKLGQVMETLTSAEKE 431
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
92-400 |
3.16e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 92 LHARQSPCQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLE--EEKKANN--EKQKAERELEGQIQRLNTEKKKLNt 167
Cdd:TIGR02169 704 LDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSslEQEIENVksELKELEARIEELEEDLHKLEEALN- 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 168 DLYHM--KHSLRYFEEESKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSK--------ALLKRQLEQSIREQ 237
Cdd:TIGR02169 783 DLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIE------QKLNRLTLEKEYLEKEiqelqeqrIDLKEQIKSIEKEI 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 238 ILLKGHVTQLKESLKEVQLERDQYAEQ---IKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAE- 313
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEi 936
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 314 --PLPPDAPAVSSEVELQDLRKELERVAGELQAQVE-NNQCISLLNRGQKERLREQEERL--QEQQErlrerekrlqQLA 388
Cdd:TIGR02169 937 edPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDELKEKRAklEEERK----------AIL 1006
|
330
....*....|..
gi 325511392 389 EPQSDLEELKHE 400
Cdd:TIGR02169 1007 ERIEEYEKKKRE 1018
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
101-489 |
4.79e-05 |
|
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: 46.50 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 101 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHmkhsLRYFE 180
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----YLKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 181 EESKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSKalLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQ 260
Cdd:pfam02463 236 EERIDLLQELLRDEQEEIESS------KQEIEKEEEKLAQVLK--ENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 261 YAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELErvAG 340
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES--ER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 341 ELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKhENKSALQLEQQVKELQEKLGQ 420
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325511392 421 VMETLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVE--KLELGFIQYRRERCHQKVHRLLTEPG 489
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglKVLLALIKDGVGGRIISAHGRLGDLG 535
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
106-433 |
7.53e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 106 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQR-------------LNTEKKKLNTDLYHM 172
Cdd:PRK03918 233 LEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkelkekaeeyikLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 173 KHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKK----KPDGFS-SRSKALLKRQLEQSIREQILLKGHVTQL 247
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRleelEERHELyEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 248 KESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKH---------DTHRVEELER---SLSRLKNQMAEpl 315
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreltEEHRKELLEEytaELKRIEKELKE-- 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 316 ppdapavsSEVELQDLRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLE 395
Cdd:PRK03918 471 --------IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
330 340 350
....*....|....*....|....*....|....*...
gi 325511392 396 ELKHENKSALQLEQQVKELQEKLGQVMETLTSAEKEPE 433
Cdd:PRK03918 543 SLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE 580
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
101-274 |
7.83e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 101 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAER---ELEGQIQRLNTEKKKLNTDLYHMKHSLR 177
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleELEEQLETLRSKVAQLELQIASLNNEIE 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 178 YFEEESKDLAGRLQRSSQRIGELEWSLcavaatqkkkpdgfSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLE 257
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKL--------------EEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
170
....*....|....*..
gi 325511392 258 RDQYAEQIKGERAQWQQ 274
Cdd:TIGR02168 470 LEEAEQALDAAERELAQ 486
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
102-336 |
8.37e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 102 QAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEekkannekqkAERELEGqiqrlntekkklntdlYHMKHSLRYFEE 181
Cdd:COG3206 159 EAYLEQNLELRREEARKALEFLEEQLPELRKELEE----------AEAALEE----------------FRQKNGLVDLSE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 182 ESKDLAGRLQRSSQRIGELEWSLCAVAATQkkkpdgfssrskALLKRQLEQSIREQILLKGH--VTQLKESLKEVQLERD 259
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELAEAEARL------------AALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 260 QYAE----------QIKGERAQWQQRMRKMSQEVC-TLKEEKKHDTHRVEELERSLSRLKNQMAEplppdAPAVssEVEL 328
Cdd:COG3206 281 ELSArytpnhpdviALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEARLAE-----LPEL--EAEL 353
|
....*...
gi 325511392 329 QDLRKELE 336
Cdd:COG3206 354 RRLEREVE 361
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
114-443 |
1.43e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 114 SRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKlntdlyhmkhslryfEEESKDLAGRLQRS 193
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK---------------AEEDKNMALRKAEE 1585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 194 SQRIGELEWSLCAVAATQKKKpdgfsSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKgeRAQWQ 273
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKK-----MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK--KAEEE 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 274 QRMRKMSQEVCTLKEEKKHDTHRVEELErslsrlKNQMAEPLPPDAPAVSSEVELQDLRKELERVAGELQAQVENNQcis 353
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK--- 1729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 354 lLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALqLEQQVKELQEKLGQVMETLTSAEKEPE 433
Cdd:PTZ00121 1730 -IKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
330
....*....|
gi 325511392 434 AAVPASGTGG 443
Cdd:PTZ00121 1808 ANIIEGGKEG 1817
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
111-313 |
2.11e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 111 IKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRL 190
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 191 QRSSQRIGELEwslcavaaTQKKKPDgfSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGERA 270
Cdd:TIGR04523 534 KEKESKISDLE--------DELNKDD--FELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 325511392 271 QWQQRMRKMSQ---EVCTLKEEKKhdthRVEELERSLSRLKNQMAE 313
Cdd:TIGR04523 604 EIEEKEKKISSlekELEKAKKENE----KLSSIIKNIKSKKNKLKQ 645
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
217-467 |
3.14e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 217 GFSSRSKALLKRQLE-QSIREQI-LLKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQ---EVCTLKEEKK 291
Cdd:TIGR02168 664 GSAKTNSSILERRREiEELEEKIeELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAlrkDLARLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 292 HDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQDLRKELERVAGELQAQVENNQCISllnRGQKERLREQEERLQ 371
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL---DELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 372 EQQERLREREKRL-----------QQLAEPQSDLEELKHE----NKSALQLEQQVKELQEKLGQVMETLTSAEKEPEAAv 436
Cdd:TIGR02168 821 NLRERLESLERRIaaterrledleEQIEELSEDIESLAAEieelEELIEELESELEALLNERASLEEALALLRSELEEL- 899
|
250 260 270
....*....|....*....|....*....|.
gi 325511392 437 pASGTGGESSGLMDLLEEKADLREHVEKLEL 467
Cdd:TIGR02168 900 -SEELRELESKRSELRRELEELREKLAQLEL 929
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
100-348 |
4.31e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 100 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQ-------VEHQLEEEKKANNEKQKAE--RELEGQIQRLNTEKKKLNTDLY 170
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKlrkelreLEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEEY 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 171 H-MKHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPD--------GFSSRSKALLK-RQLEQSIREQILL 240
Cdd:PRK03918 528 EkLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAEllkeleelGFESVEELEERlKELEPFYNEYLEL 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 241 KGHVTQLKESLKEVQLERDQyAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHR-----VEELERSLSRLKNQMAepl 315
Cdd:PRK03918 608 KDAEKELEREEKELKKLEEE-LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELE--- 683
|
250 260 270
....*....|....*....|....*....|...
gi 325511392 316 ppdapavssevELQDLRKELERVAGELQAQVEN 348
Cdd:PRK03918 684 -----------ELEKRREEIKKTLEKLKEELEE 705
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
100-329 |
4.58e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 100 QEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLyhmkhslryf 179
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 180 eeesKDLAGRLQRSSQRIGELEwslcavAATQKKKPDGFSSRSKAL--LKRQLEQSIREQILLKGHVTQLKESLKEVQLE 257
Cdd:COG3883 89 ----GERARALYRSGGSVSYLD------VLLGSESFSDFLDRLSALskIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325511392 258 RDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQ 329
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
101-433 |
5.52e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 101 EQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAeRELEGQIQRLNTEKK-----KLNTDLYHMKHS 175
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTgltpeKLEKELEELEKA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 176 LRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPdgfssrskaLLKRQLEQSIREQILLKGHVtQLKESLKEVQ 255
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP---------VCGRELTEEHRKELLEEYTA-ELKRIEKELK 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 256 ----LERDQYAEQIKGERAQWQQR----MRKMSQEVCTLKEE-KKHDTHRVEELERSLSRLKNQMAEpLPPDAPAVSSEV 326
Cdd:PRK03918 470 eieeKERKLRKELRELEKVLKKESelikLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIK-LKGEIKSLKKEL 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 327 E-LQDLRKELERVAGELQAQVENNQCI--SLLNRGQKERLREQeerlqeqqerlrereKRLQQLAEPQSDLEELKHENKS 403
Cdd:PRK03918 549 EkLEELKKKLAELEKKLDELEEELAELlkELEELGFESVEELE---------------ERLKELEPFYNEYLELKDAEKE 613
|
330 340 350
....*....|....*....|....*....|
gi 325511392 404 ALQLEQQVKELQEKLGQVMETLTSAEKEPE 433
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLE 643
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
226-325 |
7.47e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 7.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 226 LKRQLEQ-SIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRmRKMSQEVCTLKEEKKHDTHRVEELERSL 304
Cdd:COG0542 416 LERRLEQlEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAE-KELIEEIQELKEELEQRYGKIPELEKEL 494
|
90 100
....*....|....*....|.
gi 325511392 305 SRLKNQMAEPLPPDAPAVSSE 325
Cdd:COG0542 495 AELEEELAELAPLLREEVTEE 515
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
106-431 |
9.82e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 106 LNSRSIKISRLNDTIKSLKQQ-KKQVEHQLEEEKKANNEKQKAErELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESK 184
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNESLEKVS-SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVS 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 185 DLAGRLQRSSQrigelewslcAVAATQKKKPdgfSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAE- 263
Cdd:pfam15921 500 DLTASLQEKER----------AIEATNAEIT---KLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEi 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 264 ---------QIKG-----------ERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVS 323
Cdd:pfam15921 567 lrqqienmtQLVGqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 324 SeveLQDLRKELERVAGELQaqvennQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELK----- 398
Cdd:pfam15921 647 A---VKDIKQERDQLLNEVK------TSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRntlks 717
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 325511392 399 ------HENKSALQLEQQVK-------ELQEKLGQVMETLTSAEKE 431
Cdd:pfam15921 718 megsdgHAMKVAMGMQKQITakrgqidALQSKIQFLEEAMTNANKE 763
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
112-433 |
1.11e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 112 KISRLNDTIKSLKQQKK-----QVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDL----------------- 169
Cdd:PRK03918 366 EAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrel 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 170 --YHMKHSLRYFEEESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKPDGFSSRSKALLKRQLEQSI------------- 234
Cdd:PRK03918 446 teEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLkkynleelekkae 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 235 ------REQILLKGHVTQLKESLKEvqlerdqyAEQIKGERAQWQQRMRKMSQEVCTL-KEEKKHDTHRVEELERSLSRL 307
Cdd:PRK03918 526 eyeklkEKLIKLKGEIKSLKKELEK--------LEELKKKLAELEKKLDELEEELAELlKELEELGFESVEELEERLKEL 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 308 KNQMAEPLPpdapAVSSEVELQDLRKELERVAGELQAQVENnqcislLNRGQKERLREQEERLQEQQERLREREKRL-QQ 386
Cdd:PRK03918 598 EPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEE------LAETEKRLEELRKELEELEKKYSEEEYEELrEE 667
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 325511392 387 LAEPQSDLEELKHENKSALQLEQQVKELQEKLGQVMETLTSAEKEPE 433
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
99-201 |
1.15e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 41.57 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 99 CQEQAAVLNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNtdlyhmkhslRY 178
Cdd:smart00435 265 CNHQRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKK----------KE 334
|
90 100
....*....|....*....|...
gi 325511392 179 FEEESKDLAgRLQRSSQRIGELE 201
Cdd:smart00435 335 KKKEEKKKK-QIERLEERIEKLE 356
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
240-433 |
1.30e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 240 LKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDA 319
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 320 ---PAVSSEVELQDLR-KELERVAGELQAQVENnqcisllnRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLE 395
Cdd:pfam12128 347 eqlPSWQSELENLEERlKALTGKHQDVTAKYNR--------RRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQ 418
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 325511392 396 ELKHE-----NKSALQLEQQVKELQEKLGQVMETLTSAEKEPE 433
Cdd:pfam12128 419 ALESElreqlEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
114-431 |
1.56e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 114 SRLNDTIKSLKQQKKQVEH---QLEEEKKANNEKQKAERELEG-QIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGR 189
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKKAEEakkKAEEAKKADEAKKKAEEAKKAdEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 190 LQRSSQRIGELEWSLCAVAATQKKKPDGFSSRS---KALLKRQLEQSIREQ-----------ILLKGHVTQLKESLKEVQ 255
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEelkKAEEKKKAEEAKKAEedknmalrkaeEAKKAEEARIEEVMKLYE 1602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 256 LERDQYAEQIKGE-----RAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQMAEPLPPDAPAVSSEVELQD 330
Cdd:PTZ00121 1603 EEKKMKAEEAKKAeeakiKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 331 LRKELERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQ 410
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHL 1762
|
330 340
....*....|....*....|.
gi 325511392 411 VKELQEKLGQVMETLTSAEKE 431
Cdd:PTZ00121 1763 KKEEEKKAEEIRKEKEAVIEE 1783
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
123-345 |
1.69e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.39 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 123 LKQQKKQVEHQL-EEEKKANNEKQKAERELEGQIQRLNTEKKKLNTD-LYHMKHSLRYFEEEskdLAGRLQRSSQRIGEL 200
Cdd:PRK00106 26 MKSAKEAAELTLlNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKElLLEAKEEARKYREE---IEQEFKSERQELKQI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 201 EWSLCAVAATQKKKPDGFSSRSKALlkRQLEQSIREQillKGHVTqlkeslkevqlERDQYAEQIKGERAQWQQRMRKMS 280
Cdd:PRK00106 103 ESRLTERATSLDRKDENLSSKEKTL--ESKEQSLTDK---SKHID-----------EREEQVEKLEEQKKAELERVAALS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325511392 281 QEVC---TLKEEKKHDTH----RVEELERSLSRLKNQMAEPLppdapavssevelqdLRKELERVAGELQAQ 345
Cdd:PRK00106 167 QAEAreiILAETENKLTHeiatRIREAEREVKDRSDKMAKDL---------------LAQAMQRLAGEYVTE 223
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
125-301 |
1.96e-03 |
|
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: 41.49 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 125 QQKKQVEHQLEEEKKANNEKQKAERELEGqiqrLNTEKKKLNTDLYHMKHSLRYFEEESK-------DLAGRLQRSSQRI 197
Cdd:TIGR00618 670 LPKELLASRQLALQKMQSEKEQLTYWKEM----LAQCQTLLRELETHIEEYDREFNEIENassslgsDLAAREDALNQSL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 198 GELE----WSLCAVAATQKKKpdgfSSRSKALLKR-----QLEQSIREQI-LLKGHVTQLKESLKEVQLERDQYA----- 262
Cdd:TIGR00618 746 KELMhqarTVLKARTEAHFNN----NEEVTAALQTgaelsHLAAEIQFFNrLREEDTHLLKTLEAEIGQEIPSDEdilnl 821
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 325511392 263 --EQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELE 301
Cdd:TIGR00618 822 qcETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
92-350 |
1.98e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 92 LHARQSPCQEQAAVLNSRSIKISRLNDTI---KSLKQQKKQVEhqleeekKANNEKQKAERELEGQIQRLNTEKKKLNTD 168
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKILaedEKLLDEKKQFE-------KIAEELKGKEQELIFLLQAREKEIHDLEIQ 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 169 LYHMKHSLRYFEEESKDLAGRLQRSSQRIGELEwSLCAVAATQKKKPDGFSSRSKALLKRQLEQSI-----REQIL---- 239
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT-AHCDKLLLENKELTQEASDMTLELKKHQEDIInckkqEERMLkqie 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 240 -LKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRlKNQMAEPLPPD 318
Cdd:pfam05483 538 nLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN-KNKNIEELHQE 616
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 325511392 319 APAVSS------------EVELQDLRKELERVAGELQAQVENNQ 350
Cdd:pfam05483 617 NKALKKkgsaenkqlnayEIKVNKLELELASAKQKFEEIIDNYQ 660
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-426 |
2.08e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 108 SRSIKISRLNDTIKSLKQQKKqvEHQLEEEKKANNEKQKAERE---LEGQIQRLNTEKKKLNTdlyhMKHSLRYFEEESK 184
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLK--KYNLEELEKKAEEYEKLKEKlikLKGEIKSLKKELEKLEE----LKKKLAELEKKLD 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 185 DLAGRLQRSSQRIGELewslcavaatqkkkpdGFSSRSKALLK-RQLEQSIREQILLKGHVTQLKESLKEVQLERDQyAE 263
Cdd:PRK03918 567 ELEEELAELLKELEEL----------------GFESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKLEEE-LD 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 264 QIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHR-----VEELERSLSRLKNQMAEplppdapavsseveLQDLRKELERV 338
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSEEEYEelreeYLELSRELAGLRAELEE--------------LEKRREEIKKT 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 339 AGELQAQvennqcisllnrgqkerlreqeerlqeqQERLREREKRLQQLAEPQSDLEELKHENKS--ALQLEQQVKELQE 416
Cdd:PRK03918 696 LEKLKEE----------------------------LEEREKAKKELEKLEKALERVEELREKVKKykALLKERALSKVGE 747
|
330
....*....|
gi 325511392 417 KLGQVMETLT 426
Cdd:PRK03918 748 IASEIFEELT 757
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
106-487 |
4.54e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 106 LNSRSIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYfEEESKD 185
Cdd:TIGR00606 171 LKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-ENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 186 LAGRLQRSSQ---RIGELEWSLCAVAATQKKKPDgfssrskalLKRQLEQsIREQILLKghvtqLKESLKEVQLERDQYA 262
Cdd:TIGR00606 250 LKNRLKEIEHnlsKIMKLDNEIKALKSRKKQMEK---------DNSELEL-KMEKVFQG-----TDEQLNDLYHNHQRTV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 263 EQIKGERAQWQQRMRKMSQEVCTLKEEKKhdthrveELERSLSRLKNQmAEPLPPDAPAVSSEVELQDLRKELERVAGEL 342
Cdd:TIGR00606 315 REKERELVDCQRELEKLNKERRLLNQEKT-------ELLVEQGRLQLQ-ADRHQEHIRARDSLIQSLATRLELDGFERGP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 343 QAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRLQQLAEPQSDL---------------EELKHENKSALQL 407
Cdd:TIGR00606 387 FSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLgrtielkkeilekkqEELKFVIKELQQL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 408 EQQVKELQEKlgqvMETLTSAEKEPEAAVPASGTGGESSGLMDLLEEKADLREHVEKLELGFIQYRRERCHQKVHRLLTE 487
Cdd:TIGR00606 467 EGSSDRILEL----DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK 542
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
110-418 |
4.75e-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: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 110 SIKISRLNDTIKSLKQQKKQVEHQLEEEKKANNEKQKAERELEgQIQRLNTEKKKL--------NTDLYHMKHSLRYFEE 181
Cdd:COG5185 204 VNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELE-DLAQTSDKLEKLveqntdlrLEKLGENAESSKRLNE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 182 ESKDLAGRLQRSSQRIGELEWSLCAVAATQKKKpdgfSSRSKALLKRQLEQSIREQ---IL-LKGHVTQLKESLKEVQLE 257
Cdd:COG5185 283 NANNLIKQFENTKEKIAEYTKSIDIKKATESLE----EQLAAAEAEQELEESKRETetgIQnLTAEIEQGQESLTENLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 258 RDQYAEQIKGERA--QWQQRMRKMSQEVCTLKEEkkhdthrVEELERSLSRLKNQMAEplppdapAVSSEVELQDlrKEL 335
Cdd:COG5185 359 IKEEIENIVGEVElsKSSEELDSFKDTIESTKES-------LDEIPQNQRGYAQEILA-------TLEDTLKAAD--RQI 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 336 ERVAGELQAQVENNQCISLLNRGQKERLREQEERLQEQQERLREREKRlqqlAEPQSDLEELKHENKSALQLEQQVKELQ 415
Cdd:COG5185 423 EELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYD----EINRSVRSKKEDLNEELTQIESRVSTLK 498
|
...
gi 325511392 416 EKL 418
Cdd:COG5185 499 ATL 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
219-442 |
5.51e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.36 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 219 SSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIkgerAQWQQRMRKMSQEVCTLKEEKKHDTHRVE 298
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 299 ELERSLSRLKNQMAEPL---------PPDAPAVSSEVELQDLRKE--LERVAGELQAQVE----NNQCISLLNRGQKERL 363
Cdd:COG4942 94 ELRAELEAQKEELAELLralyrlgrqPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEelraDLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 364 REQEERLQEQQERLREREKRLQQLAEPQSDLE-ELKHENKSALQLEQQVKELQEKLGQVMETLTSAEKEPEAAVPASGTG 442
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEkELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
106-289 |
6.49e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.53 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 106 LNSRSIKISRLNDTIKS-------LKQQKKQVEHQLEEE--KKANNEKQKAERE---LEGQIQRLNTEKKKLNTDLYHMK 173
Cdd:PRK05771 48 LRSLLTKLSEALDKLRSylpklnpLREEKKKVSVKSLEEliKDVEEELEKIEKEikeLEEEISELENEIKELEQEIERLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 174 hSLRYFEEESKDL---------AGRLQRSSQRIGELEWSLC-------------AVAATQKKKPDgfsSRSKALLKRQLE 231
Cdd:PRK05771 128 -PWGNFDLDLSLLlgfkyvsvfVGTVPEDKLEELKLESDVEnveyistdkgyvyVVVVVLKELSD---EVEEELKKLGFE 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325511392 232 qsiREQILLKGHVTQ----LKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEE 289
Cdd:PRK05771 204 ---RLELEEEGTPSElireIKEELEEIEKERESLLEELKELAKKYLEELLALYEYLEIELER 262
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
109-310 |
6.75e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 109 RSIKISRLNDTIKSL-KQQKKQVEHQLEEEKKANNEKQKAE------RELEGQIQRLNTEKKKLNTDLYHMKHSLRYFE- 180
Cdd:COG4717 44 RAMLLERLEKEADELfKPQGRKPELNLKELKELEEELKEAEekeeeyAELQEELEELEEELEELEAELEELREELEKLEk 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 181 --------EESKDLAGRLQRSSQRIGELEWSLCAVAATQKKkpdgfssrskallKRQLEQSIREqillkgHVTQLKESLK 252
Cdd:COG4717 124 llqllplyQELEALEAELAELPERLEELEERLEELRELEEE-------------LEELEAELAE------LQEELEELLE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 325511392 253 EVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLKNQ 310
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
181-350 |
7.25e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 181 EESKDLAGRLQRSSQRIGELEwslcAVAATQkkkPDGFSSRSKALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQ 260
Cdd:COG4913 255 EPIRELAERYAAARERLAELE----YLRAAL---RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 261 YAEQIkgeRAQWQQRMRKMSQEVCTLKEEKKHDTHRVEELERSLSRLknqmaeplppDAPAVSSEVELQDLRKELERVAG 340
Cdd:COG4913 328 LEAQI---RGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL----------GLPLPASAEEFAALRAEAAALLE 394
|
170
....*....|
gi 325511392 341 ELQAQVENNQ 350
Cdd:COG4913 395 ALEEELEALE 404
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
123-475 |
8.77e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.32 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 123 LKQQKKQVEHQLEEEKKANNEKQKAERELEGQIqrlnTEKKKLNTDlyhmkhsLRYFEEESKDLAGRLQRSSQRIGElew 202
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQI----TEKENKMKD-------LTFLLEESRDKANQLEEKTKLQDE--- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 203 slcaVAATQKKKPDGFSSRSKAlLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQE 282
Cdd:pfam05483 283 ----NLKELIEKKDHLTKELED-IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 283 VCTLKEEKKHDTHRVEELERSLS----RLKNQMAEPLPPDAPAVSSEVELQDLR-------------KELERVAGELQAQ 345
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELEELKkilaedeklldekKQFEKIAEELKGK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 346 veNNQCISLLNRGQKERLREQEERLQEQQERLRErekrLQQLAEPQSDLEELK--------HENKSALQ---LEQQVKEL 414
Cdd:pfam05483 438 --EQELIFLLQAREKEIHDLEIQLTAIKTSEEHY----LKEVEDLKTELEKEKlknieltaHCDKLLLEnkeLTQEASDM 511
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325511392 415 QEKLGQVMETLTSAEKEPEAAVPAsgtggessgLMDLLEEKADLREHVEKLELGFIQYRRE 475
Cdd:pfam05483 512 TLELKKHQEDIINCKKQEERMLKQ---------IENLEEKEMNLRDELESVREEFIQKGDE 563
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
129-291 |
9.33e-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: 38.37 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 129 QVEHQLEEEKKANNEKQKAERELEGQIQRLNTEKKKLNTDLYHMKHSLRYFEEESKDLAGRLQRSSQRIGELewslcava 208
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 209 atqkKKPDGFSSRSK--ALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQIKGERAQWQQRMRKMSQEVCTL 286
Cdd:COG1579 86 ----RNNKEYEALQKeiESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
....*
gi 325511392 287 KEEKK 291
Cdd:COG1579 162 EAERE 166
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
223-418 |
9.52e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.23 E-value: 9.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 223 KALLKRQLEQSIREQILLKGHVTQLKESLKEVQLERDQYAEQ-----IKGERAQWQQRMRKMSQEVCTLKEEKkhdthrv 297
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAEL------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325511392 298 EELERSLSRLKNQMAEPlPPDAPAVSSEVELQDLRKELERVAGELQAQV-----ENNQCISLLNRGQKERLREQEERLQE 372
Cdd:COG3206 236 AEAEARLAALRAQLGSG-PDALPELLQSPVIQQLRAQLAELEAELAELSarytpNHPDVIALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 325511392 373 QQERLREREKRLQQLAEPQSDLEELKHENKSALQLEQQVKELQEKL 418
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREV 360
|
|
| |
