|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
292-557 |
3.16e-121 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 361.71 E-value: 3.16e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 292 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRESLSEVEEKYKKAMVSN 362
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 363 AQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEKHGLVIIPD 442
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIEKHGLVIVPD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 443 GTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ-KCSRNDGTVGDLAG 521
Cdd:pfam09738 190 ENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTRSSQSPDGFG 269
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462593715 522 LQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDITT 557
Cdd:pfam09738 270 LENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
379-632 |
1.50e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 379 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMEELKEGLRQRDELIEKHglviipdgtpngdv 449
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEEL-------------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 450 shepvagAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQ 529
Cdd:COG1196 252 -------EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 530 FIEMQR---DANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEE 606
Cdd:COG1196 325 LAELEEeleELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260
....*....|....*....|....*.
gi 2462593715 607 MEMTNSHLAKRLEKMKANRTALLAQQ 632
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEAL 430
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
372-632 |
2.29e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 372 LIYQVDTLKDVIEEQEEQMAEfyRENEEKSKELERQKhmcsvLQHKMEELKEGLRQRDELIEKHGlviipdgtpngdvsh 451
Cdd:COG1196 230 LLLKLRELEAELEELEAELEE--LEAELEELEAELAE-----LEAELEELRLELEELELELEEAQ--------------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 452 epvaGAITVVSQEAAQvlESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlQFI 531
Cdd:COG1196 288 ----AEEYELLAELAR--LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE----EAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 532 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTN 611
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260
....*....|....*....|.
gi 2462593715 612 SHLAKRLEKMKANRTALLAQQ 632
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEE 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
326-631 |
3.47e-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: 53.52 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 326 RGSGDT-SSLIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 404
Cdd:TIGR02168 663 GGSAKTnSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 405 ERQKHMCSVLQHKMEELKEGLRQRDELIEKHGLVIipdgtpngdvshEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKL 484
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEEL------------AEAEAEIEELEAQIEQLKEELKA--LREALDEL 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 485 AGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglQNGSDLQfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISR 564
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLE--EQIEELS--EDIESLAAEIEELEELIEELESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593715 565 LEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMtnshlakRLEKMKANRTALLAQ 631
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL-------RLEGLEVRIDNLQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-607 |
1.24e-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: 51.98 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 334 LIDPDTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSV 413
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 414 LQHKMEELKEGLRQRDELIEKhglviipdgTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGEKEELLS 493
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAAN---------LRERLESLERRIAATERRLEDLEEQIEELSE-----DIESLAAEIEELEE 866
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 494 QIRKLKLQLEE-ERQKCSRNDGTVGDLAGLQN-GSDLQFIEMQR-DANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL 570
Cdd:TIGR02168 867 LIEELESELEAlLNERASLEEALALLRSELEElSEELRELESKRsELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462593715 571 -RYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEM 607
Cdd:TIGR02168 947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
477-631 |
2.02e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 477 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 551
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 552 -----EQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEmtnSHLAKRLEKMKANRT 626
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 2462593715 627 ALLAQ 631
Cdd:COG1579 167 ELAAK 171
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-632 |
2.72e-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: 50.83 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 340 SLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERqkhmcsvLQHKME 419
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 420 ELKEGLRQRDELIEKHGLVIIPDGTPNGDVSHEpvAGAITVVSQEAAQVLESAGEgpldvRLRKLAGEKEELLSQIRKLK 499
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEE--LAELEEKLEELKEELESLEA-----ELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 500 LQLEEERQKcsrndgtvgdLAGLQNGSDLQFIEMQRdANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA 579
Cdd:TIGR02168 379 EQLETLRSK----------VAQLELQIASLNNEIER-LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462593715 580 EkvEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 632
Cdd:TIGR02168 448 E--LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-632 |
6.23e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 341 LSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM----AEFYRENEEKSKELERQKHmcsvLQH 416
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRE----LEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 417 KMEELKEglrQRDELIEKHglviipdgtpngdvshepvagaitvvsQEAAQVLESAGEgpldvRLRKLAGEKEELLSQIR 496
Cdd:COG1196 317 RLEELEE---ELAELEEEL---------------------------EELEEELEELEE-----ELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 497 KLKLQLEEERQKcsrndgtvgdlAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAA 576
Cdd:COG1196 362 EAEEALLEAEAE-----------LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462593715 577 ENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 632
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
383-620 |
1.76e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 383 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEKHGLViipdgtpngdvshEPVAGAITVVS 462
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQF-------------EKIAEELKGKE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 463 QEAAQVLESAGE--GPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRndgtvgdlagLQNGSDLQFIEmQRDANRQ 540
Cdd:pfam05483 439 QELIFLLQAREKeiHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE----------LTAHCDKLLLE-NKELTQE 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 541 ISEYKFKLSKAEQDITTLEQSISRLEGQVlryKTAAENAEKVEDELKAEKRKLQR---ELRTALDKIEEMEMTNSHLAKR 617
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQI---ENLEEKEMNLRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLK 584
|
...
gi 2462593715 618 LEK 620
Cdd:pfam05483 585 KEK 587
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
364-632 |
1.82e-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: 48.13 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 364 QLDNEKNNLiyqvDTLKDVIEEQEEQM---------AEFYRENEEKSKELERqkhmcSVLQHKMEELKEGLRQRDELIEK 434
Cdd:TIGR02168 180 KLERTRENL----DRLEDILNELERQLkslerqaekAERYKELKAELRELEL-----ALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 435 HGlviipdgtpngdVSHEPVAGAITVvSQEAAQVLESAgEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrndg 514
Cdd:TIGR02168 251 AE------------EELEELTAELQE-LEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQILRER------ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 515 tvgdLAGLQNgsDLQFIEMQRDAN-RQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKL 593
Cdd:TIGR02168 311 ----LANLER--QLEELEAQLEELeSKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2462593715 594 QRELRTALDK-------IEEMEMTNSHLAKRLEKMKANRTALLAQQ 632
Cdd:TIGR02168 385 RSKVAQLELQiaslnneIERLEARLERLEDRRERLQQEIEELLKKL 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
477-623 |
3.25e-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: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 477 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCsrnDGTVGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 555
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462593715 556 TTLEQSI-----------SRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 623
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
332-608 |
4.24e-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: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 332 SSLIDPDTSLSELRESLSEVEEKYK--KAMVSNAQLDNEKNnliyQVDTLKDVIEEQEEQMAEFyrENEEKSKELERQkh 409
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNdlEARLSHSRIPEIQA----ELSKLEEEVSRIEARLREI--EQKLNRLTLEKE-- 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 410 mcsVLQHKMEELKEGLRQRDELIEKHGLVIipdgtpngDVSHEPVAGAITVVSQEAAQVLEsagegpLDVRLRKLAGEKE 489
Cdd:TIGR02169 830 ---YLEKEIQELQEQRIDLKEQIKSIEKEI--------ENLNGKKEELEEELEELEAALRD------LESRLGDLKKERD 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 490 ELLSQIRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLE 566
Cdd:TIGR02169 893 ELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALE 971
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462593715 567 GQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 608
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-608 |
6.62e-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: 46.20 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 338 DTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNL-----IYQV--DTLKDVIEEQEEQMAEFYRENEEKSKELERQKHM 410
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkqILRErlANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 411 CSVLQHKMEELKEglrqrdELIEKHglviipdgtpngdvshepvagaitvvsqEAAQVLESAGEGpLDVRLRKLAGEKEE 490
Cdd:TIGR02168 346 LEELKEELESLEA------ELEELE----------------------------AELEELESRLEE-LEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 491 LLSQIRKLKLQLEEERQKCSRNDGTVGdlaglqngsdlQFIEMQRDANRQISEYKFKLSKAEqdITTLEQSISRLEGQVL 570
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRE-----------RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELE 457
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462593715 571 RYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 608
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
340-579 |
1.08e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 340 SLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKME 419
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 420 ELKEGLRQRDELIEKHG-----LVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGEKEELLSQ 494
Cdd:COG4942 101 AQKEELAELLRALYRLGrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 495 IRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKT 574
Cdd:COG4942 176 LEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....*
gi 2462593715 575 AAENA 579
Cdd:COG4942 242 RTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
477-631 |
1.21e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 477 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNdGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQDIT 556
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------REQAE 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462593715 557 TLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 631
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
375-606 |
1.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 375 QVDTLKDVIEEQEEqmaefYRENEEKSKELERQKHMCSV--LQHKMEELKEGLRQRDELIEKHglviipdgtpngdvshe 452
Cdd:COG4913 250 QIELLEPIRELAER-----YAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARL----------------- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 453 pvAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGE-KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFI 531
Cdd:COG4913 308 --EAELERLEARLDALREELDE--LEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 532 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQvlryktaaenAEKVEDELKA-EKRK---------LQRELRTAL 601
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE----------LRELEAEIASlERRKsniparllaLRDALAEAL 453
|
....*
gi 2462593715 602 DKIEE 606
Cdd:COG4913 454 GLDEA 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-607 |
1.35e-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: 45.05 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 341 LSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLkdviEEQEEQMAEFYRENEEKSKELERQKHMCsvlQHKMEE 420
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL----RAELTLLNEEAANLRERLESLERRIAAT---ERRLED 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 421 LKEGLRQRDELIEKHGLVIiPDGTPNGDVSHEPVAGAITVV-SQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLK 499
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEI-EELEELIEELESELEALLNERaSLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 500 LQLEEERQKCSRNDGTVGDLagLQNGSDLQFIEMQrDANRQISEYKFKLSKAEQDITTLEQSISRLeGQV-LRYKTAAEN 578
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNL--QERLSEEYSLTLE-EAEALENKIEDDEEEARRRLKRLENKIKEL-GPVnLAAIEEYEE 997
|
250 260
....*....|....*....|....*....
gi 2462593715 579 AEKVEDELKAEKRKLQRELRTALDKIEEM 607
Cdd:TIGR02168 998 LKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
349-632 |
1.49e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 349 SEVEEKYKKAMVSNAQLDNEKNnliyQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL----QHKMEELKEG 424
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNK----IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLkkenQSYKQEIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 425 LRQRDELIEKhglviipdgtpngdvshepvagaITVVSQEAAQvlesagegpLDVRLRKLAGEKEELLSQIRKLKLQLEE 504
Cdd:TIGR04523 390 ESQINDLESK-----------------------IQNQEKLNQQ---------KDEQIKKLQQEKELLEKEIERLKETIIK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 505 ERQKCSR--NDGTVGDLAGLQNGSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTLEQSI-------SRLEGQVLRYKT 574
Cdd:TIGR04523 438 NNSEIKDltNQDSVKELIIKNLDNTRESLETQLKVlSRSINKIKQNLEQKQKELKSKEKELkklneekKELEEKVKDLTK 517
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593715 575 AAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTN---------SHLAKRLEKMKANRTALLAQQ 632
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTQKSLKKKQ 584
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
341-625 |
1.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 341 LSELRESLSEVEEKYKKAMVSNAQLDNEKNNL--IYQVDTLKDVIEEQEEQMAEFYREN-EEKSKELERQKHMCSVLQHK 417
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 418 MEELKEGLRQRDELIEKHGLVIIpdgtpngdvshepvagaitvvsqeaaqvlesagegpldvRLRKLAGEKEELLSQIRK 497
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEK---------------------------------------KLDELEEELAELLKELEE 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 498 LKLQLEEErqkcsrNDGTVGDLAGLQNgsdlQFIEMqRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAE 577
Cdd:PRK03918 582 LGFESVEE------LEERLKELEPFYN----EYLEL-KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462593715 578 NAEKVEDE-----LKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANR 625
Cdd:PRK03918 651 ELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
348-622 |
3.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 348 LSEVEEKYKKAMVSNAQLDNEKNNL---IYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKE- 423
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEl 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 424 -----GLRQRDELIEKHgLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKL 498
Cdd:PRK03918 237 keeieELEKELESLEGS-KRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 499 KLQLEEERQKCSRNdgtvgdlaglqngsdlqfIEMQRDANRQISEYKFKLSKAEQDITTLE------QSISRLEGQVLRY 572
Cdd:PRK03918 316 LSRLEEEINGIEER------------------IKELEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERL 377
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462593715 573 KT--AAENAEKVEDELK-AEKRK--LQRELRTALDKIEEMEMTNSHLAKRLEKMK 622
Cdd:PRK03918 378 KKrlTGLTPEKLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
365-596 |
3.67e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 365 LDNEKNNLIYQVDTLKDVIEEQEEQMAEfyreneekskELERQKHMCSVLQHKMEELKEGLRQRDELIEKHglviipdgt 444
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGE----------NIARKQNKYDELVEEAKTIKAEIEELTDELLNL--------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 445 pngDVSHEPVAGAITVVSQEAAQV-------------LESAGEGPL--------DVRLRKLAGEKEELLSQIRKLKLQLE 503
Cdd:PHA02562 247 ---VMDIEDPSAALNKLNTAAAKIkskieqfqkvikmYEKGGVCPTctqqisegPDRITKIKDKLKELQHSLEKLDTAID 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 504 EERQKcsrndgtVGDLAGLQNgsdlqfieMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVE 583
Cdd:PHA02562 324 ELEEI-------MDEFNEQSK--------KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDEL 388
|
250
....*....|...
gi 2462593715 584 DELKAEKRKLQRE 596
Cdd:PHA02562 389 DKIVKTKSELVKE 401
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
334-632 |
4.16e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 334 LIDPDTSLSELRESLSEVEEKYkkamvsnAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSV 413
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQI-------SQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 414 LQHKMEELKEGLRQRDELIEKHglviipdgtpngDVSHEPVAGAITVVSQEAAQV------LESAgEGPLDVRLRKLAGE 487
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKL------------QQEKELLEKEIERLKETIIKNnseikdLTNQ-DSVKELIIKNLDNT 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 488 KEELLSQIRKLKLQLEEERQKCSRN----DGTVGDLAGL-QNGSDLQfiEMQRDANRQISEYKFKLSKAEQDITTLEQSI 562
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKqkelKSKEKELKKLnEEKKELE--EKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 563 SRLEGQVLRYKTaaenaEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 632
Cdd:TIGR04523 541 SDLEDELNKDDF-----ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
480-625 |
4.21e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 480 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 552
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462593715 553 QDITTLEQSISRLEGQVLRYKTAAENAEKvedELKAEKRKLQRELRTALDKIEEmemtnsHLAKRLEKMKANR 625
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
340-423 |
5.04e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.41 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 340 SLSELRESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKME 419
Cdd:COG4026 129 EYNELREELLELKEKID-------EIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFE 201
|
....
gi 2462593715 420 ELKE 423
Cdd:COG4026 202 ELLK 205
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
532-623 |
5.29e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 532 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 598
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462593715 599 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 623
Cdd:COG2433 463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
341-602 |
5.87e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 341 LSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEfyrENEEKSKELERQKHMCSVLQHKMEE 420
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE---LEEELEEAEEELEEAEAELAEAEEA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 421 LKEGLRQRDELIEKHglviipdgtpngdvshepVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKL 500
Cdd:COG1196 367 LLEAEAELAEAEEEL------------------EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 501 QLEEERQKCSRNDGTVGDLAGLQNGSDLQfiemQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAE 580
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
250 260
....*....|....*....|...
gi 2462593715 581 -KVEDELKAEKRKLQRELRTALD 602
Cdd:COG1196 505 gFLEGVKAALLLAGLRGLAGAVA 527
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
341-628 |
2.18e-03 |
|
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: 41.21 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 341 LSELRESLSEVEEKYKKamvsNAQLDNEKNNLIYQVDtlKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 420
Cdd:TIGR02169 246 LASLEEELEKLTEEISE----LEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 421 LKEGLRQRDELIEKHglviipdgtpngDVSHEPVAGAITVVSQEAAQVLEsagegpldvRLRKLAGEKEELLSQIRKLKL 500
Cdd:TIGR02169 320 AEERLAKLEAEIDKL------------LAEIEELEREIEEERKRRDKLTE---------EYAELKEELEDLRAELEEVDK 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 501 QLEEERQKCSRndgTVGDLAGLQNGSDlqfiEMQRDANRQISEykfkLSKAEQDITTLEQSISRLEGQVLRYKTAAENA- 579
Cdd:TIGR02169 379 EFAETRDELKD---YREKLEKLKREIN----ELKRELDRLQEE----LQRLSEELADLNAAIAGIEAKINELEEEKEDKa 447
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2462593715 580 ---EKVEDELK---AEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTAL 628
Cdd:TIGR02169 448 leiKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
477-632 |
2.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 477 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCS-------RNDGTVGDLAGLQNGSDLQ-FIE-------MQRDANRQI 541
Cdd:COG3883 56 LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSdFLDrlsalskIADADADLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 542 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 621
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
170
....*....|.
gi 2462593715 622 KANRTALLAQQ 632
Cdd:COG3883 216 AAAAAAAAAAA 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
375-601 |
2.68e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 375 QVDTLKDVIEEQEEQMAEfYRENEEKSKELERQKHMcsvLQHKMEELKEGLRQRDELIEKHglviipdgtpngdvshepv 454
Cdd:COG4717 72 ELKELEEELKEAEEKEEE-YAELQEELEELEEELEE---LEAELEELREELEKLEKLLQLL------------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 455 agaitvvsqeaaqvlesagegPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQ 534
Cdd:COG4717 129 ---------------------PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593715 535 RDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKvEDELKAEKRKLQRELRTAL 601
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLL 253
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
338-588 |
2.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 338 DTSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcsvlqhk 417
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 418 mEELKEGLR--QRdeliekhglviipDGTPNGDVShepvagaITVVSQEAAQVLESAgegpldVRLRKLAGEKEELLSQI 495
Cdd:COG3883 86 -EELGERARalYR-------------SGGSVSYLD-------VLLGSESFSDFLDRL------SALSKIADADADLLEEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 496 RKLKLQLEEERQKcsrNDGTVGDLAGLQNgsDLQfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTA 575
Cdd:COG3883 139 KADKAELEAKKAE---LEAKLAELEALKA--ELE--AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
250
....*....|...
gi 2462593715 576 AENAEKVEDELKA 588
Cdd:COG3883 212 AAAAAAAAAAAAA 224
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
341-622 |
3.18e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 341 LSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN---EEKSKELERqkhmcsvLQHK 417
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIER-------LEWR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 418 MEELKEGLRQRDELIEKhglviipdgtpngdvshepvagaITVVSQEAAQVLEsagegpldvrLRKLAGEKEELLSQIRK 497
Cdd:COG1340 125 QQTEVLSPEEEKELVEK-----------------------IKELEKELEKAKK----------ALEKNEKLKELRAELKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 498 LKLQLEEERQKcsrndgtVGDLAGlqngsdlqfiemqrdanrQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAE 577
Cdd:COG1340 172 LRKEAEEIHKK-------IKELAE------------------EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2462593715 578 NAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNShlAKRLEKMK 622
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKE--KEELEEKA 269
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
480-632 |
3.45e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 480 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVgdlagLQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDITTL 558
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEEL-----EQARSELEQLEEElEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462593715 559 EQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 632
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
375-629 |
5.12e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 375 QVDTLKDVIEEQEEQMAEFYRENEE----KSKELERQKhMCSVLQHKMEELKEGL-RQRDELIEKHGLVIIPDGTPNGDV 449
Cdd:TIGR00606 246 ELDPLKNRLKEIEHNLSKIMKLDNEikalKSRKKQMEK-DNSELELKMEKVFQGTdEQLNDLYHNHQRTVREKERELVDC 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 450 SHEpvagaITVVSQEAaqvlesagegpldvrlRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLaglQNGSDLQ 529
Cdd:TIGR00606 325 QRE-----LEKLNKER----------------RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSL---ATRLELD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 530 FIEMQRDANRQISEY-KFKLSKAEQDITTLEQSISRLEGQVlryKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 608
Cdd:TIGR00606 381 GFERGPFSERQIKNFhTLVIERQEDEAKTAAQLCADLQSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK 457
|
250 260
....*....|....*....|.
gi 2462593715 609 mtnsHLAKRLEKMKANRTALL 629
Cdd:TIGR00606 458 ----FVIKELQQLEGSSDRIL 474
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
383-623 |
5.96e-03 |
|
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: 40.05 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 383 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEKHG---LVIIPDGTPNGDVSHEPVAGAIT 459
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGeeeQLRVKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 460 VVSQEAAQvlesagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQkcsRNDGTVGDLAGLQNGSDLQFIEMQ----- 534
Cdd:TIGR02169 312 EKERELED---------AEERLAKLEAEIDKLLAEIEELEREIEEERK---RRDKLTEEYAELKEELEDLRAELEevdke 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 535 -RDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSH 613
Cdd:TIGR02169 380 fAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQ 459
|
250
....*....|
gi 2462593715 614 LAKRLEKMKA 623
Cdd:TIGR02169 460 LAADLSKYEQ 469
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
484-628 |
7.56e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 38.89 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 484 LAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglQNGSDLQfiemqrDANRQISEYKFKLSKAEQ----DITTLE 559
Cdd:pfam15742 81 LTAEWKHCQQKIRELELEVLKQAQSIKSQNSLQEKLA--QEKSRVA------DAEEKILELQQKLEHAHKvcltDTCILE 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462593715 560 QSisRLEGQVlryKTAAENAEKVEDELKAE--KRK--------LQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTAL 628
Cdd:pfam15742 153 KK--QLEERI---KEASENEAKLKQQYQEEqqKRKlldqnvneLQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQL 226
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
339-597 |
7.89e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.11 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 339 TSLSELRESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcsvlqhkm 418
Cdd:pfam07888 87 EELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMK---------- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 419 EELKEGLRQR-DELIEKHGLVIIPDGTPNGDVS-HEPVAGAITVVSQEAAQVLE-----SAGEGPLDVRLRKLAgEKEEL 491
Cdd:pfam07888 157 ERAKKAGAQRkEEEAERKQLQAKLQQTEEELRSlSKEFQELRNSLAQRDTQVLQlqdtiTTLTQKLTTAHRKEA-ENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593715 492 LSQIRKLKLQLEEERQKCsrnDGTVGDLAGLQNGSDLQFIEMQRdANRQISEYKFKLSKA-----------EQDITTLEQ 560
Cdd:pfam07888 236 LEELRSLQERLNASERKV---EGLGEELSSMAAQRDRTQAELHQ-ARLQAAQLTLQLADAslalregrarwAQERETLQQ 311
|
250 260 270
....*....|....*....|....*....|....*..
gi 2462593715 561 SISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQREL 597
Cdd:pfam07888 312 SAEADKDRIEKLSAELQRLEERLQEERMEREKLEVEL 348
|
|
| |
