|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-596 |
5.86e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.85 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 246 EEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKNLDESMEKESGM 325
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 326 MVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQLSREKVELEERIFSRERKLVELNRKADELTHA 405
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 406 VAVLQKNCDDQTKingklsckvdqlsnalaqvelRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKS 485
Cdd:TIGR02168 826 LESLERRIAATER---------------------RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 486 LFSAKNDLESQSESLKSENVKLEKELVELRKAMEALKTELESAGMDAKRSMVMLKSAASMLSQLENRE-DRLISEEQKRE 564
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTlEEAEALENKIE 964
|
330 340 350
....*....|....*....|....*....|....*.
gi 15229907 565 IGTEPYAMELESIEKAFKNKEDI----IEEMKKEAE 596
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVnlaaIEEYEELKE 1000
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
256-564 |
3.53e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 256 KREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKnldesmekesgmmvEIDALGKE 335
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL--------------ELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 336 RTIKESEVERLIGEKNLIEKQMEMLNVQssdkgklIDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQKNCDD 415
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEER-------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 416 QTKingklscKVDQLSNALAQVELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLES 495
Cdd:COG1196 363 AEE-------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229907 496 QSESLKSENVKLEKELVELRKAMEALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKRE 564
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
28-596 |
5.62e-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: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 28 ETDKKATVLSRQSSMEEHDSSEEQFQNLKSLNAMLLKQAMEKRNQIDSLVQAKDELETELARYCQEKTGLRDELDQVSDE 107
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 108 NFGLKFELDfvivFVESQFREMCVGVDMLVKEKSDRESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHE 187
Cdd:TIGR02168 325 LEELESKLD----ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 188 EVNRLKECVVRLEEKESNLEIVIGKLESENERL-VKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEK 266
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 267 NEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDLV--------------IGLEKNLDESM-----EKESGMMV 327
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdegyeAAIEAALGGRLqavvvENLNAAKK 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 328 EIDALGKERTIKESEVE-RLIGEKNLIEKQMEMLNVQSSDKGKLIDQLS----------------------------REK 378
Cdd:TIGR02168 561 AIAFLKQNELGRVTFLPlDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsyllggvlvvddldnalelAKK 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 379 VELEERIF----------------SRERKLVELNRKA--DELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELR 440
Cdd:TIGR02168 641 LRPGYRIVtldgdlvrpggvitggSAKTNSSILERRReiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 441 REEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSENVKLEKELVELRKAMEA 520
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229907 521 LKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELESIEKAFKNKEDIIEEMKKEAE 596
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-591 |
9.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 18 RQQQHDQKAPETDKKATVLSRQSSMEEHDSSEEQFQNLKSLNAMLLKQAMEKRNQIDSLVQAKDELETELARYCQEKTGL 97
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 98 RDELDQVSDENfglkfeldfvivfvesqfremcvgvDMLVKEKSDRESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDL 177
Cdd:COG1196 315 EERLEELEEEL-------------------------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 178 IKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKR 257
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 258 EIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKNLDESME-KESGMMVEIDALGKER 336
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAaLLLAGLRGLAGAVAVL 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 337 TIKESEVERLIGEKnLIEKQMEMLNVQSSDKGKLIDQLSREKVELEERI-FSRERKLVELNRKADELTHAVAVLQKNCDD 415
Cdd:COG1196 530 IGVEAAYEAALEAA-LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLpLDKIRARAALAAALARGAIGAAVDLVASDL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 416 QtkingKLSCKVDQLSNALAQVELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLES 495
Cdd:COG1196 609 R-----EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 496 QSESLKSENVKLEKELVELRKAMEALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELE 575
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
570
....*....|....*.
gi 15229907 576 SIEKAFKNKEDIIEEM 591
Cdd:COG1196 764 ELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
295-587 |
4.92e-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: 56.23 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 295 RSLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQL 374
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 375 SR-------EKVELEERIFSRERKLVEL-----NRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRRE 442
Cdd:TIGR02169 750 EQeienvksELKELEARIEELEEDLHKLeealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 443 EADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSENVKLEKELVELRKAMEALK 522
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229907 523 TELESAGMDAKRSMVMLKSAASMLSQLEnREDRLISEEQKREIGTEPYAMELESIEKAFKNKEDI 587
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPV 973
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-524 |
5.60e-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: 56.22 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 138 KEKSDRESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESEN 217
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 218 ERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEknemeivkieqkgvIEELERKLDKLNETVRSL 297
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA--------------LDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 298 TKEEKVLRDLVIGLEKnldesmekesgmmvEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQLSRE 377
Cdd:TIGR02168 823 RERLESLERRIAATER--------------RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 378 KVELEERIFSRERKLVELNRKADELTHAVAVLQKncddqtkingklscKVDQLSNALAQVELRREE-ADKALDEEKRNGE 456
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELRE--------------KLAQLELRLEGLEVRIDNlQERLSEEYSLTLE 954
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229907 457 DLKAEVLKSEKMVAKTLEELEKVKIERKSL----FSAKNDLESQSES---LKSENVKLEKELVELRKAMEALKTE 524
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKIKELgpvnLAAIEEYEELKERydfLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-342 |
6.26e-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: 56.22 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 71 NQIDSLVQAKDELETELARYCQEKTGLRDELDQVSDENFGLKFELDFV---IVFVESQFREMCVGVDMLVKEKSDRESEI 147
Cdd:TIGR02168 691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeVEQLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 148 RVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKERKVR 227
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 228 EEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDL 307
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
250 260 270
....*....|....*....|....*....|....*..
gi 15229907 308 VIGLEKNLDESMEK--ESGMMVEIDALGKERTIKESE 342
Cdd:TIGR02168 931 LEGLEVRIDNLQERlsEEYSLTLEEAEALENKIEDDE 967
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
186-515 |
7.08e-08 |
|
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: 55.80 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 186 HEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSE 265
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 266 KNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVER 345
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 346 LIGEKNLIEKQMEMLNVQSSDKGKLIDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQK---------NCDDQ 416
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESkisdledelNKDDF 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 417 TKINGKLSCKVDQLSNALAQVEL-------RREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSA 489
Cdd:TIGR04523 553 ELKKENLEKEIDEKNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
330 340
....*....|....*....|....*.
gi 15229907 490 KNDLESQSESLKSENVKLEKELVELR 515
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEIR 658
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
138-443 |
1.07e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 138 KEKSDRESEIRVLKG--EAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLES 215
Cdd:TIGR02169 207 REKAERYQALLKEKReyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 216 ENERLVKErkvreeEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVR 295
Cdd:TIGR02169 287 EEQLRVKE------KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 296 SLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQLS 375
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229907 376 REKVELEERIFSRERKLVELnrkADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREE 443
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQL---AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
146-410 |
2.10e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 146 EIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKERK 225
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 226 VREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLR 305
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 306 DLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQLSREKVELEERI 385
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260
....*....|....*....|....*
gi 15229907 386 FSRERKLVELNRKADELTHAVAVLQ 410
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
136-600 |
2.27e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 136 LVKEKSDRESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLES 215
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 216 ENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVR 295
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 296 SLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQLS 375
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 376 REKVELEERIFSRERKLVELN------------------RKADELTHAVAVLQKNCDD---------------------- 415
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGlrglagavavligveaayEAALEAALAAALQNIVVEDdevaaaaieylkaakagratfl 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 416 -------QTKINGKLSCKVDQLSNALAQVELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFS 488
Cdd:COG1196 578 pldkiraRAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 489 AKNDLESQSESLKSENVKLEKELVELRKAMEA-----LKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKR 563
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAeeeleLEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
490 500 510
....*....|....*....|....*....|....*..
gi 15229907 564 EIGTEPYAMELESIEKAFKNKEDIIEEMKKEAEIMKQ 600
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
143-593 |
5.07e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 143 RESEIRVLKGEAIELTGKVEiEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVK 222
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 223 ERKVREE---EIEGVKKEKIGLEKIMEeKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGviEELERKLDKLNETVRSLTK 299
Cdd:PRK03918 343 LKKKLKElekRLEELEERHELYEEAKA-KKEELERLKKRLTGLTPEKLEKELEELEKAK--EEIEEEISKITARIGELKK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 300 EEKVLRDLVIGLEK----------NLDESMEKE--SGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDK 367
Cdd:PRK03918 420 EIKELKKAIEELKKakgkcpvcgrELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 368 gKLIDQLSREKVELE----ERIFSRERKLVELNRKADELTHAVAVLQKNCDdqtkingklscKVDQLSNALAQVELRREE 443
Cdd:PRK03918 500 -ELAEQLKELEEKLKkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-----------KLEELKKKLAELEKKLDE 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 444 ADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSENVKLEKELVELRKAMEALKT 523
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 524 ELESAGMD---------AKRSMVMLKSAASMLSQLENREDRLIS-----EEQKREIGT-EPYAMELESIEKAFKNKEDII 588
Cdd:PRK03918 648 ELEELEKKyseeeyeelREEYLELSRELAGLRAELEELEKRREEikktlEKLKEELEErEKAKKELEKLEKALERVEELR 727
|
....*
gi 15229907 589 EEMKK 593
Cdd:PRK03918 728 EKVKK 732
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
149-611 |
5.23e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.13 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 149 VLKGEAIELTGKVEIeKEQLrKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKERKVRE 228
Cdd:TIGR01612 1075 ILEEAEINITNFNEI-KEKL-KHYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQI 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 229 EEIEGVKKEKI------GLEKIMEEKKNEIDGLK---REIKVLLSEKNEMEIVKI---EQKGVIEELERKLDKLneTVRS 296
Cdd:TIGR01612 1153 NDLEDVADKAIsnddpeEIEKKIENIVTKIDKKKniyDEIKKLLNEIAEIEKDKTsleEVKGINLSYGKNLGKL--FLEK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 297 LTKEEKVlrdlviglEKNLDESMEKesgMMVEIDALGKertiKESEVERLIGEKNLIEKQMEMLNVqSSDKGKLIDQLSR 376
Cdd:TIGR01612 1231 IDEEKKK--------SEHMIKAMEA---YIEDLDEIKE----KSPEIENEMGIEMDIKAEMETFNI-SHDDDKDHHIISK 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 377 EKVELEERIFSRERKLVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRR-----EEADKALDEE 451
Cdd:TIGR01612 1295 KHDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKikkiiDEVKEYTKEI 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 452 KRNGEDLKAEVLKSEKMVAKTLEE----------------------LEKVKIERKSLFSAKNDLESQSESLK--SENVKL 507
Cdd:TIGR01612 1375 EENNKNIKDELDKSEKLIKKIKDDinleeckskiestlddkdidecIKKIKELKNHILSEESNIDTYFKNADenNENVLL 1454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 508 EKELVEL--RKAMEALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELESI-----EKA 580
Cdd:TIGR01612 1455 LFKNIEMadNKSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELlnkysALA 1534
|
490 500 510
....*....|....*....|....*....|.
gi 15229907 581 FKNKediIEEMKKEAEIMKQSTEEAHKKQTF 611
Cdd:TIGR01612 1535 IKNK---FAKTKKDSEIIIKEIKDAHKKFIL 1562
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
210-412 |
2.54e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 210 IGKLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLlseknEMEIVKIEQKgvIEELERKLDK 289
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-----EQELAALEAE--LAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 290 LNetvRSLTKEEKVLRDLVIGLEKNLD----------ESMEKESGMMVEIDALGKERtikESEVERLIGEKNLIEKQMEM 359
Cdd:COG4942 95 LR---AELEAQKEELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPAR---REQAEELRADLAELAALRAE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15229907 360 LNVQSSDKGKLIDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQKN 412
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
371-600 |
3.47e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 371 IDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREEADKALDE 450
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 451 EKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSENVKLEKELVELRKAMEALKTELESAGM 530
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 531 DAKRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEpyAMELESIEKAFKNKEDIIEEMKKEAEIMKQ 600
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL--EEELEELQEELERLEEALEELREELEEAEQ 475
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
281-579 |
3.84e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 281 EELERKLDKLNETVRSLTKEEKVLRDLVIGLEKNLDESMEKEsgmmvEIDALGKERtiKESEVERLIGEKNLIEKQMEML 360
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-----RYQALLKEK--REYEGYELLKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 361 NVQSSDKGKLIDQLSREKVELEERIFSRERKLVELNRKADELT-----------HAVAVLQKNCDDQTKIN--------- 420
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeqlrvkekiGELEAEIASLERSIAEKereledaee 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 421 ---------GKLSCKVDQLSNALAQVELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKN 491
Cdd:TIGR02169 323 rlakleaeiDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 492 DLESQSESLKSENVKLEKELVELRKAME-------ALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKRE 564
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAgieakinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
330
....*....|....*
gi 15229907 565 IGTEPYAMELESIEK 579
Cdd:TIGR02169 483 KELSKLQRELAEAEA 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
164-604 |
5.12e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 164 EKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKERKVREE---EIEGVKKEKIG 240
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEElekELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 241 LEKIMEEKKNEIDGLKREIKVLlsEKNEMEIVKIEQKG-VIEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKNLDESM 319
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEEL--EEKVKELKELKEKAeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 320 EKESgmmvEIDALGKERTIKESEVERLIGEKNLIE----KQMEMLNVQSSDKGKLIDQLSREKVELEERIFSRERKLVEL 395
Cdd:PRK03918 335 EKEE----RLEELKKKLKELEKRLEELEERHELYEeakaKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 396 NRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSnalaqvELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEE 475
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGKCPVCGRELT------EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 476 LEKVKIERKSLFSAK---NDLESQSESLKSENV-----------KLEKELVELRKAMEALKTELESAGMDAKRSMVMLKS 541
Cdd:PRK03918 485 LEKVLKKESELIKLKelaEQLKELEEKLKKYNLeelekkaeeyeKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 542 AASMLSQLENREDRLIS------EEQKREIGT-EPYAMELESIEKAFKNKEDIIEEMKKEAEIMKQSTEE 604
Cdd:PRK03918 565 LDELEEELAELLKELEElgfesvEELEERLKElEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
64-607 |
9.21e-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: 48.86 E-value: 9.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 64 KQAMEKRNQIDSLVQAKDELETELARYCQEKTGLRDELDQVSDENFGLKFELdFVIVFVESQFREMCVGVDMLVKEKSDR 143
Cdd:TIGR04523 152 KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLL-SNLKKKIQKNKSLESQISELKKQNNQL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 144 ESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESE-NERLVK 222
Cdd:TIGR04523 231 KDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 223 ERKvreEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEK 302
Cdd:TIGR04523 311 ELK---SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 303 VLRDLVIGLEKNLDESMEKESgmmveidalgkertIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQLSREKVELE 382
Cdd:TIGR04523 388 NLESQINDLESKIQNQEKLNQ--------------QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 383 ERIFSRERKLVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREEADKALDEEKRNGEDLKAEV 462
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 463 LKSEKMVAKTLEELEKVKIERKSlfsakndlesqsESLKSENVKLEKELVELRKAMEALKTELESAGMDAKrsmvmlksa 542
Cdd:TIGR04523 534 KEKESKISDLEDELNKDDFELKK------------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID--------- 592
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229907 543 asmlsQLENREDRLISEEQKREIGTEPYAMELESIEKAFKNKEDIIEEMKKEAEIMKQSTEEAHK 607
Cdd:TIGR04523 593 -----QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
228-451 |
9.87e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 228 EEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEmeivkIEQKgvIEELERKLDKLNETVRSLTKEEKVLRDL 307
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-----LQAE--LEALQAEIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 308 VigleKNLDESMEKESGMMVEIDALgkertIKESEVERLIGeknliekQMEMLNVQSSDKGKLIDQLSREKVELEERIFS 387
Cdd:COG3883 88 L----GERARALYRSGGSVSYLDVL-----LGSESFSDFLD-------RLSALSKIADADADLLEELKADKAELEAKKAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229907 388 RERKLVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREEADKALDEE 451
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
349-611 |
1.68e-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: 47.81 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 349 EKNLIEKQMEMLNVQSSDKGKLIDQLSREKVELE-ERIFSRERKLVELNRKADelthavavlqkncddqtkingklscKV 427
Cdd:pfam17380 340 ERMAMERERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNE-------------------------RV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 428 DQLSNALAQVELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEE-----LEKVKIERKSLFSAKNDLESQSESLKS 502
Cdd:pfam17380 395 RQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEerareMERVRLEEQERQQQVERLRQQEEERKR 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 503 ENVKLEKELVELRKAMEALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELEsIEKAFK 582
Cdd:pfam17380 475 KKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE-MEERRR 553
|
250 260 270
....*....|....*....|....*....|....*...
gi 15229907 583 NKEDI---------IEEMKKEAEIMKQSTEEAHKKQTF 611
Cdd:pfam17380 554 IQEQMrkateersrLEAMEREREMMRQIVESEKARAEY 591
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
200-503 |
2.88e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.20 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 200 EEKESN--LEIVIGKLESENERLVKERKVREEEIEGvkkekigLEKIMEEKkneiDGLKREIKVL---LSEKNEMEIVKI 274
Cdd:PLN02939 122 GEQLSDfqLEDLVGMIQNAEKNILLLNQARLQALED-------LEKILTEK----EALQGKINILemrLSETDARIKLAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 275 EQKGVIEELERKLDKLNETVR-----------------SLTKEEKV-LRDLVIGLEKNLDESMEKESGMMVeidaLGKER 336
Cdd:PLN02939 191 QEKIHVEILEEQLEKLRNELLirgateglcvhslskelDVLKEENMlLKDDIQFLKAELIEVAETEERVFK----LEKER 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 337 TIKESEVERLigEKNLIEKQMEMLNVqssdkGKLIDQLSREKVELEERIfsrerklveLNRKADELTHAVAVLQKNCDdq 416
Cdd:PLN02939 267 SLLDASLREL--ESKFIVAQEDVSKL-----SPLQYDCWWEKVENLQDL---------LDRATNQVEKAALVLDQNQD-- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 417 tkingkLSCKVDQLSNALAQ----------VELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIErksl 486
Cdd:PLN02939 329 ------LRDKVDKLEASLKEanvskfssykVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEE---- 398
|
330
....*....|....*..
gi 15229907 487 fSAKNDLESQSESLKSE 503
Cdd:PLN02939 399 -SKKRSLEHPADDMPSE 414
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
246-475 |
3.39e-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: 46.68 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 246 EEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKnldesmekesgm 325
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK------------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 326 mvEIDALGKERTIKESEVERLIGE---KNLIEKQMEMLNVQSSDK----GKLIDQLSREKVELEERIfsrERKLVELNRK 398
Cdd:COG4942 91 --EIAELRAELEAQKEELAELLRAlyrLGRQPPLALLLSPEDFLDavrrLQYLKYLAPARREQAEEL---RADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229907 399 ADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEE 475
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
147-303 |
3.46e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 147 IRVLKGEAIEltgkVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKERKV 226
Cdd:COG2433 370 ARVIRGLSIE----EALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIER 445
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229907 227 REEEIEGVKKEkiglEKIMEEKKNEIDGLKREIKVLLSEKNEMEivkieqkGVIEELERKLDKLNETVRSLTKEEKV 303
Cdd:COG2433 446 LERELSEARSE----ERREIRKDREISRLDREIERLERELEEER-------ERIEELKRKLERLKELWKLEHSGELV 511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
134-600 |
4.32e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 134 DMLVKEKSDRESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKN---GFDLQHEEVNRLKECVVRLEEKESNLEIVI 210
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEkaeAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 211 GKLEsENERLVKERKVREEEiegvKKEKIGLEKIMEEKKnEIDGLKReiKVLLSEKNEMEIVKIEQKGVIEELERKLDKL 290
Cdd:PTZ00121 1398 KKAE-EDKKKADELKKAAAA----KKKADEAKKKAEEKK-KADEAKK--KAEEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 291 NETVRSLTKEEKVLRdlVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKL 370
Cdd:PTZ00121 1470 KKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 371 IDQLSREkvelEERIFSRERKLVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREEADKALDE 450
Cdd:PTZ00121 1548 ADELKKA----EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAE 1623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 451 EKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSENVKLEKELVELRKAMEALKTELESA-- 528
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAkk 1703
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229907 529 GMDAKRSMVMLKSAASMLSQlENREDRLISEEQKREIGTEPYAMELESIEKAFKNK--EDIIEEMKKEAEIMKQ 600
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKK-AEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKiaHLKKEEEKKAEEIRKE 1776
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
243-527 |
4.46e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 243 KIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGV------IEELERKLDKLNE---TVRSLTKEEKVLRDLVIGLEK 313
Cdd:PRK05771 2 APVRMKKVLIVTLKSYKDEVLEALHELGVVHIEDLKEelsnerLRKLRSLLTKLSEaldKLRSYLPKLNPLREEKKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 314 NLDESMEKESGMMV-----EIDALGKERTIKESEVERLIGEKNLIEKqMEMLNVQSSD--KGKLIDQ----LSREKVELE 382
Cdd:PRK05771 82 KSLEELIKDVEEELekiekEIKELEEEISELENEIKELEQEIERLEP-WGNFDLDLSLllGFKYVSVfvgtVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 383 ERIFSrERKLVELNRKADELTHAVAVLQKNCDDQTKIngklsckvdqlsnaLAQVELRREEadkaLDEEKRNGEDLKaev 462
Cdd:PRK05771 161 KLESD-VENVEYISTDKGYVYVVVVVLKELSDEVEEE--------------LKKLGFERLE----LEEEGTPSELIR--- 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229907 463 lksekmvaKTLEELEKVKIERKSLfsaKNDLESQSESLKSENVKLEKELVELRKAMEALKTELES 527
Cdd:PRK05771 219 --------EIKEELEEIEKERESL---LEELKELAKKYLEELLALYEYLEIELERAEALSKFLKT 272
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
160-402 |
5.43e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.46 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 160 KVEIEKEQLRKVcderdlikngfdlqHEEVNRLKECVVRLEEkesnleiVIGKLESENERLVKERKVREEEI-EGVKKEK 238
Cdd:PRK05771 37 KEELSNERLRKL--------------RSLLTKLSEALDKLRS-------YLPKLNPLREEKKKVSVKSLEELiKDVEEEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 239 IGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVkieqKGVIEELERKLDKLNETVRS-LTKEEKVLRDLVIGLEKNLDE 317
Cdd:PRK05771 96 EKIEKEIKELEEEISELENEIKELEQEIERLEPW----GNFDLDLSLLLGFKYVSVFVgTVPEDKLEELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 318 SMEKESGMMVEIDALGKertiKESEVERLIgeknlieKQMEMLNVQSSDKGK---LIDQLSREKVELEERIFSRERKLVE 394
Cdd:PRK05771 172 ISTDKGYVYVVVVVLKE----LSDEVEEEL-------KKLGFERLELEEEGTpseLIREIKEELEEIEKERESLLEELKE 240
|
....*...
gi 15229907 395 LNRKADEL 402
Cdd:PRK05771 241 LAKKYLEE 248
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
33-430 |
5.92e-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: 46.26 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 33 ATVLSRQSSMEEHDSSEEQFQNLKSLNAMLLKQAMEKRNQIDS-------LVQAKDELETELARYCQEKTGLRDELDQVS 105
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESsertvsdLTASLQEKERAIEATNAEITKLRSRVDLKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 106 DENFGLKFEldfvivfvESQFREMCVGVDMLVKEKSDRESEIRVLKGEAIELT----------GKVEIEKEQLRKVCDER 175
Cdd:pfam15921 531 QELQHLKNE--------GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTqlvgqhgrtaGAMQVEKAQLEKEINDR 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 176 DLikngfdlqheEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGL 255
Cdd:pfam15921 603 RL----------ELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 256 KREIKVL----LSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDA 331
Cdd:pfam15921 673 SEDYEVLkrnfRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF 752
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 332 LGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQLSREKVELEERIFSRErklVELNRKADELTHAVAVLQK 411
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME---VALDKASLQFAECQDIIQR 829
|
410
....*....|....*....
gi 15229907 412 NCDDQTKINGKLSCKVDQL 430
Cdd:pfam15921 830 QEQESVRLKLQHTLDVKEL 848
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
153-609 |
6.12e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 153 EAIELTGKVEIEK-EQLRKVCDER--DLIKNGFDLQHEEVNRLKECVVRLEEKESNLEiviGKLESENERLVKERKVREE 229
Cdd:PTZ00121 1183 KAEEVRKAEELRKaEDARKAEAARkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 230 EIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDLVI 309
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 310 GLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEmlNVQSSDKGKLIDQLSREKVELEERIFSRE 389
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE--EKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 390 RKLVELNRKADELTHAvavlqkncdDQTKINGKLSCKVDQLSNalaqvelRREEADKALDEEKRNGEDLKAEVLKSEKMV 469
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKA---------DEAKKKAEEAKKADEAKK-------KAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 470 AKTLEELEKVKIE-RKSLFSAKNDLESQSESLKSENVKLEKELVELRKAMEALKTElESAGMDAKRSMVMLKSAASMLSQ 548
Cdd:PTZ00121 1482 AKKADEAKKKAEEaKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD-EAKKAEEKKKADELKKAEELKKA 1560
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229907 549 LENREDRLISEEQKREIGTEPYAMELESIEKAfknkeDIIEEMKKEAEIMKQSTEEAHKKQ 609
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAE 1616
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
118-600 |
7.53e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 118 VIVFVESQFREMCVGVDMLVKEKSDRESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVV 197
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 198 RLEEKESNLEIVIGKLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQK 277
Cdd:TIGR04523 107 KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 278 GVIEELERKLDKLNETVRSLTKEEKVLRDlvigLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQM 357
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLSNLKKKIQKNKS----LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 358 EMLNVQSSDKGKLIDQLSREKVELEERIFSRERKLVELNRKADElthavaVLQKNCDDQTKINGKlscKVDQLSNALAQV 437
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ------DWNKELKSELKNQEK---KLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 438 ELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSENVKLEKELVELRKA 517
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 518 MEALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELESIEKAFKNKEDIIEEMKKEAEI 597
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
...
gi 15229907 598 MKQ 600
Cdd:TIGR04523 494 KEK 496
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
369-564 |
1.36e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 369 KLIDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREEADKAL 448
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 449 DEEK-----------RNGEDLKAEVLKS--------------EKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSE 503
Cdd:COG4942 100 EAQKeelaellralyRLGRQPPLALLLSpedfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229907 504 NVKLEKELVELRKAMEALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKRE 564
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
444-609 |
1.73e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 444 ADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSENVKLEKELVELRKAMEALKT 523
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 524 ELESAGMDAKRSMVMLKSA--------ASMLSQLENREDRLIsEEQKREIGtepyamELESIEKAFKNKEDIIEEMKKEA 595
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSEsfsdfldrLSALSKIADADADLL-EELKADKA------ELEAKKAELEAKLAELEALKAEL 166
|
170
....*....|....
gi 15229907 596 EIMKQSTEEAHKKQ 609
Cdd:COG3883 167 EAAKAELEAQQAEQ 180
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-605 |
2.62e-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: 44.28 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 136 LVKEKSDRESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLES 215
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 216 ENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVR 295
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 296 SLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKErtIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQLS 375
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK--LEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 376 REKVELEERIFSRERKLVELNRKADEL----------THAVAVLQKNCDDQTKINGKLS--CKVDQ---------LSNAL 434
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLerlqenlegfSEGVKALLKNQSGLSGILGVLSelISVDEgyeaaieaaLGGRL 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 435 AQVELRREEADK---ALDEEKRNG---------------EDLKAEVLKSEKMVAKTLEELEKVKIERKSLFS-------- 488
Cdd:TIGR02168 548 QAVVVENLNAAKkaiAFLKQNELGrvtflpldsikgteiQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlv 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 489 ----------AKN----------------------------------------DLESQSESLKSENVKLEKELVELRKAM 518
Cdd:TIGR02168 628 vddldnalelAKKlrpgyrivtldgdlvrpggvitggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 519 EALKTELESAGMDAKRSMVMLKSAASMLSQLENR----EDRLISEEQKREIGTEPYAMELESIEKAFKNKEDIIEEMKKE 594
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEveqlEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
570
....*....|.
gi 15229907 595 AEIMKQSTEEA 605
Cdd:TIGR02168 788 EAQIEQLKEEL 798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
123-510 |
2.69e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 123 ESQFREMCVGVDMLVKEKSDRESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKECVVR---- 198
Cdd:PRK03918 316 LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKelee 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 199 LEEKESNLEIVIGKLESENERLVKERKVREEEIEGVKKEK-----IGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVK 273
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 274 IEQKGVIEELERKLDKlNETVRSLTKEEKVLRDLVIGLEKNLDESMEKES----GMMVEIDALGKERTIKESEVERLIGE 349
Cdd:PRK03918 476 RKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEELEKKAeeyeKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 350 KNLIEKQMEMLNVQSSDKGKLIDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQ 429
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 430 LSNALAQVELRREEAD-------------------------KALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERK 484
Cdd:PRK03918 635 LAETEKRLEELRKELEelekkyseeeyeelreeylelsrelAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
410 420
....*....|....*....|....*.
gi 15229907 485 SLFSAKNDLESQSESLKSENVKLEKE 510
Cdd:PRK03918 715 KLEKALERVEELREKVKKYKALLKER 740
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
138-603 |
3.80e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 138 KEKSDRESEIRVLKGEAIELTGKVEIEKEQLRKVCDERDLIKNGFDLQH--EEVNRLKECVVRLEEKESNLEIvigKLES 215
Cdd:PTZ00121 1377 KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKkaEEKKKADEAKKKAEEAKKADEA---KKKA 1453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 216 ENERLVKERKVREEEiegvKKEKIGLEKIMEEKKnEIDGLKREIKVLLSEKNEMEiVKIEQKGVIEELERKLDKLNETVR 295
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEE----AKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAK-KAAEAKKKADEAKKAEEAKKADEA 1527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 296 SLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEmlNVQSSDKGKLIDQLS 375
Cdd:PTZ00121 1528 KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE--EARIEEVMKLYEEEK 1605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 376 REKVElEERIFSRERKLVELNRKADELTHAVAVLQKNCDDQTKingklscKVDQLSNALAQVELRREE-ADKALDEEKRN 454
Cdd:PTZ00121 1606 KMKAE-EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK-------KAEELKKAEEENKIKAAEeAKKAEEDKKKA 1677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 455 GEDLKAEVLKSEKMVAKTLEELEKVKIERksLFSAKNDLESQSESLKSENVKLEKELVELRKAMEALKTELESAGMD--A 532
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEE--LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeE 1755
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229907 533 KRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELESIEKAFKNKEDIIEEMKKEAEIMKQSTE 603
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKE 1826
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
301-549 |
3.82e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.38 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 301 EKVLRDLVIGLEKNLDESMEK--ESGMMVEIDALGKERTIKESEVERLIGE--------------KNLIEKQMEMLNVQS 364
Cdd:PRK05771 4 VRMKKVLIVTLKSYKDEVLEAlhELGVVHIEDLKEELSNERLRKLRSLLTKlsealdklrsylpkLNPLREEKKKVSVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 365 SDKgkLIDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQK----NCDDQTKINGK-LSCKVDQLSNALAQVEL 439
Cdd:PRK05771 84 LEE--LIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwgnfDLDLSLLLGFKyVSVFVGTVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 440 RREEADKALDEEKRNGEDLKAeVLKSEKMVAKTLEELEKVKIERKSLfSAKNDLESQSESLKSENVKLEKELVELRKAME 519
Cdd:PRK05771 162 LESDVENVEYISTDKGYVYVV-VVVLKELSDEVEEELKKLGFERLEL-EEEGTPSELIREIKEELEEIEKERESLLEELK 239
|
250 260 270
....*....|....*....|....*....|
gi 15229907 520 ALKTELESAGMDAKRSMVMLKSAASMLSQL 549
Cdd:PRK05771 240 ELAKKYLEELLALYEYLEIELERAEALSKF 269
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
212-597 |
4.46e-04 |
|
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: 43.42 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 212 KLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLN 291
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 292 ETVRSLTKEEKVLRDLVIGLEKNLDESMEKESGmmVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLI 371
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK--LLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 372 DQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREEADKALDEE 451
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 452 KRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSENVKLEKELVELRKAMEALKTELESAGMD 531
Cdd:pfam02463 415 RQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQK 494
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229907 532 AKRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELESIEKAFKNKEDIIEEMKKEAEI 597
Cdd:pfam02463 495 LEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
204-592 |
4.95e-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: 43.57 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 204 SNLEIVIGKLESEnerLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKRE-------IKVLLSE----KNEMEIV 272
Cdd:pfam15921 320 SDLESTVSQLRSE---LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnlddqLQKLLADlhkrEKELSLE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 273 KIEQKGV----------IEELERKLDKLNETVRSLTKEEKVLRDLVIG-LEKNL------DESMEKESGMMVEIDALGK- 334
Cdd:pfam15921 397 KEQNKRLwdrdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGqMERQMaaiqgkNESLEKVSSLTAQLESTKEm 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 335 -ERTIKESEVERLIGEKNliEKQMEMLNVQSSDKGKLIDQLSREKVELEERIFSRERKLVELNRKADELTHAvavlQKNC 413
Cdd:pfam15921 477 lRKVVEELTAKKMTLESS--ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNV----QTEC 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 414 DdqtkingKLSCKVDQLSNALAQVELRREEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDL 493
Cdd:pfam15921 551 E-------ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 494 ESQSESLKSENVKLEKELVELRKAMEALKTELESAGMDAKRSMVMLKSAASMLSQLEnREDRLISEEQkrEIGTEPYAME 573
Cdd:pfam15921 624 EARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK-RNFRNKSEEM--ETTTNKLKMQ 700
|
410
....*....|....*....
gi 15229907 574 LESIEKAFKNKEDIIEEMK 592
Cdd:pfam15921 701 LKSAQSELEQTRNTLKSME 719
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
363-605 |
6.53e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 363 QSSDKGKLIDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQKNCDDQTKingklsckvdQLSNALAQVELRRE 442
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 443 EADKALDEEKRNGEDLKA-EVLKSEKMVAKTLEELEKVkierKSLFSAKNDLESQSESLKSENVKLEKELVELRKAMEAL 521
Cdd:COG3883 87 ELGERARALYRSGGSVSYlDVLLGSESFSDFLDRLSAL----SKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 522 KTELESAgmdakrsmvmLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELESIEKAFKNKEDIIEEMKKEAEIMKQS 601
Cdd:COG3883 163 KAELEAA----------KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
....
gi 15229907 602 TEEA 605
Cdd:COG3883 233 AAAA 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
212-358 |
9.47e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 212 KLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKvllseKNEMEIVKIEQKgvIEELERKLDKL- 290
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIK-----RLELEIEEVEAR--IKKYEEQLGNVr 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229907 291 -NETVRSLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQME 358
Cdd:COG1579 87 nNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
64-324 |
1.03e-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: 41.67 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 64 KQAMEKRNQIDSLVQAKDELETELARYCQEKTGLRDELDQVSDEnfglkfeldfvIVFVESQFREmcvgvdmLVKEKSDR 143
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-----------IAALARRIRA-------LEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 144 ESEIRVLKGEAIELTGKVEIEKEQLRKVcdERDLIKNGfdlqheEVNRLKecvVRLEEKESNLEIVIGKLeseNERLVKE 223
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAEL--LRALYRLG------RQPPLA---LLLSPEDFLDAVRRLQY---LKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 224 RKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKvllSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKV 303
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELE---EERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|.
gi 15229907 304 LRDLVIGLEKNLDESMEKESG 324
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
174-384 |
1.13e-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: 41.67 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 174 ERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEID 253
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 254 ---------GLKREIKVLLSEKNEMEIVKIEQ--KGVIEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKNLDESMEke 322
Cdd:COG4942 108 ellralyrlGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE-- 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229907 323 sgmmvEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGKLIDQLSREKVELEER 384
Cdd:COG4942 186 -----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
190-604 |
1.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 190 NRLKECVVRLEEKESNLEIVIgKLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEM 269
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFI-KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 270 EIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKnLDESMEKESGMMVEIDALGKERTIKESEVERLIGE 349
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 350 KNLIEKQMEMLNVQSSDKGKL---IDQLSREKVELEERIFSRERKLVELNR----KADELTHAVAVLQKNCDDQTKINGK 422
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELkkkLKELEKRLEELEERHELYEEAKAKKEElerlKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 423 LSCKVDQLSNALAQVELRREEADKALDEEKrnGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKS 502
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELK--KAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 503 ENVKLEKELVELRKAMEALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKREI------GTEPYAMELES 576
Cdd:PRK03918 481 ELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSlkkeleKLEELKKKLAE 560
|
410 420
....*....|....*....|....*...
gi 15229907 577 IEKAFKNKEDIIEEMKKEAEIMKQSTEE 604
Cdd:PRK03918 561 LEKKLDELEEELAELLKELEELGFESVE 588
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
299-603 |
1.62e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 299 KEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIgeKNLIEKQMEMLNVQSSDKGKLIDQLSREK 378
Cdd:PLN02939 53 NIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRAS--MQRDEAIAAIDNEQQTNSKDGEQLSDFQL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 379 VELEERIFSRERKLVELNR-KADELTHAVAVLQKNCDDQTKIN---GKLScKVDQLSNALAQVELRREEADKALdEEKRN 454
Cdd:PLN02939 131 EDLVGMIQNAEKNILLLNQaRLQALEDLEKILTEKEALQGKINileMRLS-ETDARIKLAAQEKIHVEILEEQL-EKLRN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 455 geDLKAEVLKSEKMVAKTLEELEKVKIERKSLfsaKNDLESQSESL----KSEN--VKLEKElvelRKAMEALKTELESA 528
Cdd:PLN02939 209 --ELLIRGATEGLCVHSLSKELDVLKEENMLL---KDDIQFLKAELievaETEErvFKLEKE----RSLLDASLRELESK 279
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229907 529 GMDAKRSMVMLKSAA--SMLSQLENREDRLISEEQKreigTEPYAMELESiEKAFKNKEDIIEEMKKEAEIMKQSTE 603
Cdd:PLN02939 280 FIVAQEDVSKLSPLQydCWWEKVENLQDLLDRATNQ----VEKAALVLDQ-NQDLRDKVDKLEASLKEANVSKFSSY 351
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
280-609 |
1.87e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 280 IEELERKLDKLNETVRSLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEM 359
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 360 LNVQSSDKGKLIDQLSREKVELEERIfsrerklVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVEL 439
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERA-------EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 440 RREEADKALDEEKRNGEDLKAEvlksEKMVAKTLEELEKVKIERKSLFSAKNDLESQSESLKSENVKLEKELVELRKAME 519
Cdd:PRK02224 406 DLGNAEDFLEELREERDELRER----EAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 520 ALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELESIEKAFKNKEDIIEEMKKEAEIMK 599
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA 561
|
330
....*....|
gi 15229907 600 QSTEEAHKKQ 609
Cdd:PRK02224 562 EAEEEAEEAR 571
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
285-527 |
2.88e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 285 RKLDKLNETVRSLTKEEKVLRDLVIGLEKNLDESMEKESGMMVE---IDALGKERTIKEsEVERLIGEKNLIEKQMEMLN 361
Cdd:COG4913 204 KPIGDLDDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAreqIELLEPIRELAE-RYAAARERLAELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 362 VQssDKGKLIDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQKNCDDQtkiNGKlscKVDQLSNALAQVELRR 441
Cdd:COG4913 283 LW--FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN---GGD---RLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 442 EEADKALDEEKRNGEDLKAEVLKSEKMVAKTLEELEkvkierkslfSAKNDLESQSESLKSENVKLEKELVELRKAMEAL 521
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAA----------ALLEALEEELEALEEALAEAEAALRDLRRELREL 424
|
....*.
gi 15229907 522 KTELES 527
Cdd:COG4913 425 EAEIAS 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
126-358 |
3.66e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 126 FREMcvgvdMLvkEKSDRESEIRVLKGEAIELTG---KVEIEKEQ------LRKVCDERDLIKNGFDLQHEEVNRLKecV 196
Cdd:COG4913 213 VREY-----ML--EEPDTFEAADALVEHFDDLERaheALEDAREQiellepIRELAERYAAARERLAELEYLRAALR--L 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 197 VRLEEKESNLEIVIGKLESENERLVKERKVREEEIEGVKKEKIGLEK-IMEEKKNEIDGLKREIKVLLSEKNEmeivkie 275
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqIRGNGGDRLEQLEREIERLERELEE------- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 276 QKGVIEELERKLDKLNETV----RSLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKN 351
Cdd:COG4913 357 RERRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
....*..
gi 15229907 352 LIEKQME 358
Cdd:COG4913 437 NIPARLL 443
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
145-356 |
3.67e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 145 SEIRVLKGEAIELTGKVEIEKEQLRKvcdERDLIKNGFDLQHEEVNRLKECVVRLEEKESNLEIVIGKLESENERLVKER 224
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKT---YNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 225 KVREEEIegvKKEKIGLEKImeekKNEIDGLKREIKVL------------LSEKNEMeIVKIEQKGV-----IEELERKL 287
Cdd:PHA02562 251 EDPSAAL---NKLNTAAAKI----KSKIEQFQKVIKMYekggvcptctqqISEGPDR-ITKIKDKLKelqhsLEKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229907 288 DKLNETVRSLTKEEKVLRDLVIGLEKN---LDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQ 356
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELKNKISTNkqsLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKT 394
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
386-533 |
4.26e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 386 FSRERKLVELNRKADELTHAVAVLQKncdDQTKINGKLSCKVDQLSNALAQVELRREEAD-KALDEEKRNGEDLKAEVLK 464
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEE---RLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDA 682
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229907 465 SEKMVAKTLEELEKVKIERKslfsaknDLESQSESLKSENVKLEKELVELRKAMEALKTELESAGMDAK 533
Cdd:COG4913 683 SSDDLAALEEQLEELEAELE-------ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
378-536 |
6.61e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.63 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 378 KVELEERIFSRERKLVELNRKADELTHAVAVLQKNCDdqtkingKLSCKVDQLSNALAQVELRREEADKALDEEKR---- 453
Cdd:pfam05667 323 VETEEELQQQREEELEELQEQLEDLESSIQELEKEIK-------KLESSIKQVEEELEELKEQNEELEKQYKVKKKtldl 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 454 ------NGEDLKAEVLKSEKMVAKTLEELEKVKI----ERKSLFSAKNDLESQSESLKSENVKLEKEL----VELRKAME 519
Cdd:pfam05667 396 lpdaeeNIAKLQALVDASAQRLVELAGQWEKHRVplieEYRALKEAKSNKEDESQRKLEEIKELREKIkevaEEAKQKEE 475
|
170 180
....*....|....*....|
gi 15229907 520 A---LKTELESAGMDAKRSM 536
Cdd:pfam05667 476 LykqLVAEYERLPKDVSRSA 495
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
228-412 |
6.99e-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: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 228 EEEIEGVKKEKIGLEKIME------EKKNEIDGLKREIKVLLSEKNEMEIVKIEQKgvIEELERKLDKLNETVRSLTKEE 301
Cdd:COG4913 241 HEALEDAREQIELLEPIRElaeryaAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 302 KVLRDLVIGLEKNLDESmekeSGmmVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKGK-----------L 370
Cdd:COG4913 319 DALREELDELEAQIRGN----GG--DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaalraeaaaL 392
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 15229907 371 IDQLSREKVELEERIFSRERKLVELNRKADELTHAVAVLQKN 412
Cdd:COG4913 393 LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-462 |
7.08e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 3 KKKASRNSNDTANDNRQQQHDQKAPETDKKATVLSRQSsmEEHDSSEEQFQNLKSLNAMLLKQAMEKRN-----QIDSLV 77
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAA--EAKKKADEAKKAEEAKKADEAKKAEEAKKadeakKAEEKK 1546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 78 QAKDELETELARYCQEKTGLRDELDQVSDENFGLKfeldfvivfvesQFREMCVGVDMLVKEKSDRESEIRVLKGEAIEL 157
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR------------KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 158 TGKVEIEKEQLRKVCDERDLIKNGFDLQHEEVNRLKEcvVRLEEKESNLEIVIGKLESENERLVKERKVREEEIEGVKKE 237
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE--LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 238 KIGLEkimEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLDKLNETVRSLTKEEKVLRDlvigLEKNLDE 317
Cdd:PTZ00121 1693 ALKKE---AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK----IAHLKKE 1765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 318 SMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQS-SDKGKLIDQLSREKVELEERIFSRERKLVELN 396
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEgGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229907 397 RKAdelthavavLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREEADKALDEEKRNGEDLKAEV 462
Cdd:PTZ00121 1846 ADA---------FEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
209-604 |
8.01e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.23 E-value: 8.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 209 VIGKLESENERLVKERKVREEEIEGVKKEKIGLEKIMEEKKNEIDGLKREIKVLLSEKNEMEIVKIEQKGVIEELERKLD 288
Cdd:TIGR04523 27 IANKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 289 KLNETVRSLTKEEKVLRDLVIGLEKNLDESMEKESGMMVEIDALGKERTIKESEVERLIGEKNLIEKQMEMLNVQSSDKG 368
Cdd:TIGR04523 107 KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 369 KLIDQLSREKVELEERIFsrerKLVELNRKADELTHAVAVLQKNCDDQTKINGKLSCKVDQLSNALAQVELRREEADKAL 448
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLS----NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 449 DEEKRNGEDLKAEVLKSEKMVAKTLEELEKVKIERKSLFSAKN------------DLESQSESLKSENVKLEKELVELRK 516
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkelkselkNQEKKLEEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229907 517 AMEALKTELESAGMDAKRSMVMLKSAASMLSQLENREDRLISEEQKREIGTEPYAMELESIEKAFKNKEDIIEEMKKEAE 596
Cdd:TIGR04523 343 QISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE 422
|
....*...
gi 15229907 597 IMKQSTEE 604
Cdd:TIGR04523 423 LLEKEIER 430
|
|
| |
