|
Name |
Accession |
Description |
Interval |
E-value |
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
12-257 |
1.51e-30 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 124.90 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 12 CEESGAEPQEAVLQQLHQLPK-GGLDLTTQSLTVETCRALGKLLHKETLLKELVLSDCMLSEEGSTLLFQGLCANTSVQH 90
Cdd:COG5238 189 CNQIGDEGIEELAEALTQNTTvTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVET 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 91 LDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGtwEDAFATFCGGLAANSALRQLDLRNNQISHKGAEELALALKG 170
Cdd:COG5238 269 LYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG--DEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 171 NTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLDLAGNNIPGDILRAVEQAMDHNQDRLTAFRENQARTKILSKEVQH 250
Cdd:COG5238 347 NTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLILDGNLIGAEAQQRLEQL 426
|
....*..
gi 266456389 251 LQEEKSK 257
Cdd:COG5238 427 LERIKSV 433
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
35-229 |
2.60e-24 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 104.36 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 35 LDLTTQSLTVETCRALGKLLHKETLlKELVLSDCMLSEEGSTLLFQGLCANT-SVQHLDLKGNNLRATGAEALGKLLRQN 113
Cdd:cd00116 86 LDLSDNALGPDGCGVLESLLRSSSL-QELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRLEGASCEALAKALRAN 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 114 KSIQSLTLEWNNLGtwEDAFATFCGGLAANSALRQLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNIGLLGGRALV 193
Cdd:cd00116 165 RDLKELNLANNGIG--DAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALA 242
|
170 180 190
....*....|....*....|....*....|....*..
gi 266456389 194 NCLPS-NRTLWKLDLAGNNIPGDILRAVEQAMDHNQD 229
Cdd:cd00116 243 SALLSpNISLLTLSLSCNDITDDGAKDLAEVLAEKES 279
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
28-185 |
1.09e-17 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 84.71 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 28 HQLPKGGLDLTTQSLTVETCRALGKLLHKETLLKELVLSDCMLSEEGSTLLFQGLCANTSVQHLDLKGNNLRATGAEALG 107
Cdd:cd00116 135 LPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALA 214
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 266456389 108 KLLRQNKSIQSLTLEWNNLGTWedAFATFCGGL-AANSALRQLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNIG 185
Cdd:cd00116 215 ETLASLKSLEVLNLGDNNLTDA--GAAALASALlSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFG 291
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
48-231 |
3.26e-16 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 80.09 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 48 RALGKLLHKETLLKELVLSDCMLSEEGSTLlFQGLCANTSVQHLDLKGNNLRATGAEALGKLLRQNK-SIQSLTLEWNNL 126
Cdd:cd00116 71 QSLLQGLTKGCGLQELDLSDNALGPDGCGV-LESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPpALEKLVLGRNRL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 127 gTWEDAFATfCGGLAANSALRQLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLD 206
Cdd:cd00116 150 -EGASCEAL-AKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLN 227
|
170 180
....*....|....*....|....*
gi 266456389 207 LAGNNIPGDILRAVEQAMDHNQDRL 231
Cdd:cd00116 228 LGDNNLTDAGAAALASALLSPNISL 252
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
372-665 |
3.80e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.13 E-value: 3.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 372 LRSQVDELERKARsQQEQLFLTKQELTNTSAELKIRAIQ-AEERLDVEKRRAKQNMEDLEKLhSKEVDHMTRHLEESERA 450
Cdd:COG1196 198 LERQLEPLERQAE-KAERYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEEL-EAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 451 MQERVQRLEALRLSLEEELSRmkAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMV 530
Cdd:COG1196 276 LEELELELEEAQAEEYELLAE--LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 531 AESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQmgrmQADLVAQEALREKVAALERQMKVIGSE 610
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL----EELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 266456389 611 HREALLDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVLAYVQGSPLRA 665
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
261-616 |
9.06e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.97 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 261 DLMETIDKQREEMARDSRAsAVRVGQLQEALNERQsiINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRH 340
Cdd:COG1196 193 DILGELERQLEPLERQAEK-AERYRELKEELKELE--AELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 341 EKERkLERQEAADReskllrdLSAASEKNLLLRSQVDELERKARSQQEQLfltkQELTNTSAELKIRAIQAEERLDVEKR 420
Cdd:COG1196 270 EELR-LELEELELE-------LEEAQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 421 RAKQNMEDLEKLHSKEvdhmtRHLEESERAMQERVQRLEALRLSLEEELSRMKAAVLSERgqaeeelikarnQARLEEQH 500
Cdd:COG1196 338 ELEELEEELEEAEEEL-----EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL------------RAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 501 RLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELInKDQEKVAEVARVRVELQEQM 580
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE-ALLELLAELLEEAALLEAAL 479
|
330 340 350
....*....|....*....|....*....|....*.
gi 266456389 581 GRMQADLVAQEALREKVAALERQMKVIGSEHREALL 616
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-648 |
2.10e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 230 RLTAFRENQARTKILSKEVQHLQEEKskqfldlmETIDKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTE 309
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAEL--------EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 310 AALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKlERQEAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQ 389
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 390 LfltkQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQERVQRLEALRLSLEEEL 469
Cdd:COG1196 381 L----EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 470 SRMKAAVLSERGQAEEELIKARNQARLEEQHRLAhLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQR 549
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAA-ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 550 RLEELQQELINKDQEKVAEVARVRVEL-----QEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREALLDRESENAS 624
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDDEVAAAAieylkAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
410 420
....*....|....*....|....
gi 266456389 625 LREKLRLKEAEISRIRDEEAQRAS 648
Cdd:COG1196 616 YVLGDTLLGRTLVAARLEAALRRA 639
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
267-608 |
9.96e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 9.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 267 DKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKl 346
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK- 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 347 ERQEAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKiraiqaeeRLDVEKRRAKQNM 426
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT--------LLNEEAANLRERL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 427 EDLEKLHSKEVDHMTRHLEESERaMQERVQRLEALRLSLEEELSRMKAAVlsergQAEEELIKARNQARLEEQHRLAHLE 506
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEE-LSEDIESLAAEIEELEELIEELESEL-----EALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 507 EKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQelinkdqekvaevarvrVELQEQMGRMQAD 586
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS-----------------LTLEEAEALENKI 963
|
330 340
....*....|....*....|..
gi 266456389 587 LVAQEALREKVAALERQMKVIG 608
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELG 985
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
230-563 |
2.83e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 230 RLTAFRENQARTKILSKEVQ------HLQEEKSKQFLDLMETI-DKQREEMARDSRASAVRVGQLQEALNERQSIINALK 302
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELErqlkslERQAEKAERYKELKAELrELELALLVLRLEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 303 AKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQR-HEKERKLERQEAadRESKLLRDLSAASEKNLLLRSQVDELER 381
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEiSRLEQQKQILRE--RLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 382 KARSQQEQLFLTKQELTNTSAELKIRAIQAEERldveKRRAKQNMEDLEKLHSKEVDHmtRHLEESERA----MQERVQR 457
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEAELEEL----ESRLEELEEQLETLRSKVAQL--ELQIASLNNeierLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 458 LEALRLSLEEELSRMKAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARV 537
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL 491
|
330 340
....*....|....*....|....*.
gi 266456389 538 SQLNLQMEGQQRRLEELQQELINKDQ 563
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-651 |
1.18e-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: 61.61 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 338 QRHEKERKLER-QEAADRESKLLRDlsaaseknllLRSQVDELERKARSQQEQLFLtKQELTNTSAEL-KIRAIQAEERL 415
Cdd:TIGR02168 173 RRKETERKLERtRENLDRLEDILNE----------LERQLKSLERQAEKAERYKEL-KAELRELELALlVLRLEELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 416 DvEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQERVQRLEALR---LSLEEELSRMKA--AVLSERGQAEEELIKA 490
Cdd:TIGR02168 242 E-ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelYALANEISRLEQqkQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 491 RNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVA 570
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 571 RVRV------ELQEQMGRMQADLVAQEALREKVAALERQMKVigSEHREALLDRESENASLREKLRLKEAEISRIRDEEA 644
Cdd:TIGR02168 401 EIERlearleRLEDRRERLQQEIEELLKKLEEAELKELQAEL--EELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
....*..
gi 266456389 645 QRASFLQ 651
Cdd:TIGR02168 479 AAERELA 485
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
215-646 |
3.67e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.15 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 215 DILRAVEQAMDHNQDRLTAFRENQARTkilSKEVQHLQEEKSKQflDLMETIDKQREEMARDSRASAVRVGQLQEALNER 294
Cdd:PTZ00121 1253 EIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 295 QSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKleRQEAADRESKLLRDLSAASEKNLLLRS 374
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK--KADAAKKKAEEKKKADEAKKKAEEDKK 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 375 QVDELERKARSQQEQLFLTKQ-ELTNTSAELKIRAIQAEERLDVEKR-RAKQNMEDLEKL--HSKEVDHMTRHLEESERA 450
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKaEEKKKADEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKaeEAKKADEAKKKAEEAKKA 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 451 ------MQERVQRLEALRLSLEEELSRMKAAVLSERGQAEE----------------------------------ELIKA 490
Cdd:PTZ00121 1486 deakkkAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakkaeeakkadeakkaeekkkadelkkaeelkkaEEKKK 1565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 491 RNQARLEEQHRLAHLE--EKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQ---ELINKDQEK 565
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKkveQLKKKEAEE 1645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 566 VAEVARVRVElqEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISR----IRD 641
Cdd:PTZ00121 1646 KKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkaeeLKK 1723
|
....*
gi 266456389 642 EEAQR 646
Cdd:PTZ00121 1724 AEEEN 1728
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
217-608 |
5.34e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 217 LRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQS 296
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 297 IINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAAD-------RESKLLRDLSAASEKN 369
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegflegvKAALLLAGLRGLAGAV 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 370 LLLRSQVDELE-----RKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHL 444
Cdd:COG1196 527 AVLIGVEAAYEaaleaALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 445 EESERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQAEEELIKAR---NQARLEEQHRLAHLEEKIRLLAQARDEAQG 521
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGeggSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 522 TCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQ-------EALR 594
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEElpeppdlEELE 766
|
410
....*....|....
gi 266456389 595 EKVAALERQMKVIG 608
Cdd:COG1196 767 RELERLEREIEALG 780
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
229-645 |
2.31e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 229 DRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSR---ASAVRVGQLQEALNERQSIINALKAKL 305
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERereELAEEVRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 306 QMTEAALALSEQKVRDLG----ELLVAGDQERQSLsQRHEKERKLERQEAADRESKLLRDLSAASEknllLRSQVDELER 381
Cdd:PRK02224 303 GLDDADAEAVEARREELEdrdeELRDRLEECRVAA-QAHNEEAESLREDADDLEERAEELREEAAE----LESELEEARE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 382 KARSQQEQLfltkQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDhmtrhLEESERAMQERVQRLEAL 461
Cdd:PRK02224 378 AVEDRREEI----EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAE-----LEATLRTARERVEEAEAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 462 R-----------------LSLEEELSRMKAAVLSERGQAEEELikARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCV 524
Cdd:PRK02224 449 LeagkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEV--EEVEERLERAEDLVEAEDRIERLEERREDLEELIA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 525 QQKQMVAESQARVSQLNLQMEGQQRRLEElQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALERQM 604
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEE-KREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 266456389 605 KVIGS--EHREALLDRESEN----ASLREKLRLKEAEISRIRDEEAQ 645
Cdd:PRK02224 606 DEIERlrEKREALAELNDERrerlAEKRERKRELEAEFDEARIEEAR 652
|
|
| LRR_RI |
cd00116 |
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ... |
88-228 |
3.07e-08 |
|
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).
Pssm-ID: 238064 [Multi-domain] Cd Length: 319 Bit Score: 55.82 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 88 VQHLDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGTWEDAFATFCGGLAANSALRQLDLRNNQISHKGAEELALA 167
Cdd:cd00116 25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRIPRGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVLESL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 168 LKgNTTLQQLDLRWNNIGLLGGR-----------------------------ALVNCLPSNRTLWKLDLAGNNIPGDILR 218
Cdd:cd00116 105 LR-SSSLQELKLNNNGLGDRGLRllakglkdlppaleklvlgrnrlegasceALAKALRANRDLKELNLANNGIGDAGIR 183
|
170
....*....|
gi 266456389 219 AVEQAMDHNQ 228
Cdd:cd00116 184 ALAEGLKANC 193
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
248-605 |
3.13e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 57.06 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 248 VQHLQEEKSKQFLDLMETIDKQREEMARDSRASAV-RVGQLQEALNERQSIINALKAklqmteaalalseqkvrdlgell 326
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVeRRRKLEEAEKARQAEMDRQAA----------------------- 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 327 VAGDQERQSLsqrhEKERKLER--QEAADRESKLLRDLSAASEKnlllrSQVDELERKARSQQEQLFLTKQELtntSAEL 404
Cdd:pfam17380 335 IYAEQERMAM----ERERELERirQEERKRELERIRQEEIAMEI-----SRMRELERLQMERQQKNERVRQEL---EAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 405 KIRaIQAEERldveKRRAKQNMEDLEKLHSKEVDHMTRHLEESEramQERVQRLEALRlslEEELSRMKAAvlsERGQAE 484
Cdd:pfam17380 403 KVK-ILEEER----QRKIQQQKVEMEQIRAEQEEARQREVRRLE---EERAREMERVR---LEEQERQQQV---ERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 485 EELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQgtcvqqKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQE 564
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILEKELEER------KQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER 542
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 266456389 565 KVAEVARVRVELQEQMGRMQADLVAQEALrEKVAALERQMK 605
Cdd:pfam17380 543 RKQQEMEERRRIQEQMRKATEERSRLEAM-EREREMMRQIV 582
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
439-646 |
4.33e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 439 HMTRHLEE-SERAMQERVQRLEALRLSLEEElsrMKAAVLSERGQAEEElikarnqarleEQHRLAHLEEKIRLLAQard 517
Cdd:pfam17380 276 HIVQHQKAvSERQQQEKFEKMEQERLRQEKE---EKAREVERRRKLEEA-----------EKARQAEMDRQAAIYAE--- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 518 eaqgtcvqQKQMVAESQARVSQLnlQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAqeALREKV 597
Cdd:pfam17380 339 --------QERMAMERERELERI--RQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA--ARKVKI 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 266456389 598 AALERQMKVIGSEHREALLDRESENASLREKLRLKEA---EISRIRDEEAQR 646
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEErarEMERVRLEEQER 458
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
437-640 |
5.28e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 437 VDHMtRHLEESERAMQERVQRLEALRlSLEEELSRMKAAVlsergQAEEELIKARNQARLEE-QHRLAHLEEKIRLLAQA 515
Cdd:COG4913 231 VEHF-DDLERAHEALEDAREQIELLE-PIRELAERYAAAR-----ERLAELEYLRAALRLWFaQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 516 RDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQ-RRLEELQQELINKDQEKvAEVARVRVELQEQMGRMQADLVAQE--- 591
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLEREL-EERERRRARLEALLAALGLPLPASAeef 382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 266456389 592 -ALREKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISRIR 640
Cdd:COG4913 383 aALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| RNA1 |
COG5238 |
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ... |
84-227 |
7.53e-08 |
|
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444072 [Multi-domain] Cd Length: 434 Bit Score: 55.18 E-value: 7.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 84 ANTSVQHLDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGTwedaFATFCGGLAANSALRQLDLRNNQISHKGAEE 163
Cdd:COG5238 124 AKTLEDSLILYLALPRRINLIQVLKDPLGGNAVHLLGLAARLGLL----AAISMAKALQNNSVETVYLGCNQIGDEGIEE 199
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 266456389 164 LALALKGNTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLDLAGNNIPGDILRAVEQAMDHN 227
Cdd:COG5238 200 LAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN 263
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
24-212 |
1.34e-07 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 54.55 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 24 LQQLHQLPKGGLDLTTQSLTVETCRALGKLLHKETLLKELVLSDCmlseegstllfQGLCANTSVQHLDLKGNNLratga 103
Cdd:COG4886 62 LSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-----------EELSNLTNLESLDLSGNQL----- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 104 EALGKLLRQNKSIQSLTLEWNNLgtwedafATFCGGLAANSALRQLDLRNNQIShkgaeELALALKGNTTLQQLDLRWNN 183
Cdd:COG4886 126 TDLPEELANLTNLKELDLSNNQL-------TDLPEPLGNLTNLKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQ 193
|
170 180
....*....|....*....|....*....
gi 266456389 184 IGLLGgralvNCLPSNRTLWKLDLAGNNI 212
Cdd:COG4886 194 ITDLP-----EPLGNLTNLEELDLSGNQL 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
347-643 |
3.24e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.92 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 347 ERQEAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQLfltkqeltntsAELKIRAIQAEERLDVEKRRAKQNM 426
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-----------GEIEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 427 EDLEKLhskevdhmTRHLEESERAMQERVQRLEALRL---SLEEELSRMKAAVLSERGQAEEELIKARNQARLEEQHRLA 503
Cdd:TIGR02169 744 EDLSSL--------EQEIENVKSELKELEARIEELEEdlhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 504 HLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKdQEKVAEVARVRVELQEQMGRM 583
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL-EAALRDLESRLGDLKKERDEL 894
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 584 QADLVAQEALREKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISRIRDEE 643
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE 954
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
219-630 |
3.52e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 219 AVEQAMDHNQDRLTAFREN--QARTKILSKEVQhlQEEKSKQFLDLMETIDKQREEMAR-DSRASAVRvgqlqEALNERQ 295
Cdd:PRK02224 311 AVEARREELEDRDEELRDRleECRVAAQAHNEE--AESLREDADDLEERAEELREEAAElESELEEAR-----EAVEDRR 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 296 SIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRhEKERKLERQEAADRESKLLRDLSAAS----EKNLL 371
Cdd:PRK02224 384 EEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRER-EAELEATLRTARERVEEAEALLEAGKcpecGQPVE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 372 LRSQVDELERKaRSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKR--RAKQNMEDLEKLHSkevDHMTRHLEESER 449
Cdd:PRK02224 463 GSPHVETIEED-RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEERREDLEELIA---ERRETIEEKRER 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 450 A--MQERVQRLEAlrlslEEELSRMKAAVLSERGQAEEELIKARNQARLE---EQHRLAHLEEKIRLLAQARDEAQGTCV 524
Cdd:PRK02224 539 AeeLRERAAELEA-----EAEEKREAAAEAEEEAEEAREEVAELNSKLAElkeRIESLERIRTLLAAIADAEDEIERLRE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 525 QQKQM----------VAESQARVSQLNLQMEGQqrRLEELQQELINKDQ------EKVAEVARVRVELQEQMGRMQADLV 588
Cdd:PRK02224 614 KREALaelnderrerLAEKRERKRELEAEFDEA--RIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVENELE 691
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 266456389 589 AQEALREKVAALERQMKVIGSEHREAlLDRESENASLREKLR 630
Cdd:PRK02224 692 ELEELRERREALENRVEALEALYDEA-EELESMYGDLRAELR 732
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-596 |
4.17e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 236 ENQARTKILSKEVQHLQEEKSKQfldlmETIDKQREEMARDSRASAvrvgQLQEALNERQSIINALKAKLQMTEAALALS 315
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKA-----EEAKKKAEEAKKADEAKK----KAEEAKKADEAKKKAEEAKKKADEAKKAAE 1507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 316 EQKVRDlgELLVAGDQERQSLSQRHEKERKLERQEAADrESKLLRDLSAASEknLLLRSQVDELERKARSQQEQ-LFLTK 394
Cdd:PTZ00121 1508 AKKKAD--EAKKAEEAKKADEAKKAEEAKKADEAKKAE-EKKKADELKKAEE--LKKAEEKKKAEEAKKAEEDKnMALRK 1582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 395 QELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEV---DHMTRHLEESERAMQERVQRLEALRLslEEELSR 471
Cdd:PTZ00121 1583 AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELkkaEEEKKKVEQLKKKEAEEKKKAEELKK--AEEENK 1660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 472 MKAAVLSERGQAE----EELIKARNQARLEEQHRLAHLEE--KIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQME 545
Cdd:PTZ00121 1661 IKAAEEAKKAEEDkkkaEEAKKAEEDEKKAAEALKKEAEEakKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 266456389 546 GQQRRLEELQQEliNKDQEKVAEVARVRVELQEQMgRMQADLVAQEALREK 596
Cdd:PTZ00121 1741 EDKKKAEEAKKD--EEEKKKIAHLKKEEEKKAEEI-RKEKEAVIEEELDEE 1788
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-653 |
5.90e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 5.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 236 ENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDS----RASAVRVGQLQEALNERQSIINALKAKlQMTEAA 311
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAeearKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 312 LALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKLlrdlsAASEKNLLLRSQVDELERKARSQQEQLF 391
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKA-----EAVKKAEEAKKDAEEAKKAEEERNNEEI 1254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 392 LTKQELTNTSAELKIRAIQAEERL---DVEKRRAKQNMEDLEKLHS-KEVDHMTRHLEESERA------MQERVQRLEAL 461
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARkadELKKAEEKKKADEAKKAEEkKKADEAKKKAEEAKKAdeakkkAEEAKKKADAA 1334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 462 RLSLEE-----ELSRMKAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQArDEAQGTCVQQKQMvAESQAR 536
Cdd:PTZ00121 1335 KKKAEEakkaaEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKK-ADELKK 1412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 537 VSQLNLQMEGQQRRLEELQQElinKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREALL 616
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKA---DEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 266456389 617 DRESENASLREKLRLKEAEISRIRD----EEAQRASFLQNA 653
Cdd:PTZ00121 1490 KKAEEAKKKADEAKKAAEAKKKADEakkaEEAKKADEAKKA 1530
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
396-642 |
7.30e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 396 ELTNTSAELKIRAIQAEERLDvEKRRAKQNMEDLEKLHSKEVDHMTRHLeeseRAMQERVQRLEALRLSLEEELSRMKAA 475
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKELEELSRQI----SALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 476 VLSERGQAEEELikarnQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQ 555
Cdd:TIGR02168 756 LTELEAEIEELE-----ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 556 QElinkdqekVAEVARVRVELQEQMGRMQADLV----AQEALREKVAALERQMKVIG---SEHREALLDRESENASLREK 628
Cdd:TIGR02168 831 RR--------IAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLnerASLEEALALLRSELEELSEE 902
|
250
....*....|....
gi 266456389 629 LRLKEAEISRIRDE 642
Cdd:TIGR02168 903 LRELESKRSELRRE 916
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
286-648 |
1.14e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 286 QLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKLLRDLSAA 365
Cdd:TIGR00618 212 CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 366 SEKNLLLRSQVDELERKARSQQEQLFLTKQELtnTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLE 445
Cdd:TIGR00618 292 AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR--AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 446 ESERAMQERvQRLEALRLSLEEELSRMKAAV-LSERGQAEEELIKARNQARLEEQHRLAHL--EEKIRLLAQARDEAQGT 522
Cdd:TIGR00618 370 ISCQQHTLT-QHIHTLQQQKTTLTQKLQSLCkELDILQREQATIDTRTSAFRDLQGQLAHAkkQQELQQRYAELCAAAIT 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 523 CVQQKQMVAESQARVSQLNLQMEGQQrrlEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALE- 601
Cdd:TIGR00618 449 CTAQCEKLEKIHLQESAQSLKEREQQ---LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGp 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 266456389 602 RQMKVIGSEHREALLDRESENA-----SLREKLRLKEAEISRIRDEEAQRAS 648
Cdd:TIGR00618 526 LTRRMQRGEQTYAQLETSEEDVyhqltSERKQRASLKEQMQEIQQSFSILTQ 577
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
357-645 |
1.17e-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: 51.99 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 357 KLLRDLSAASEKNLLLRSQVDELerkaRSQQEQLFLTKQELtntsaeLKIRAIQAE--ERLDVEKRRAKQNMEDLEKLHS 434
Cdd:TIGR02169 174 KALEELEEVEENIERLDLIIDEK----RQQLERLRREREKA------ERYQALLKEkrEYEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 435 KEVDHMTRHLEESERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQAEEELikarnqarLEEQHRLAHLEEKIRLLAQ 514
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI--------GELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 515 ARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELinkdQEKVAEVARVRVELQEQMGRMQADLVAQEALR 594
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY----AELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 266456389 595 EKVAALERQMkvigSEHREALLDRESENASLREKLRLKEAEISRIRDEEAQ 645
Cdd:TIGR02169 392 EKLEKLKREI----NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
324-645 |
2.75e-06 |
|
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: 50.89 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 324 ELLVAGDQERQS--LSQRHEKERKLE--RQEAADRESKLLRDLSAASEKNLLLRSQVDELER----KARSQQEQLFLTKQ 395
Cdd:pfam15921 277 EVEITGLTEKASsaRSQANSIQSQLEiiQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 396 ELTNTSAE-----------------LKIRAIQAEERLDVEKRRAKQnMEDLEKLHSKEVDHMTRHLEesERAMQerVQRL 458
Cdd:pfam15921 357 ELTEARTErdqfsqesgnlddqlqkLLADLHKREKELSLEKEQNKR-LWDRDTGNSITIDHLRRELD--DRNME--VQRL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 459 EALRLSLEEELsrmkaavlseRGQAEEEL--IKARNQARLEEQHRLAHLEEKIRLLAQARDEaqgtcVQQKQMVAESQAR 536
Cdd:pfam15921 432 EALLKAMKSEC----------QGQMERQMaaIQGKNESLEKVSSLTAQLESTKEMLRKVVEE-----LTAKKMTLESSER 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 537 -VSQLNLQMEGQQRRLEELQQE---LINKDQEKVAEVARVRVElQEQMGRMQAD---LVAQEALREKVAALERQ-----M 604
Cdd:pfam15921 497 tVSDLTASLQEKERAIEATNAEitkLRSRVDLKLQELQHLKNE-GDHLRNVQTEceaLKLQMAEKDKVIEILRQqienmT 575
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 266456389 605 KVIGSEHR--------EALLDRE--SENASLREKLRLKEAEISRIRDEEAQ 645
Cdd:pfam15921 576 QLVGQHGRtagamqveKAQLEKEinDRRLELQEFKILKDKKDAKIRELEAR 626
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
343-605 |
3.79e-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: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 343 ERKLERQEAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKiRAIQAEERLdvEKRRA 422
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA-RLEAEVEQL--EERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 423 KQNMEDLEKLHSKEVDHMTRHLEESERAmqervqRLEALRLSLEEELSRMKaavlSERGQAEEELIKARNQARLEEQhRL 502
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELA------EAEAEIEELEAQIEQLK----EELKALREALDELRAELTLLNE-EA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 503 AHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKvAEVARVRVELQEQMGR 582
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER-ASLEEALALLRSELEE 898
|
250 260
....*....|....*....|...
gi 266456389 583 MQADLvaqEALREKVAALERQMK 605
Cdd:TIGR02168 899 LSEEL---RELESKRSELRRELE 918
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
331-567 |
4.67e-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: 49.38 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 331 QERQSLSQRHEKERKlERQEAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQ 410
Cdd:COG4942 27 AELEQLQQEIAELEK-ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 411 AEERLDVEKRRAKQNMEDLeKLHSKEVDHMTRHLEESERAMQERVQRLEALRLSLEEelsrmkaavlsergqaEEELIKA 490
Cdd:COG4942 106 LAELLRALYRLGRQPPLAL-LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE----------------LAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 266456389 491 RNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVA 567
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
215-647 |
6.77e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.75 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 215 DILRAVEQAMDHNQDRLTAFRENQARTKIlsKEVQHLQEEKSKQFLDLMETIDKQREEMardSRASAVRVGQlqealnER 294
Cdd:PTZ00121 1186 EVRKAEELRKAEDARKAEAARKAEEERKA--EEARKAEDAKKAEAVKKAEEAKKDAEEA---KKAEEERNNE------EI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 295 QSIINALKAKLQMTEAALALSEQKVRDlgELLVAGDQERQSLSQRHEKERKLERQEAADRESKLLRDLSAASEKNlllRS 374
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKAD--ELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA---KK 1329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 375 QVDELERKARSQQEQLFLTKQELTNTSAELKI---RAIQAEERLDVEKRRA---KQNMEDLEKLHS--KEVDHMTRHLEE 446
Cdd:PTZ00121 1330 KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAaeeKAEAAEKKKEEAKKKAdaaKKKAEEKKKADEakKKAEEDKKKADE 1409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 447 SERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQAEE------ELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQ 520
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEakkkaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK 1489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 521 GTCVQQKQMVAESQarvsqlnlQMEGQQRRLEELQ--QELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVA 598
Cdd:PTZ00121 1490 KKAEEAKKKADEAK--------KAAEAKKKADEAKkaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 266456389 599 ALERQMKVIGSEHREALLDRESENASLREKLRLKEA-----EISRIRDEEAQRA 647
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVmklyeEEKKMKAEEAKKA 1615
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
235-605 |
8.87e-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: 49.30 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 235 RENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAvRVGQLQEALNERQSIINALKAKLQMTEAALAL 314
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK-EIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 315 SEQKVRDLGELLvagDQERQSLSQRHEKERKLERQEAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQeqlfLTK 394
Cdd:TIGR02169 756 VKSELKELEARI---EELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT----LEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 395 QELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHmtrhlEESERAMQERVQRLEALRLSLEEELSRMKa 474
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL-----EAALRDLESRLGDLKKERDELEAQLRELE- 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 475 avlSERGQAEEELIKARnqarleeqHRLAHLEEKIRLLAQARDEAqGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEEL 554
Cdd:TIGR02169 903 ---RKIEELEAQIEKKR--------KRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 266456389 555 qQELINKDQEKVAEVARVRVELQEQMGRMQADlvaQEALREKVAALERQMK 605
Cdd:TIGR02169 971 -EPVNMLAIQEYEEVLKRLDELKEKRAKLEEE---RKAILERIEEYEKKKR 1017
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
409-646 |
9.16e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 9.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 409 IQAEErlDVEKRRAKQNMEDLEKLHS-KEVDHMTRHLEESERAMQERVQRLEALRLSLEEelSRMKAAVLSERGQAEEEL 487
Cdd:PRK03918 185 IKRTE--NIEELIKEKEKELEEVLREiNEISSELPELREELEKLEKEVKELEELKEEIEE--LEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 488 IKARNQARLEEQHRLAHLEEKIRLLAQARDEAQ------GTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELqqeliNK 561
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL-----EE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 562 DQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREAlLDRESENAS-----LREKLRLKEAEI 636
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEK-LEKELEELEkakeeIEEEISKITARI 414
|
250
....*....|
gi 266456389 637 SRIRDEEAQR 646
Cdd:PRK03918 415 GELKKEIKEL 424
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
225-536 |
1.15e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 225 DHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQSI---INAL 301
Cdd:PLN02939 96 DHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALqgkINIL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 302 KAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLerqeaadrESKLLRDLSAASEKNLLLRSQVDELER 381
Cdd:PLN02939 176 EMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLC--------VHSLSKELDVLKEENMLLKDDIQFLKA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 382 K---ARSQQEQLFLTKQE---LTNTSAELKIRAIQAEErlDVEKRRAKQ---------NMEDLEKLHSKEVDHMTRHLEE 446
Cdd:PLN02939 248 ElieVAETEERVFKLEKErslLDASLRELESKFIVAQE--DVSKLSPLQydcwwekveNLQDLLDRATNQVEKAALVLDQ 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 447 SeRAMQERVQRLEAlrlSLEE----ELSRMKAAVLSERGQAEEElikaRNQARLEEQHrlahleEKIRLLAQARDEAQGT 522
Cdd:PLN02939 326 N-QDLRDKVDKLEA---SLKEanvsKFSSYKVELLQQKLKLLEE----RLQASDHEIH------SYIQLYQESIKEFQDT 391
|
330
....*....|....
gi 266456389 523 CvqqKQMVAESQAR 536
Cdd:PLN02939 392 L---SKLKEESKKR 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
351-592 |
1.26e-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: 47.84 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 351 AADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKiraiQAEERLDVEKRRAKQNMEDLE 430
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIR----ALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 431 KLHsKEVDHMTRHLEESERAMQERVQRLEALRLsleeeLSRMKAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIR 510
Cdd:COG4942 94 ELR-AELEAQKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 511 LLAQARDeaqgtcvQQKQMVAESQARVSQLNLQMEGQQRRLEELQQElINKDQEKVAEVARVRVELQEQMGRMQADLVAQ 590
Cdd:COG4942 168 ELEAERA-------ELEALLAELEEERAALEALKAERQKLLARLEKE-LAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
..
gi 266456389 591 EA 592
Cdd:COG4942 240 AE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
444-656 |
1.32e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 444 LEESERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQ---AEEELIKARNQARLEEQ------HRLAHLEEKIRLLAQ 514
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisaLRKDLARLEAEVEQLEEriaqlsKELTELEAEIEELEE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 515 ARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQqelinkdqekvAEVARVRVELQEQMGRMqadlvaqEALR 594
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR-----------AELTLLNEEAANLRERL-------ESLE 830
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 266456389 595 EKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVLA 656
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
268-571 |
1.86e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 268 KQREEMARDSRASAVRVGQLQEALNERQSiiNALKAKLQMTEAALALSEQKVRDLGELLVAGD-QERQSLSQRHEKERKL 346
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKA--DEAKKAEEAKKADEAKKAEEKKKADELKKAEElKKAEEKKKAEEAKKAE 1573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 347 ERQEAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNM 426
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 427 EDLEKLH------SKEVDHMTRHLEESERAMQERVQRLEALRLSLEEelsrmkAAVLSERGQAEEELIKARNQARLEEQH 500
Cdd:PTZ00121 1654 KAEEENKikaaeeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE------AKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 266456389 501 RLAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVAR 571
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
217-635 |
1.88e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 217 LRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSR------ASAVRVGQLQEA 290
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKevkeleELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 291 LNERQSIINALKAKLQMTEAALALSEQKVRDLGELlVAGDQERQSLSQRHEKERKLeRQEAADRESKLLRDLSAASEKNL 370
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEF-YEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 371 LLRSQVDELERKaRSQQEQLFLTKQELTNTSAELKIRAIQAEErldvekrrAKQNMEDLEKLHSKEVDHMTRHLEESERA 450
Cdd:PRK03918 325 GIEERIKELEEK-EERLEELKKKLKELEKRLEELEERHELYEE--------AKAKKEELERLKKRLTGLTPEKLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 451 MQERVQRLEALRLSLEEELSRMKAAVlSERGQAEEELIKARNQ-----ARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQ 525
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEI-KELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 526 QKQMVAESQ------------ARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEAL 593
Cdd:PRK03918 475 ERKLRKELRelekvlkkeselIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 266456389 594 REKVAALERQMKVIGSEHREALLDRESENASLREKL--RLKEAE 635
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGFESVEELeeRLKELE 598
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
358-605 |
1.95e-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: 47.45 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 358 LLRDLSAASEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKiraiQAEERLDVEKRRAKQNMEDLEKLhskev 437
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAAL----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 438 dhmtrhlEESERAMQERVQRLEALRLSLEEELSRMkAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEkirlLAQARD 517
Cdd:COG4942 82 -------EAELAELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY----LAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 518 EAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKV 597
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
....*...
gi 266456389 598 AALERQMK 605
Cdd:COG4942 230 ARLEAEAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
302-497 |
2.03e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 302 KAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESK-LLRDLSAASEKNLLLRSQVDELE 380
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 381 RkARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLEE-SERAMQERVQRle 459
Cdd:COG4913 689 A-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErFAAALGDAVER-- 765
|
170 180 190
....*....|....*....|....*....|....*...
gi 266456389 460 ALRLSLEEELSRMKAavlsERGQAEEELIKARNQARLE 497
Cdd:COG4913 766 ELRENLEERIDALRA----RLNRAEEELERAMRAFNRE 799
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
336-516 |
3.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 336 LSQRHEKERKLERQEAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQLfltkqeltntsAELKIRAIQAEERL 415
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAEL-----------ERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 416 D-VEKRRAKQNMEDLEKLhSKEVDHMTRHLEESERAMQERVQRLEALRLSLE----------EELSRMKAAVLSERGQAE 484
Cdd:COG4913 326 DeLEAQIRGNGGDRLEQL-EREIERLERELEERERRRARLEALLAALGLPLPasaeefaalrAEAAALLEALEEELEALE 404
|
170 180 190
....*....|....*....|....*....|..
gi 266456389 485 EELIKARNQARlEEQHRLAHLEEKIRLLAQAR 516
Cdd:COG4913 405 EALAEAEAALR-DLRRELRELEAEIASLERRK 435
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
244-493 |
4.22e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 244 LSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLG 323
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 324 ELLVAGDQERQSLSQRHEKERKlERQEAADRESKLLRDLSAA-SEKNLLLRSQVDELERKARSQQEQLFLtKQELTNTSA 402
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDK-EFAETRDELKDYREKLEKLkREINELKRELDRLQEELQRLSEELADL-NAAIAGIEA 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 403 ---ELKIRAIQAEERLDVEKRRAKQNMEDLEKLhskevdhmtrhlEESERAMQERVQRLEALRLSLEEELSRMKAAVLSE 479
Cdd:TIGR02169 435 kinELEEEKEDKALEIKKQEWKLEQLAADLSKY------------EQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
250
....*....|....*....
gi 266456389 480 R-----GQAEEELIKARNQ 493
Cdd:TIGR02169 503 EervrgGRAVEEVLKASIQ 521
|
|
| LRR_8 |
pfam13855 |
Leucine rich repeat; |
146-212 |
1.96e-04 |
|
Leucine rich repeat;
Pssm-ID: 404697 [Multi-domain] Cd Length: 61 Bit Score: 39.82 E-value: 1.96e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 266456389 146 LRQLDLRNNQISHKGAEelalALKGNTTLQQLDLRWNNIGLLGGRALVnCLPSnrtLWKLDLAGNNI 212
Cdd:pfam13855 3 LRSLDLSNNRLTSLDDG----AFKGLSNLKVLDLSNNLLTTLSPGAFS-GLPS---LRYLDLSGNRL 61
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
315-613 |
1.98e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 315 SEQKVRDLGELLVAGDQERQSLSQRHEKERKLER-----QEAADRESKLLRDLSAASEK-NLLL------------RSQV 376
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEmarelEELSARESDLEQDYQAASDHlNLVQtalrqqekieryQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 377 DELERKARSQQEQLfltkQELTNTSAELKIRAIQAEERLDvekrRAKQNMEDLEklhskevdhmtRHLEESE-RAMQER- 454
Cdd:COG3096 357 EELTERLEEQEEVV----EEAAEQLAEAEARLEAAEEEVD----SLKSQLADYQ-----------QALDVQQtRAIQYQq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 455 -VQRLE-ALRLSLEEELSRMKAAVLSERGQAEEELIkarNQARLEEQHRLAHLEEKIRLLAQA------------RDEAQ 520
Cdd:COG3096 418 aVQALEkARALCGLPDLTPENAEDYLAAFRAKEQQA---TEEVLELEQKLSVADAARRQFEKAyelvckiageveRSQAW 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 521 GTCVQQKQMVAESQA---RVSQLNLQM------EGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQE 591
Cdd:COG3096 495 QTARELLRRYRSQQAlaqRLQQLRAQLaeleqrLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
330 340
....*....|....*....|..
gi 266456389 592 ALREKVAALERQMKVIGSEHRE 613
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKE 596
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
339-569 |
2.59e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 339 RHEK--ERKLERQ-----EAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQA 411
Cdd:COG4913 589 RHEKddRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 412 E-ERLDVEKRRAKQNMEDLEKlhskevdhmtrhLEESERAMQERVQRLEALRLSLEEELSRMKaavlSERGQAEEELikA 490
Cdd:COG4913 669 EiAELEAELERLDASSDDLAA------------LEEQLEELEAELEELEEELDELKGEIGRLE----KELEQAEEEL--D 730
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 266456389 491 RNQARLEEQHRLAHLEEkiRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEV 569
Cdd:COG4913 731 ELQDRLEAAEDLARLEL--RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADL 807
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
75-212 |
4.14e-04 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 43.38 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 75 STLLFQGLCANTSVQHLDLKGNNLRATGAEALGKLLRQNKSIQSLTLEWNNLGTWEDAFATFCGGLAANSALRQLDLRNN 154
Cdd:COG4886 44 SLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGN 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 266456389 155 QIShkgaeELALALKGNTTLQQLDLRWNNIgllggRALVNCLPSNRTLWKLDLAGNNI 212
Cdd:COG4886 124 QLT-----DLPEELANLTNLKELDLSNNQL-----TDLPEPLGNLTNLKSLDLSNNQL 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
217-640 |
6.12e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 217 LRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQfldlmeTIDKQREEMARDSRASAVRVGQLQEALNERQS 296
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL------REELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 297 IINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKE---RKLERQEAADRESKLLRDLSAASEKNLLLR 373
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 374 SQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQE 453
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 454 RVQRLEALRLSLEEELSRMKAAVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQKQMVAES 533
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 534 QARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVA-----RVRVELQEQMGRMQADLVAQEALREKVAALERQMKVIG 608
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELEAELEQLE 466
|
410 420 430
....*....|....*....|....*....|..
gi 266456389 609 SEHReaLLDRESENASLREKLRLKEAEISRIR 640
Cdd:COG4717 467 EDGE--LAELLQELEELKAELRELAEEWAALK 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-405 |
6.24e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 216 ILRAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQEEKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQ 295
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 296 SIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAADRESKLLRDlsaaseknllLRSQ 375
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE----------LQEE 455
|
170 180 190
....*....|....*....|....*....|
gi 266456389 376 VDELERKARSQQEQLFLTKQELTNTSAELK 405
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELA 485
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
236-508 |
6.47e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 236 ENQARTKILSKEVQHLQEEKSKQFLDL------METIDKQREEMARDSRASAVRVGQLQealNERQSIINALKAKLQMTE 309
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTLELkkhqedIINCKKQEERMLKQIENLEEKEMNLR---DELESVREEFIQKGDEVK 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 310 AALALSEQKVRDLGELLVAGDQERQSLSQ-----RHEKERKLERQEAADRESKLLRDLSAASEKNL-LLRSQVDELERKA 383
Cdd:pfam05483 566 CKLDKSEENARSIEYEVLKKEKQMKILENkcnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLnAYEIKVNKLELEL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 384 RSQQEQLfltkQELTNT-SAELKIRAIqAEERLDVEKRRAKQNMEDLEKLHsKEVDH------------MTRHLEESERA 450
Cdd:pfam05483 646 ASAKQKF----EEIIDNyQKEIEDKKI-SEEKLLEEVEKAKAIADEAVKLQ-KEIDKrcqhkiaemvalMEKHKHQYDKI 719
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 266456389 451 MQER----------VQRLEALRLSLEEELSRMKAAVLSERGQAEEELiKARNQARLEEQHRLAHLEEK 508
Cdd:pfam05483 720 IEERdselglyknkEQEQSSAKAALEIELSNIKAELLSLKKQLEIEK-EEKEKLKMEAKENTAILKDK 786
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
254-605 |
7.89e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 254 EKSKQFLDLMETIDKQREEMARDSRASAVRVGQLQEALNERQSIINA-LKAKLQMTEAALALS-EQKVRDLGELLVAGDQ 331
Cdd:pfam12128 340 ETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIrEARDRQLAVAEDDLQA 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 332 ERQSLSQRHE------KERKLERQEAADRESKLLRDLSAASEKNLLLRSQVDELERkARSQQEQLFLTKQELTNTSAELK 405
Cdd:pfam12128 420 LESELREQLEagklefNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIER-AREEQEAANAEVERLQSELRQAR 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 406 IRAIQAEERLDVEKRRAKQNMEDLEKLHSK---------------------------------------EVDHMTRHLEE 446
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflrkeapdweqsigkvispellhrtdldpEVWDGSVGGEL 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 447 SERAMQERVQRLE-----ALRLSLEEELSRMKAAVLSER---GQAEEELIKARNQ---ARLEEQHRLAHLEEKIRLLAQA 515
Cdd:pfam12128 579 NLYGVKLDLKRIDvpewaASEEELRERLDKAEEALQSARekqAAAEEQLVQANGElekASREETFARTALKNARLDLRRL 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 516 RDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEvarVRVELQEQMGRMQADLVAQEA-LR 594
Cdd:pfam12128 659 FDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKRE---ARTEKQAYWQVVEGALDAQLAlLK 735
|
410
....*....|.
gi 266456389 595 EKVAALERQMK 605
Cdd:pfam12128 736 AAIAARRSGAK 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
490-647 |
9.30e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 490 ARNQARLEEQHR-LAHLEEKIRLLAQARDEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQE---- 564
Cdd:TIGR02169 677 QRLRERLEGLKReLSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienv 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 565 --KVAEVARVRVELQEQMGRMQADLVAQEA--LREKVAALERQMKVIGSEHREALLDRESENASLREKLRLKEAEISRIR 640
Cdd:TIGR02169 757 ksELKELEARIEELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836
|
....*..
gi 266456389 641 DEEAQRA 647
Cdd:TIGR02169 837 ELQEQRI 843
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
218-487 |
1.23e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 218 RAVEQAMDHNQDRLTAFRENQARTKILSKEVQHLQ--EEKSKQFLDLMETIDKQREEMAR-DSRASAVRVGQLQEALNER 294
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 295 QSIINALKAKLQMTEAALALSEQKVRDLGELLvagdqerqslsqrhekerkleRQEAADRESKLLRDLSAaseknllLRS 374
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQI---------------------RGNGGDRLEQLEREIER-------LER 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 375 QVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDhmtrhLEESERAMQER 454
Cdd:COG4913 353 ELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD-----LRRELRELEAE 427
|
250 260 270
....*....|....*....|....*....|...
gi 266456389 455 VQRLEALRLSLEEELSRMKAAVLSERGQAEEEL 487
Cdd:COG4913 428 IASLERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
444-661 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 444 LEESERAMQERVQRLEALRLSLEEELSRmKAAVLSERGQAEEELIKARNQARLEEQhRLAHLEEKIRLLAQARDEAQGTC 523
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQ-ELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 524 VQQKQMVAE------SQARVSQLNLQMEGQQ-----------RRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQAD 586
Cdd:COG4942 100 EAQKEELAEllralyRLGRQPPLALLLSPEDfldavrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 587 LVAQEALREK-----------VAALERQMKvigsehreallDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVL 655
Cdd:COG4942 180 LAELEEERAAlealkaerqklLARLEKELA-----------ELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....*.
gi 266456389 656 AYVQGS 661
Cdd:COG4942 249 AALKGK 254
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
328-591 |
1.31e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 328 AGDQERQSLS---QRHEKERKLERQEAADRESKLLRDLSAASE-----------------------KNLLLRSQVDELER 381
Cdd:pfam02029 56 GGLDEEEAFLdrtAKREERRQKRLQEALERQKEFDPTIADEKEsvaerkenneeeensswekeekrDSRLGRYKEEETEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 382 KARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDvEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQER-VQRLEA 460
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVP-TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVkSQNGEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 461 LRLSLEEELSRMKAAVLSERGQAEEElikarnQARLEEQHRLahleEKIRLLAQARDEAQGTCVQQKQmvAESQARVSQL 540
Cdd:pfam02029 215 EVTKLKVTTKRRQGGLSQSQEREEEA------EVFLEAEQKL----EELRRRRQEKESEEFEKLRQKQ--QEAELELEEL 282
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 266456389 541 NLQME--------GQQRRLEELQQELINKDQEK---VAEVARVRVELQEQMGRMQADLVAQE 591
Cdd:pfam02029 283 KKKREerrklleeEEQRRKQEEAERKLREEEEKrrmKEEIERRRAEAAEKRQKLPEDSSSEG 344
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
448-645 |
1.42e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 448 ERAMQERVQRLEALRLSLEEELSRMKAAVLsergQAEEELikarnqARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQK 527
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE----EAEAAL------EEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 528 QMVAESQARVSQLNLQMEGQQRRLEELQQELINkdQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAALERQMKvi 607
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQSPVI--QQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ-- 308
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 266456389 608 gSEHREALLDRESEN-------ASLREKLRLKEAEISRIRDEEAQ 645
Cdd:COG3206 309 -QEAQRILASLEAELealqareASLQAQLAQLEARLAELPELEAE 352
|
|
| LRR |
COG4886 |
Leucine-rich repeat (LRR) protein [Transcription]; |
60-227 |
1.63e-03 |
|
Leucine-rich repeat (LRR) protein [Transcription];
Pssm-ID: 443914 [Multi-domain] Cd Length: 414 Bit Score: 41.46 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 60 LKELVLSDCMLSEegstlLFQGLCANTSVQHLDLKGNNLraTGAEALGKLlrqnKSIQSLTLEWNNLGTWEDafatfcgg 139
Cdd:COG4886 207 LEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQL--TDLPELGNL----TNLEELDLSNNQLTDLPP-------- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 140 LAANSALRQLDLRNNQISHKGAEELALALKGNTTLQQLDLRWNNIGLLGGRALVNCLPSNRTLWKLDLAGNNIPGDILRA 219
Cdd:COG4886 268 LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLL 347
|
....*...
gi 266456389 220 VEQAMDHN 227
Cdd:COG4886 348 ALLTLLLL 355
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
341-476 |
1.76e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 341 EKERKLERQEAADRESKLLRDLSAASEKNLLLRSQVDELERKARSQQEQlfLTKQELTNTSAELKIRAIQAEERLDVEKR 420
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAE--LEEKDERIERLERELSEARSEERREIRKD 464
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 266456389 421 RAKQNMEdleklhsKEVDHMTRHLEESERAMQERVQRLEALRLSLEEELSRMKAAV 476
Cdd:COG2433 465 REISRLD-------REIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPV 513
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
234-643 |
2.31e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 234 FRENQARTKILSKEVQHLQEEKSKQFLDLMETIDK--------------QREEMARDSRASAVRVGQLQEalnERQSIIN 299
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKmilafeelrvqaenARLEMHFKLKEDHEKIQHLEE---EYKKEIN 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 300 ALKAKLQMTEAALALSEQKVRDLGELLvagDQERQSLSQRHEK-----ERKLERQEAADRESKLLRDLSAASEKNLLLRS 374
Cdd:pfam05483 237 DKEKQVSLLLIQITEKENKMKDLTFLL---EESRDKANQLEEKtklqdENLKELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 375 QVDE-----------LERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNmEDLEKLHSKEVDHMTRH 443
Cdd:pfam05483 314 ALEEdlqiatkticqLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN-EDQLKIITMELQKKSSE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 444 LEESERAMQERVQRLEALRLSLEEELSRM----KAAVLSERGQAEEELIKARNQARLEEQHRLahleeKIRLLAQARDEa 519
Cdd:pfam05483 393 LEEMTKFKNNKEVELEELKKILAEDEKLLdekkQFEKIAEELKGKEQELIFLLQAREKEIHDL-----EIQLTAIKTSE- 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 520 QGTCVQQKQMVAESQARVSQlNLQMEGQQRRLEELQQELINKDQEKVAEVARVRVELQEQMGRMQADLVAQEALREKVAA 599
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLK-NIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN 545
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 266456389 600 LERQMKVIGSEHRE------ALLDRESENASLREKLRLKEAEISRIRDEE 643
Cdd:pfam05483 546 LRDELESVREEFIQkgdevkCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
286-480 |
2.72e-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: 40.52 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 286 QLQEALNERQSIINALKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQR----HEKERKLERQEAADRE--SKLL 359
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElaelEKEIAELRAELEAQKEelAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 360 RDL---SAASEKNLLLRSQ-----------VDELERKARSQQEQLFLTKQELTNTSAELKiraiQAEERLDVEKRRAKQN 425
Cdd:COG4942 111 RALyrlGRQPPLALLLSPEdfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELE----AERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 266456389 426 MEDLEKLHSKEVDHMTRhLEESERAMQERVQRLEALRLSLEEELSRMKAAVLSER 480
Cdd:COG4942 187 RAALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
506-657 |
3.07e-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: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 506 EEKIRLLAQARDEAQgtcvqqkQMVAESQARVSQLNLQMEGQQRRLEELQQ-ELINKDQEKVAEVARVRVELQEQMGRMQ 584
Cdd:COG4913 609 RAKLAALEAELAELE-------EELAEAEERLEALEAELDALQERREALQRlAEYSWDEIDVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 266456389 585 ADLVAQEALREKVAALERQMKvigsEHREALLDRESENASLREKLRLKEAEISRIRDEEAQRASFLQNAVLAY 657
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELE----ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
235-478 |
3.12e-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: 40.52 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 235 RENQARTKILSKEVQHLQEEKSKQfldlmetiDKQREEMARDSRASAVRVGQLQEALNERQSIINALKAKLQMTEAALAL 314
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAAL--------KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 315 SEQKVRDLGELLVAGDQERQSLSQRHEKERKLERQEAAD--RESKLLRDLSAASEKNLL-LRSQVDELERKARSQQEQlf 391
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavRRLQYLKYLAPARREQAEeLRADLAELAALRAELEAE-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 392 ltKQELTNTSAELKiraiQAEERLDVEKRRAKQNMEDLEKLHSKEvdhmtrhlEESERAMQERVQRLEALRLSLEEELSR 471
Cdd:COG4942 173 --RAELEALLAELE----EERAALEALKAERQKLLARLEKELAEL--------AAELAELQQEAEELEALIARLEAEAAA 238
|
....*..
gi 266456389 472 MKAAVLS 478
Cdd:COG4942 239 AAERTPA 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
372-574 |
5.94e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 372 LRSQVDELERKARSQQEQL--FLTKQELTNTSAELKIRAIQAEE------RLDVEKRRAKQNMEDLEKLHSKEVDHMTRH 443
Cdd:COG3206 180 LEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSElesqlaEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 444 LEESerAMQERVQRLEALRLSLEEELSRMKA------AVLSERGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARD 517
Cdd:COG3206 260 LQSP--VIQQLRAQLAELEAELAELSARYTPnhpdviALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 266456389 518 EAQgtcvQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINKDQEKVAEVARVRV 574
Cdd:COG3206 338 QLE----ARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
400-571 |
6.13e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 400 TSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLhskevdhmtrhLEESERAMQERVQRLEALRLSLEEELSRMKAAVLSE 479
Cdd:COG0542 398 AAARVRMEIDSKPEELDELERRLEQLEIEKEAL-----------KKEQDEASFERLAELRDELAELEEELEALKARWEAE 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 480 RGQAEEELikaRNQARLEEQHRLAHLEEKIRLLAQARDEAQGTCVQQ---KQMVAESQAR-----VSQLnlqMEGQQRRL 551
Cdd:COG0542 467 KELIEEIQ---ELKEELEQRYGKIPELEKELAELEEELAELAPLLREevtEEDIAEVVSRwtgipVGKL---LEGEREKL 540
|
170 180
....*....|....*....|....
gi 266456389 552 ----EELQQELINKDqEKVAEVAR 571
Cdd:COG0542 541 lnleEELHERVIGQD-EAVEAVAD 563
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
403-522 |
6.64e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 403 ELKIRAIQA---EERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQERVQRLEALRLSLEEELSRMKAAVlsE 479
Cdd:COG2433 367 EVKARVIRGlsiEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI--E 444
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 266456389 480 RGQAEEELIKARNQARLEEQHRLAHLEEKIRLLAQARDEAQGT 522
Cdd:COG2433 445 RLERELSEARSEERREIRKDREISRLDREIERLERELEEERER 487
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
268-645 |
7.68e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 268 KQREEMARDSRASAVRVGQLQEALNERQSiinaLKAKLQMTEAALALSEQKVRDLGELLVAGDQERQSLSQRHEKERKLE 347
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 348 RQEAADRESKLLRDLsaaseknlllRSQVDELERKARSQQEQLFLTKQELTNTSAELKIRAIQAEERLDVEKRRAKQNME 427
Cdd:COG4717 147 RLEELEERLEELREL----------EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 428 DL-EKLHSKEVDHMTRHLEESERAMQERVQRLEALRLSL--------------EEELSRMKAAVLSERGQAEEELIKARN 492
Cdd:COG4717 217 EAqEELEELEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllSLILTIAGVLFLVLGLLALLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 493 QARLEEQHRLAHLEEKIRLLAQAR-----DEAQGTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELINkdQEKVA 567
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEEleellAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE--QEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 568 EVARVRVELQEQMGRMQADLVAQEALREKVAALERQMKVIGSEHREALLDRESEN-----ASLREKLRLKEAEISRIRDE 642
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleeelEELEEELEELEEELEELREE 454
|
...
gi 266456389 643 EAQ 645
Cdd:COG4717 455 LAE 457
|
|
| PPP1R42 |
cd21340 |
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ... |
54-159 |
8.43e-03 |
|
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.
Pssm-ID: 411060 [Multi-domain] Cd Length: 220 Bit Score: 38.23 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 54 LHKETLLKELVLSDCMLsEEGSTLLFQGLCANT---SVQHLDLKGNNLRATgaEALGKLlrqnKSIQSLTLEWNNLGTWE 130
Cdd:cd21340 86 LENLTNLEELHIENQRL-PPGEKLTFDPRSLAAlsnSLRVLNISGNNIDSL--EPLAPL----RNLEQLDASNNQISDLE 158
|
90 100
....*....|....*....|....*....
gi 266456389 131 DAFATfcggLAANSALRQLDLRNNQISHK 159
Cdd:cd21340 159 ELLDL----LSSWPSLRELDLTGNPVCKK 183
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
347-560 |
8.66e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 38.59 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 347 ERQEAADRESKLLRDLSAASEKNLLLrsqvDELERKARSQQEQLFLTKQELTNTSAELKiraiQAEERLDVEKRRAKQNM 426
Cdd:pfam09787 24 EKLIASLKEGSGVEGLDSSTALTLEL----EELRQERDLLREEIQKLRGQIQQLRTELQ----ELEAQQQEEAESSREQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 427 EDLEKLHSKEvdhmtrhlEESERAMQERVQRLEALRLSLEEELSRMKAAVLSERGQAEEELIKARNQARLEEQHRL--AH 504
Cdd:pfam09787 96 QELEEQLATE--------RSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSsqSE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 266456389 505 LEEKIRLLAQardeaqgTCVQQKQMVAESQARVSQLNLQMEGQQRRLEELQQELIN 560
Cdd:pfam09787 168 LENRLHQLTE-------TLIQKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSN 216
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
236-558 |
9.89e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.40 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 236 ENQARTKILSKEVQHLQEEKskqfLDLMETIDKQREEMARDSRASavrvgqlQEALNERQsiinALKAKLQMTEAALALS 315
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEG----AALRGQLDALTKQLQRDESEA-------QSLRQEEQ----ALTQQWQAVCASLNIT 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 316 EQKVRDLGELLVAGDQERQSL---SQRHEKERKLERQEA---------ADRESKLLRDLSAAS-------EKNLLLRSQV 376
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLrllSQRHELQGQIAAHNQqiiqyqqqiEQRQQQLLTALAGYAltlpqedEEASWLATRQ 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 377 DELERKARSQQEQLFLTKQ--ELTNTSAELKIRAIQAEERLDVEKRRAKQNMEDLEKLHSKEVDHMTRHLEESERAMQER 454
Cdd:PRK10246 672 QEAQSWQQRQNELTALQNRiqQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQ 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 266456389 455 VQRLEALRLSLEEELSRMKAAVLSERGQAEEELIKARNQARLEEQHRLAhleEKIRLLAQARDEAQGTCVQQKQMVAESQ 534
Cdd:PRK10246 752 AQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLV---TQTAQALAQHQQHRPDGLDLTVTVEQIQ 828
|
330 340
....*....|....*....|....
gi 266456389 535 ARVSQLNLQMEGQQRRLEELQQEL 558
Cdd:PRK10246 829 QELAQLAQQLRENTTRQGEIRQQL 852
|
|
| |
