|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
292-615 |
7.50e-108 |
|
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: 328.96 E-value: 7.50e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 292 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqiqdvegrym 362
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 363 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 442
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 443 EELKEGLRQRDELIEalekqkeyiaclrnerdmlreeladlqetvktgeKHGLVIIPDGTPNGDVSHEPVAGAITVVSQE 522
Cdd:pfam09738 166 AELKEQLKQRDELIE----------------------------------KHGLVIVPDENTNGEEENSPADAKRALVSVE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 523 AAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ-KCSRNDGTVGDLAGLQNGSDLqfIEMQRDANRQISE 601
Cdd:pfam09738 212 AAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTRSSQSPDGFGLENGSHV--IEVQREANKQISD 289
|
330
....*....|....
gi 2462593701 602 YKFKLSKAEQDITT 615
Cdd:pfam09738 290 YKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
326-665 |
8.02e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 326 RGSGDT-SSLIDPDTSLSELR-DIYDLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTL 403
Cdd:TIGR02168 663 GGSAKTnSSILERRREIEELEeKIEELEEKIAELE----KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 404 KDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELI----EALEKQKEYIACLRNERDMLREE 479
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIeqlkEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 480 LADLQETVKTGEKhglviipdgtpngdvSHEPVAGAITVVSQEAAQVLEsagegpldvRLRKLAGEKEELLSQIRKLKLQ 559
Cdd:TIGR02168 819 AANLRERLESLER---------------RIAATERRLEDLEEQIEELSE---------DIESLAAEIEELEELIEELESE 874
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 560 LEE-ERQKCSRNDGTVGDLAGLQN-GSDLQFIEMQR-DANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL-RYKTAAE 635
Cdd:TIGR02168 875 LEAlLNERASLEEALALLRSELEElSEELRELESKRsELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLE 954
|
330 340 350
....*....|....*....|....*....|
gi 2462593701 636 NAEKVEDELKAEKRKLQRELRTALDKIEEM 665
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
349-666 |
3.67e-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: 63.54 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 349 DLKDQIQDVEGR-YMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKE 427
Cdd:TIGR02168 217 ELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 428 LERQKHMCSVLQHKM-----------EELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVktgekhglv 496
Cdd:TIGR02168 297 ISRLEQQKQILRERLanlerqleeleAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 497 iipdgtpngdvshepvagaitvvsqeaaQVLESAGEGpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGd 576
Cdd:TIGR02168 368 ----------------------------EELESRLEE-LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE- 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 577 laglqngsdlQFIEMQRDANRQISEYKFKLSKAEqdITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELR 656
Cdd:TIGR02168 418 ----------RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330
....*....|
gi 2462593701 657 TALDKIEEME 666
Cdd:TIGR02168 486 QLQARLDSLE 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
322-666 |
1.62e-09 |
|
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: 61.24 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 322 NSSRRGSGDTSSliDPDTSLSELRDIYDLKDQ---IQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIY 398
Cdd:TIGR02169 660 RAPRGGILFSRS--EPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 399 QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQR--DELIEALEKQKEYIACLRNERDML 476
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSriPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 477 REELADLQETVKTGEK---HGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGE-GPLDVRLRKLAGEKEELLSQ 552
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKeiqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 553 IRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLR 629
Cdd:TIGR02169 898 LRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNML 976
|
330 340 350
....*....|....*....|....*....|....*..
gi 2462593701 630 YKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 666
Cdd:TIGR02169 977 AIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
403-690 |
2.05e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 403 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMEELKEGLRQRDELIEALEKQKEyiaCLRNER 473
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEELEAELE---ELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 474 DMLREELADLQETVktgekhglviipdgtpngdvshepvagaitvvsQEAAQVLESAGEgpldvRLRKLAGEKEELLSQI 553
Cdd:COG1196 263 AELEAELEELRLEL---------------------------------EELELELEEAQA-----EEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 554 RKLKLQLEEERQKCSRNDGTVGDLAglqngsdlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTA 633
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELE-----------EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593701 634 AENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 690
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
349-690 |
4.53e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 4.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 349 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 428
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 429 ERQKHMCSVLQHKMEELKEGLRQRDELIEALEKQKEYiacLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvs 508
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL---LEKEIERLKETIIKNNSEIKDLTN---------------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 509 hepvagaitvvsQEAAqvlesagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRN----DGTVGDLAGL-QNG 583
Cdd:TIGR04523 448 ------------QDSV----------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkelKSKEKELKKLnEEK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 584 SDLQfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTaaenaEKVEDELKAEKRKLQRELRTALDKIE 663
Cdd:TIGR04523 506 KELE--EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF-----ELKKENLEKEIDEKNKEIEELKQTQK 578
|
330 340
....*....|....*....|....*..
gi 2462593701 664 EMEMTNSHLAKRLEKMKANRTALLAQQ 690
Cdd:TIGR04523 579 SLKKKQEEKQELIDQKEKEKKDLIKEI 605
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
342-665 |
4.65e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 342 SELRDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 421
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 422 EEKSKELERQKHMCSVLQHKMEELKEGLRqrdELIEALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVI---I 498
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELT---LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 499 PDGTPNGDVSHEPVAGAITVV-SQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDL 577
Cdd:TIGR02168 862 EELEELIEELESELEALLNERaSLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 578 agLQNGSDLQFIEMQrDANRQISEYKFKLSKAEQDITTLEQSISRLeGQV-LRYKTAAENAEKVEDELKAEKRKLQRELR 656
Cdd:TIGR02168 942 --QERLSEEYSLTLE-EAEALENKIEDDEEEARRRLKRLENKIKEL-GPVnLAAIEEYEELKERYDFLTAQKEDLTEAKE 1017
|
....*....
gi 2462593701 657 TALDKIEEM 665
Cdd:TIGR02168 1018 TLEEAIEEI 1026
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
377-680 |
2.31e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 377 EKYKKAMvsnAQLDNEKNNLIYQVDTLKDVIEeQEEQMAEFYRENEeksKELERQKHMCSVLQHKMEELKEGLRQRDELI 456
Cdd:PRK03918 158 DDYENAY---KNLGEVIKEIKRRIERLEKFIK-RTENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 457 EALEKQKEYIACLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvSHEPVAGAITVVSQEAAQVLESAGEGPLD 536
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEGSKRKLEEKIRELEE---------------RIEELKKEIEELEEKVKELKELKEKAEEY 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 537 VRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNdgtvgdlaglqngsdlqfIEMQRDANRQISEYKFKLSKAEQDITTL 616
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEER------------------IKELEEKEERLEELKKKLKELEKRLEEL 357
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462593701 617 E------QSISRLEGQVLRYKT--AAENAEKVEDELK-AEKRK--LQRELRTALDKIEEMEMTNSHLAKRLEKMK 680
Cdd:PRK03918 358 EerhelyEEAKAKKEELERLKKrlTGLTPEKLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
434-689 |
4.74e-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: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 434 MCSVLQHKMEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepva 513
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR--------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 514 gAITVVSQEAAQvlesagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNdGTVGDLAGLQNGSDLQFIEMQR 593
Cdd:COG4942 70 -RIRALEQELAA---------LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 594 DANRQISEYKfklskaEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLA 673
Cdd:COG4942 139 QYLKYLAPAR------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
|
250
....*....|....*.
gi 2462593701 674 KRLEKMKANRTALLAQ 689
Cdd:COG4942 213 AELAELQQEAEELEAL 228
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-686 |
5.37e-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: 50.06 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 407 IEEQEEQMAEFYRENEEKSKELERqkhmcsvLQHKMEELKEGLRQRDELIEALEKQ----KEYIACLRNERDMLREELAD 482
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAE-------LRKELEELEEELEQLRKELEELSRQisalRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 483 LQETVKtgekhglviipdgtpngdvshepvagaitvvsqEAAQVLESagegpLDVRLRKLAGEKEELLSQIRKLKLQLEE 562
Cdd:TIGR02168 752 LSKELT---------------------------------ELEAEIEE-----LEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 563 ERQKCSRNDGTvgdLAGLQNGSDLQFIEMQRDANRqISEYKFKLSKAEQDITTLEQSISRLEGQVLRY----KTAAENAE 638
Cdd:TIGR02168 794 LKEELKALREA---LDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEELSEDIESLaaeiEELEELIE 869
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462593701 639 KVEDELKA---EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTAL 686
Cdd:TIGR02168 870 ELESELEAllnERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
389-654 |
1.02e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 389 LDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKElerqkHMCSVLQHKME--ELKEGLRqrdELIEALEKQKEYI 466
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDE-----LVEEAKTIKAEieELTDELL---NLVMDIEDPSAAL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 467 ACLRNERDMLREELADLQETVKTGEKHGlviipdgtpngdvshepvagaitvVSQEAAQVLESAGEgpldvRLRKLAGEK 546
Cdd:PHA02562 258 NKLNTAAAKIKSKIEQFQKVIKMYEKGG------------------------VCPTCTQQISEGPD-----RITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 547 EELLSQIRKLKLQLEEERQKcsrndgtVGDLAGLQNgsdlqfieMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQ 626
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEI-------MDEFNEQSK--------KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAE 373
|
250 260
....*....|....*....|....*...
gi 2462593701 627 VLRYKTAAENAEKVEDELKAEKRKLQRE 654
Cdd:PHA02562 374 FVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
365-679 |
1.10e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 444
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 445 LKEGLRQRDELIEALEKQKEYIAcLRNERDMLREELADLQETvktgekhglviipdgtpngdvshepvagaITVVSQEAA 524
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKR-----------------------------LSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 525 QVLESAGEGPLDV-RLRKLAGEKEELLSQIRKLK---LQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQIS 600
Cdd:PRK03918 325 GIEERIKELEEKEeRLEELKKKLKELEKRLEELEerhELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 601 EykfKLSKAEQDITTLEQSISRLEGQVLRYKTAAE-----NAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKR 675
Cdd:PRK03918 405 E---EISKITARIGELKKEIKELKKAIEELKKAKGkcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKE 481
|
....
gi 2462593701 676 LEKM 679
Cdd:PRK03918 482 LREL 485
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
341-480 |
2.50e-05 |
|
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: 46.07 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 341 LSELRDIYD-LKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-----VDTLKDVIEEQEEQM 414
Cdd:COG1579 33 LAELEDELAaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462593701 415 AEFYRENEEKSKELERQKhmcSVLQHKMEELKEGLRQRDELIEALEKQKEYiacLRNERDMLREEL 480
Cdd:COG1579 113 LELMERIEELEEELAELE---AELAELEAELEEKKAELDEELAELEAELEE---LEAEREELAAKI 172
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-678 |
3.16e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 342 SELRDIYDLKDQIQDVEgrymQGLKELKESLSEVEEKYKK---------AMVSNAQLDNEKNNLIYQVDTLKD---VIEE 409
Cdd:COG4717 85 EKEEEYAELQEELEELE----EELEELEAELEELREELEKlekllqllpLYQELEALEAELAELPERLEELEErleELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 410 QEEQMAEFYRENEEKSKELERQKHMCSVLQHkmEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKT 489
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATE--EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 490 GEKH--------------GLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLEsagegpLDVRLRKLAGEKEELLSQIRK 555
Cdd:COG4717 239 AALEerlkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL------LLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 556 LKlQLEEERQKcsrndgtvGDLAGLQNGSDLQfIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAE 635
Cdd:COG4717 313 LE-ELEEEELE--------ELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE 382
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2462593701 636 NAEKVED--ELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEK 678
Cdd:COG4717 383 DEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-646 |
3.40e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 345 RDIYDLKDQIQDVEGRYmqglKELKESLSEVEEKYKKaMVSNAQLdneknnliyqvdTLKDVIEEQEEQMAEFYRENEEK 424
Cdd:TIGR02169 251 EELEKLTEEISELEKRL----EEIEQLLEELNKKIKD-LGEEEQL------------RVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 425 SKELERQKhmcsvlqhkmEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKTGEKhglviipdgtpn 504
Cdd:TIGR02169 314 ERELEDAE----------ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA------------ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 505 gDVSHEPVAGAITVVSQEAAQV-LESAGE--GPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLA--- 578
Cdd:TIGR02169 372 -ELEEVDKEFAETRDELKDYREkLEKLKReiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAlei 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462593701 579 GLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKA 646
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
443-681 |
3.93e-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: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 443 EELKEGLRQRDELIEALEKQKEYIAcLRNERDMLREELADLQetvktgekhglviipdgtpngdvshepvagaiTVVSQE 522
Cdd:COG4913 242 EALEDAREQIELLEPIRELAERYAA-ARERLAELEYLRAALR--------------------------------LWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 523 AAQVLESAGEGpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGtvGDLAGLQNgsDLQFIEMQRD-ANRQISE 601
Cdd:COG4913 289 RLELLEAELEE-LRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLER--EIERLERELEeRERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 602 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAEN----AEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLE 677
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
....
gi 2462593701 678 KMKA 681
Cdd:COG4913 444 ALRD 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
523-690 |
6.29e-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: 46.59 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 523 AAQVLESAGEG--PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlQFIEMQRDANRQIS 600
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 601 EYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMK 680
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 2462593701 681 ANRTALLAQQ 690
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
365-683 |
7.94e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVI------------EEQEEQMAEFYRENEEKSKELERqk 432
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteEHRKELLEEYTAELKRIEKELKE-- 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 433 hmcsvLQHKMEELKEGLRqrdELIEALEKQKEYIAclrnerdmLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEPV 512
Cdd:PRK03918 471 -----IEEKERKLRKELR---ELEKVLKKESELIK--------LKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKL 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 513 AGaitvVSQEAAQVLESAGEG-PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRN-DGTVGDLAGLQNgsdlQFIE 590
Cdd:PRK03918 535 IK----LKGEIKSLKKELEKLeELKKKLAELEKKLDELEEELAELLKELEELGFESVEElEERLKELEPFYN----EYLE 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 591 MqRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDE-----LKAEKRKLQRELRTALDKIEEM 665
Cdd:PRK03918 607 L-KDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEEL 685
|
330
....*....|....*...
gi 2462593701 666 EMTNSHLAKRLEKMKANR 683
Cdd:PRK03918 686 EKRREEIKKTLEKLKEEL 703
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
340-664 |
8.02e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 340 SLSELRD-IYDLKDQIQDVEGRYMQGLKELKESLSEVE------EKYKKamvSNAQLDNEKNNLIYQVDTLKDVIEEQEE 412
Cdd:TIGR04523 336 IISQLNEqISQLKKELTNSESENSEKQRELEEKQNEIEklkkenQSYKQ---EIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 413 QMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEALEK----QKEYIACLRNERDMLREELADLQETVK 488
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNtresLETQLKVLSRSINKIKQNLEQKQKELK 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 489 TGEKHGLVIIPDgtpNGDVSHEpvagaITVVSQEAAQVLEsagegpldvRLRKLAGEKEELLSQIRKLKLQLEEERQKCS 568
Cdd:TIGR04523 493 SKEKELKKLNEE---KKELEEK-----VKDLTKKISSLKE---------KIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 569 RNdgtvgDLAGLQNGSDLQFIEMQRDanrqISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEK 648
Cdd:TIGR04523 556 KE-----NLEKEIDEKNKEIEELKQT----QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKEN 626
|
330
....*....|....*....
gi 2462593701 649 RKLQRELRT---ALDKIEE 664
Cdd:TIGR04523 627 EKLSSIIKNiksKKNKLKQ 645
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
365-660 |
1.03e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM----AEFYRENEEKSKELERQKHMCSVLQH 440
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 441 KMEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIpdgtpngdvsHEPVAGAITVVS 520
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE----------EELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 521 QEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQfiemQRDANRQIS 600
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE----EEALLELLA 466
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462593701 601 EYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAE-KVEDELKAEKRKLQRELRTALD 660
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGLRGLAGAVA 527
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
365-666 |
1.25e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 365 LKELKESLSEVEEKYkkAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQmaefyRENEEKSKElerqkhmcsVLQHKMEE 444
Cdd:PRK02224 182 LSDQRGSLDQLKAQI--EEKEEKDLHERLNGLESELAELDEEIERYEEQ-----REQARETRD---------EADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 445 LKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVktgekhglviipdgtpngdvshEPVAGAITVVSQEAA 524
Cdd:PRK02224 246 HEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERL----------------------EELEEERDDLLAEAG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 525 qvLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGlqNGSDLQfiEMQRDANRQISEYKF 604
Cdd:PRK02224 304 --LDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE--RAEELR--EEAAELESELEEARE 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462593701 605 KLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEK-------RKLQRELRTALDKIEEME 666
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERdelrereAELEATLRTARERVEEAE 446
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
360-681 |
1.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 360 RYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNL--IYQVDTLKDVIEEQEEQMAEFYREN-EEKSKELERQKHMCS 436
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 437 VLQHKMEELKEGLrqrdELIEALEKQKEYiacLRNERDMLREELADLQETVKTgekhglviipdgtpNGDVSHEPVAGAI 516
Cdd:PRK03918 536 KLKGEIKSLKKEL----EKLEELKKKLAE---LEKKLDELEEELAELLKELEE--------------LGFESVEELEERL 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 517 tvvsqeaaQVLESAGEGPLdvRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlqfiemqrDAN 596
Cdd:PRK03918 595 --------KELEPFYNEYL--ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE-----------ELE 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 597 RQISEYKFKlsKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLqRELRTALDKIEEMEMTNSHLAKRL 676
Cdd:PRK03918 654 KKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER-EKAKKELEKLEKALERVEELREKV 730
|
....*
gi 2462593701 677 EKMKA 681
Cdd:PRK03918 731 KKYKA 735
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
399-664 |
1.42e-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: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 399 QVDTLKDVIEEQEEqmaefYRENEEKSKELERQKHMCSV--LQHKMEELKEGLRQRDELIEALEKQKEYiacLRNERDML 476
Cdd:COG4913 250 QIELLEPIRELAER-----YAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELER---LEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 477 REELADLQetvktgekhglviipdgtpngdvshepvagaitvvsqeaAQVLESAGEgpldvrlrklagEKEELLSQIRKL 556
Cdd:COG4913 322 REELDELE---------------------------------------AQIRGNGGD------------RLEQLEREIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 557 KLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQvlryktaaen 636
Cdd:COG4913 351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE---------- 420
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462593701 637 AEKVEDELKA-EKRK---------LQRELRTALDKIEE 664
Cdd:COG4913 421 LRELEAEIASlERRKsniparllaLRDALAEALGLDEA 458
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-667 |
1.66e-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: 45.06 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 407 IEEQEEQMAEFYRENEEKSKELER------QKHMCSVLQHKMEELKEGLRQRDelIEALEKQKEYIaclRNERDMLREEL 480
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERlrrereKAERYQALLKEKREYEGYELLKE--KEALERQKEAI---ERQLASLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 481 ADLQETVKTGEKHglviipdgtpngdvshepVAGAITVVSQEAAQVLESAGEGPLDVR--LRKLAGEKEELLSQIRKLKL 558
Cdd:TIGR02169 254 EKLTEEISELEKR------------------LEEIEQLLEELNKKIKDLGEEEQLRVKekIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 559 QLE----EERQKCSRNDGTVGDLAGLQngSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTA 633
Cdd:TIGR02169 316 ELEdaeeRLAKLEAEIDKLLAEIEELE--REIEEERKRRDKlTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
250 260 270
....*....|....*....|....*....|....
gi 2462593701 634 AENAEKVEDELKAEKRKLQRELRTALDKIEEMEM 667
Cdd:TIGR02169 394 LEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
361-690 |
1.82e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 361 YMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVL-- 438
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELek 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 439 ---QHKME--------------ELKEGLRQRDELIEALEKQ-----------KEYIACLRNERDMLREELADLQETVKTG 490
Cdd:TIGR04523 289 qlnQLKSEisdlnnqkeqdwnkELKSELKNQEKKLEEIQNQisqnnkiisqlNEQISQLKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 491 EKHGLVIIPDGTPNGDvSHEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSR- 569
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQ--KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDl 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 570 -NDGTVGDLAGLQNGSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTLEQSI-------SRLEGQVLRYKTAAENAEKV 640
Cdd:TIGR04523 446 tNQDSVKELIIKNLDNTRESLETQLKVlSRSINKIKQNLEQKQKELKSKEKELkklneekKELEEKVKDLTKKISSLKEK 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462593701 641 EDELKAEKRKLQRELRTALDKIEEMEMTN---------SHLAKRLEKMKANRTALLAQQ 690
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTQKSLKKKQ 584
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
538-689 |
2.53e-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: 42.99 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 538 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQfIEMQRDaNRQISEYKFKLSKAEQDITTLE 617
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRN-NKEYEALQKEIESLKRRISDLE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462593701 618 QSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEememtnshlaKRLEKMKANRTALLAQ 689
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE----------AELEELEAEREELAAK 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
349-681 |
2.96e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 349 DLKDQIQDVEGRYMQGLKELKESLSEVE---------EKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 419
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 420 ENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKTGE--KHGLVI 497
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEelKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 498 IPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDV--RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVG 575
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 576 DLAGLQNGSDLQFIEMQRDANRQI-SEYKFKLSKAEQDITTLEQSISRL-------------EGQVLRYKTAAENAEKVE 641
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLrkelrelekvlkkESELIKLKELAEQLKELE 509
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2462593701 642 DELKA----EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 681
Cdd:PRK03918 510 EKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
442-659 |
3.20e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 442 MEELKEglrQRDELIEALEKQKEYIAcLRNERDMLREELADLQEtvktgekhglviipdgtpngdvshepvagAITVVSQ 521
Cdd:COG4717 70 LKELKE---LEEELKEAEEKEEEYAE-LQEELEELEEELEELEA-----------------------------ELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 522 EAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISE 601
Cdd:COG4717 117 ELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462593701 602 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKvEDELKAEKRKLQRELRTAL 659
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLL 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
341-664 |
4.57e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 341 LSELRDiyDLKDQIQDVE---GRYMQGLKELKESLSEVEEKykkamvsnaqlDNEKNNLIYQVDTLKDVIEEQEEQmAEF 417
Cdd:PRK03918 298 LSEFYE--EYLDELREIEkrlSRLEEEINGIEERIKELEEK-----------EERLEELKKKLKELEKRLEELEER-HEL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 418 YRENEEKSKELER--QKHMCSVLQHKMEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKTGEkhgl 495
Cdd:PRK03918 364 YEEAKAKKEELERlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP---- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 496 viipdgTPNGDVSHEPVAGAITVVSQEAAQVLEsagegpldvRLRKLAGEKEELLSQIRKLKLQLEEERqKCSRNDGTVG 575
Cdd:PRK03918 440 ------VCGRELTEEHRKELLEEYTAELKRIEK---------ELKEIEEKERKLRKELRELEKVLKKES-ELIKLKELAE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 576 DLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQREL 655
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELG 583
|
....*....
gi 2462593701 656 RTALDKIEE 664
Cdd:PRK03918 584 FESVEELEE 592
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
365-686 |
4.71e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQH---K 441
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 442 MEELKEGLRQRDELIEALEKQKEYI-----------ACLRNERDMLREELAD----LQETVKTGEKHGLVIIPDGTPNGD 506
Cdd:pfam15921 550 CEALKLQMAEKDKVIEILRQQIENMtqlvgqhgrtaGAMQVEKAQLEKEINDrrleLQEFKILKDKKDAKIRELEARVSD 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 507 VSHEPV----AG-----AITVVSQEAAQVLESAGEG---------PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCS 568
Cdd:pfam15921 630 LELEKVklvnAGserlrAVKDIKQERDQLLNEVKTSrnelnslseDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELE 709
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 569 RNDGTVGDLaglqNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISrlegqvlryktaaeNAEKVEDELKAEK 648
Cdd:pfam15921 710 QTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT--------------NANKEKHFLKEEK 771
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2462593701 649 RKLQRELRT-ALDKIE---EMEMTNSHLAKRLEKMKANRTAL 686
Cdd:pfam15921 772 NKLSQELSTvATEKNKmagELEVLRSQERRLKEKVANMEVAL 813
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
365-686 |
5.69e-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: 43.09 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 444
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 445 LKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEP---VAGAITVVSQ 521
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNKKIKE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 522 EAAQVLEsagegpLDVRLRKLAGEKE-----ELLSQIRKLKLQLEEERQKCSRNDGTVGDLaglqnGSDLQFIEMQRD-- 594
Cdd:TIGR04523 286 LEKQLNQ------LKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQL-----NEQISQLKKELTns 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 595 ------ANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMT 668
Cdd:TIGR04523 355 esenseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKET 434
|
330
....*....|....*...
gi 2462593701 669 NSHLAKRLEKMKANRTAL 686
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVK 452
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
365-683 |
6.67e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcsvLQHKMEE 444
Cdd:pfam02463 192 LEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQE-----IEKEEEK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 445 LKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKTGEKhglviipdgtpNGDVSHEPVAGAITVVSQEAA 524
Cdd:pfam02463 267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE-----------KLKESEKEKKKAEKELKKEKE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 525 QVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ--KCSRNDGTVGDLAGL-QNGSDLQFIEMQRDANRQISE 601
Cdd:pfam02463 336 EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLakKKLESERLSSAAKLKeEELELKSEEEKEAQLLLELAR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 602 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 681
Cdd:pfam02463 416 QLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495
|
..
gi 2462593701 682 NR 683
Cdd:pfam02463 496 EE 497
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
590-681 |
8.51e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 590 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 656
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462593701 657 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 681
Cdd:COG2433 463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
365-662 |
8.61e-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: 42.79 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 365 LKELKESLSEVEEKYKKamvsnaqldnEKNNLIYQVDTLKDVIEEQEEQMAE---FYRENEEKSKELERQKHMCSvlqhk 441
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKK----------EINDKEKQVSLLLIQITEKENKMKDltfLLEESRDKANQLEEKTKLQD----- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 442 mEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREelaDLQETVKTgekhglviIPDGTPNGDVSHEPVAGAITVVSQ 521
Cdd:pfam05483 282 -ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE---DLQIATKT--------ICQLTEEKEAQMEELNKAKAAHSF 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 522 EAAQVleSAGEGPLDVRLRKlagEKEELLSQIRKLKLQLEEERQKCSRndgtVGDLAGLQNGSDLQFIEMQR-------- 593
Cdd:pfam05483 350 VVTEF--EATTCSLEELLRT---EQQRLEKNEDQLKIITMELQKKSSE----LEEMTKFKNNKEVELEELKKilaedekl 420
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593701 594 -DANRQISEYKFKLSKAEQDITTL----EQSISRLEGQVLRYKTAAENAEKVEDELKA--EKRKLQR-ELRTALDKI 662
Cdd:pfam05483 421 lDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKTSEEHYLKEVEDLKTelEKEKLKNiELTAHCDKL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
369-686 |
1.00e-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: 42.36 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 369 KESLSEVEEKYKKAMVsnaqLDNEKNNliyQVDTLKDvieeqEEQMAEFYRENEEKSKELERQKHMCSVLQHKmEELKEG 448
Cdd:TIGR02169 176 LEELEEVEENIERLDL----IIDEKRQ---QLERLRR-----EREKAERYQALLKEKREYEGYELLKEKEALE-RQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 449 LRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLE 528
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 529 SAGEgpLDVRLRKLAGEKEEL---LSQIRKLKLQLEEE---------------RQKCSRNDGTVGDLAGLQNGSDlQFIE 590
Cdd:TIGR02169 323 RLAK--LEAEIDKLLAEIEELereIEEERKRRDKLTEEyaelkeeledlraelEEVDKEFAETRDELKDYREKLE-KLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 591 MQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA----EKVEDELK---AEKRKLQRELRTALDKIE 663
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQEWKLEqlaADLSKYEQELYDLKEEYD 479
|
330 340
....*....|....*....|...
gi 2462593701 664 EMEMTNSHLAKRLEKMKANRTAL 686
Cdd:TIGR02169 480 RVEKELSKLQRELAEAEAQARAS 502
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
338-566 |
1.12e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 338 DTSLSELRD-----IYDLKDQIQDVEGR----YMQGLKELKESLSEVEEKYKKAmvsnaqldnEKNNLIYQVDTLKDVIE 408
Cdd:PRK05771 19 DEVLEALHElgvvhIEDLKEELSNERLRklrsLLTKLSEALDKLRSYLPKLNPL---------REEKKKVSVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 409 EQEE---QMAEFYRENEEKSKELERQKhmcSVLQHKMEELK--EGLrqrdELIEALEKQKEYIACL-------RNERDML 476
Cdd:PRK05771 90 DVEEeleKIEKEIKELEEEISELENEI---KELEQEIERLEpwGNF----DLDLSLLLGFKYVSVFvgtvpedKLEELKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 477 REELADLQETVKTGEKHGLVIIPDgtpngdvshepvAGAITVVSQEAAQV----LESAGEGPLDVRLRKLAGEKEELLSQ 552
Cdd:PRK05771 163 ESDVENVEYISTDKGYVYVVVVVL------------KELSDEVEEELKKLgferLELEEEGTPSELIREIKEELEEIEKE 230
|
250
....*....|....
gi 2462593701 553 IRKLKLQLEEERQK 566
Cdd:PRK05771 231 RESLLEELKELAKK 244
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
338-653 |
1.14e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 338 DTSLSELRDIYDLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKA-----MVSNAQLDNEK--------NNLIYQVD 401
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQEKieryqadlEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 402 TLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEALEKQK--------------EYIA 467
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKqlcglpdltadnaeDWLE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 468 CLRNERDMLREELADLQETVKtgekhglviipdgtpngdvshepvagaitvVSQEAAQVLESAGEgpldvRLRKLAGE-- 545
Cdd:PRK04863 446 EFQAKEQEATEELLSLEQKLS------------------------------VAQAAHSQFEQAYQ-----LVRKIAGEvs 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 546 KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQngsdlQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEG 625
Cdd:PRK04863 491 RSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA 565
|
330 340 350
....*....|....*....|....*....|..
gi 2462593701 626 QVLRYK----TAAENAEKVEDELKAEKRKLQR 653
Cdd:PRK04863 566 RLESLSesvsEARERRMALRQQLEQLQARIQR 597
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-637 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 363 QGLKELKESLSEVEEKYKKAmvsNAQLDNEKNnliyQVDTLKDVIEEQEEQMAefyrENEEKSKELERQkhmcsvlqhkM 442
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAEL---EKELAALKK----EEKALLKQLAALERRIA----ALARRIRALEQE----------L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 443 EELKEGLRQRDELIEALEKQkeyiacLRNERDMLREELADLQetvKTGEKHGL-VIIPDGTPNGDVSHEPVAGAITVVSQ 521
Cdd:COG4942 79 AALEAELAELEKEIAELRAE------LEAQKEELAELLRALY---RLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 522 EAAQVLESAGEgpldvRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISE 601
Cdd:COG4942 150 EQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAE 210
|
250 260 270
....*....|....*....|....*....|....*.
gi 2462593701 602 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA 637
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
341-689 |
1.33e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 341 LSELRD-IYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMA---- 415
Cdd:pfam15921 319 LSDLEStVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSleke 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 416 -----------------EFYRENEEKSKELERQ----KHMCSVLQHKMEELKEGLRQRDElieALEKQKEYIACLRNERD 474
Cdd:pfam15921 399 qnkrlwdrdtgnsitidHLRRELDDRNMEVQRLeallKAMKSECQGQMERQMAAIQGKNE---SLEKVSSLTAQLESTKE 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 475 MLR---EELADLQETVKTGEKhglvIIPDGTpngdVSHEPVAGAITVVSQEAAQVlesagEGPLDVRLRKLAGEKEE--- 548
Cdd:pfam15921 476 MLRkvvEELTAKKMTLESSER----TVSDLT----ASLQEKERAIEATNAEITKL-----RSRVDLKLQELQHLKNEgdh 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 549 ---LLSQIRKLKLQLEEE-------RQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDAN-RQISEYKFKLSKAEQD--ITT 615
Cdd:pfam15921 543 lrnVQTECEALKLQMAEKdkvieilRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINdRRLELQEFKILKDKKDakIRE 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 616 LEQSISRLEGQVLR----------------------------------------------YKTAAENAEKVEDELKAEKR 649
Cdd:pfam15921 623 LEARVSDLELEKVKlvnagserlravkdikqerdqllnevktsrnelnslsedyevlkrnFRNKSEEMETTTNKLKMQLK 702
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2462593701 650 KLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 689
Cdd:pfam15921 703 SAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQ 742
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
376-690 |
1.34e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 376 EEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEGLRQRDEL 455
Cdd:COG5185 228 IINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENA---NNLIKQFENTKEKIAEYTKS 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 456 IEALEKQKEYIACLRneRDMLREELADLQETVKTGEKhglviipDGTPNGDVSHEPVAGAITVVSQEAAQVLESagegpl 535
Cdd:COG5185 305 IDIKKATESLEEQLA--AAEAEQELEESKRETETGIQ-------NLTAEIEQGQESLTENLEAIKEEIENIVGE------ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 536 dVRLRKLAGEKEELLSQIRKLKLQLEEER--QKCSRNDGTVGDLAGLQNgSDLQFIEMQRDANRQISEYKFKLSKAEQDI 613
Cdd:COG5185 370 -VELSKSSEELDSFKDTIESTKESLDEIPqnQRGYAQEILATLEDTLKA-ADRQIEELQRQIEQATSSNEEVSKLLNELI 447
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593701 614 TTLEQsiSRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 690
Cdd:COG5185 448 SELNK--VMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQV 522
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
538-683 |
1.68e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 538 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 610
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462593701 611 QDITTLEQSISRLEGQVLRYKTAAENAEKvedELKAEKRKLQRELRTALDKIEEmemtnsHLAKRLEKMKANR 683
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
365-489 |
1.70e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN---EEKSKELER--QKHMCSVLQ 439
Cdd:COG1340 52 VKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERleWRQQTEVLS 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2462593701 440 HK-----MEELKEgLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKT 489
Cdd:COG1340 132 PEeekelVEKIKE-LEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKE 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
338-534 |
1.78e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 338 DTSLSELRD-IYDLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAE 416
Cdd:COG3883 15 DPQIQAKQKeLSELQAELEAAQAE----LDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 417 FYR-------------------------------------------ENEEKSKELERQKHMCSVLQHKMEELKEGL-RQR 452
Cdd:COG3883 91 RARalyrsggsvsyldvllgsesfsdfldrlsalskiadadadlleELKADKAELEAKKAELEAKLAELEALKAELeAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 453 DELIEALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGE 532
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
..
gi 2462593701 533 GP 534
Cdd:COG3883 251 AA 252
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
405-685 |
2.43e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 405 DVIEEQEEQMAEFYRENEEKSKELERQkhmcsvLQHKMEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQ 484
Cdd:COG1340 4 DELSSSLEELEEKIEELREEIEELKEK------RDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 485 ETVKTgekhglviipdgtpngdvshepVAGAITVVSQEAAQVLESAGEGPLDVR----LRK-------------LAGEKE 547
Cdd:COG1340 78 EERDE----------------------LNEKLNELREELDELRKELAELNKAGGsidkLRKeierlewrqqtevLSPEEE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 548 -ELLSQIRKLKLQLEEERQKCSRNDgtvgDLAGLQNGSDLQFIEMqRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQ 626
Cdd:COG1340 136 kELVEKIKELEKELEKAKKALEKNE----KLKELRAELKELRKEA-EEIHKKIKELAEEAQELHEEMIELYKEADELRKE 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462593701 627 VLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTA 685
Cdd:COG1340 211 ADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
416-686 |
2.77e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 416 EFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEALEKqkeyiacLRNERDMLREELADLQETvktgekhgl 495
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPE-------LREELEKLEKEVKELEEL--------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 496 viipdgtpngdvshepvagaitvvsqeaAQVLESagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVG 575
Cdd:PRK03918 237 ----------------------------KEEIEE-----LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 576 DLAGLQnGSDLQFIEMqrdaNRQISEYKFKLSKAEQDITTLEQSISRLEGQVlryKTAAENAEKVEdELKAEKRKLQREL 655
Cdd:PRK03918 284 ELKELK-EKAEEYIKL----SEFYEEYLDELREIEKRLSRLEEEINGIEERI---KELEEKEERLE-ELKKKLKELEKRL 354
|
250 260 270
....*....|....*....|....*....|.
gi 2462593701 656 RTALDKIEEMEMTNShLAKRLEKMKANRTAL 686
Cdd:PRK03918 355 EELEERHELYEEAKA-KKEELERLKKRLTGL 384
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
535-690 |
3.11e-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: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 535 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCS-------RNDGTVGDLAGLQNGSDLQ-FIE-------MQRDANRQI 599
Cdd:COG3883 56 LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSdFLDrlsalskIADADADLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 600 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 679
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
170
....*....|.
gi 2462593701 680 KANRTALLAQQ 690
Cdd:COG3883 216 AAAAAAAAAAA 226
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
327-485 |
3.12e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 327 GSGDTSSLIDPDTSLSELR-DIYDLKDQIQDVEGRyMQGLKELKESLSEVEEkykkamvsnaqLDNEKNNLIYQVDTLKD 405
Cdd:PRK02224 463 GSPHVETIEEDRERVEELEaELEDLEEEVEEVEER-LERAEDLVEAEDRIER-----------LEERREDLEELIAERRE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 406 VIEEQEEQMAEFYRENEEKSKELERQKHMCSVL----QHKMEELKEGLRQRDEL---IEALEK---QKEYIACLRNERDM 475
Cdd:PRK02224 531 TIEEKRERAEELRERAAELEAEAEEKREAAAEAeeeaEEAREEVAELNSKLAELkerIESLERirtLLAAIADAEDEIER 610
|
170
....*....|
gi 2462593701 476 LREELADLQE 485
Cdd:PRK02224 611 LREKREALAE 620
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
345-690 |
3.12e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.61 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 345 RDIYDLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAMVSNAQLDNE--KNNLIY--QVDTLKDVIEEQEEQMAEF 417
Cdd:pfam06160 86 KALDEIEELLDDIEEDIkqiLEELDELLESEEKNREEVEELKDKYRELRKTllANRFSYgpAIDELEKQLAEIEEEFSQF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 418 YRENE-----EKSKELERQKHMCSVLQHKMEELKEGLRQrdeliealekqkeyiacLRNErdmLREELADLQETVKTGEK 492
Cdd:pfam06160 166 EELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEE-----------------LKTE---LPDQLEELKEGYREMEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 493 HGLVIipdgtpngdvSHEPVAGAITVVSQEAAQVLESAGEGPLDvrlrKLAGEKEELLSQIRKLKLQLEEE---RQKCSR 569
Cdd:pfam06160 226 EGYAL----------EHLNVDKEIQQLEEQLEENLALLENLELD----EAEEALEEIEERIDQLYDLLEKEvdaKKYVEK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 570 NDGTVGDlaglqngsdlqFIEMQRDANRQISEykfklskaeqDITTLEQSisrlegqvlrYKTAAENAEKVEDeLKAEKR 649
Cdd:pfam06160 292 NLPEIED-----------YLEHAEEQNKELKE----------ELERVQQS----------YTLNENELERVRG-LEKQLE 339
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2462593701 650 KLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 690
Cdd:pfam06160 340 ELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQ 380
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
404-566 |
3.73e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 40.51 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 404 KDVIEEQEEQMAEFYRENEEKSKELERQKHMcsvLQHKMEELKEGLRQRDELIEALEKQKEYIAclRNERDMLREELADL 483
Cdd:COG1193 499 EEIIERARELLGEESIDVEKLIEELERERRE---LEEEREEAERLREELEKLREELEEKLEELE--EEKEEILEKAREEA 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 484 QETVKTGEKhglviipdgtpngdvshepvagaitvvsqEAAQVLEsagegpldvRLRKLAGEKEEL---LSQIRKLKLQL 560
Cdd:COG1193 574 EEILREARK-----------------------------EAEELIR---------ELREAQAEEEELkeaRKKLEELKQEL 615
|
....*.
gi 2462593701 561 EEERQK 566
Cdd:COG1193 616 EEKLEK 621
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
407-680 |
3.74e-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: 40.48 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 407 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEAlEKQKEYIAclrNERDMLREELADLQET 486
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDE-KKQFEKIA---EELKGKEQELIFLLQA 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 487 vKTGEKHGLVIIPDGTPNGDVSH-EPVAGAITVVSQEAAQVLEsagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ 565
Cdd:pfam05483 448 -REKEIHDLEIQLTAIKTSEEHYlKEVEDLKTELEKEKLKNIE------LTAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 566 KCSRNDGTVGDLagLQNGSDLQFIEMQ---------RDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRY------ 630
Cdd:pfam05483 521 DIINCKKQEERM--LKQIENLEEKEMNlrdelesvrEEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILenkcnn 598
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462593701 631 -KTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMK 680
Cdd:pfam05483 599 lKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAK 649
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
362-447 |
4.21e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.71 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 362 MQGLKELKESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHK 441
Cdd:COG4026 127 IPEYNELREELLELKEKID-------EIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
|
....*.
gi 2462593701 442 MEELKE 447
Cdd:COG4026 200 FEELLK 205
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
338-638 |
4.38e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 338 DTSLSELRD-IYDLKDQIQDVEGRYMQGLKELKESLSEV---EEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQ 413
Cdd:COG1196 266 EAELEELRLeLEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 414 MAEFYRENEEKSKEL----ERQKHMCSVLQHKMEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADLQETVKT 489
Cdd:COG1196 346 LEEAEEELEEAEAELaeaeEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 490 GEKhglviipdgtpngdvshepvagaitvvSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSR 569
Cdd:COG1196 426 LEE---------------------------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462593701 570 NDGTVGDLAGLQNGSDLQfIEMQRDANRQISEYKFKLSKAEQDIttLEQSISRLEGQVLRYKTAAENAE 638
Cdd:COG1196 479 LAELLEELAEAAARLLLL-LEAEADYEGFLEGVKAALLLAGLRG--LAGAVAVLIGVEAAYEAALEAAL 544
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
349-566 |
4.55e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 349 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 428
Cdd:COG4942 24 EAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 429 ERQKHM-------------------------CSVLQHKMEELKEGLRQRDELIEALEKQKEYIACLRNERDMLREELADL 483
Cdd:COG4942 100 EAQKEElaellralyrlgrqpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 484 QETVKTGEKhglviipdgtpngdvshepvagAITVVSQEAAQVLES--AGEGPLDVRLRKLAGEKEELLSQIRKLKLQLE 561
Cdd:COG4942 180 LAELEEERA----------------------ALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*
gi 2462593701 562 EERQK 566
Cdd:COG4942 238 AAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
335-489 |
5.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 335 IDPDTSLSELRDIYDLKDQIQDVEGRYMQGLKELKEslsEVEEKYKKAMVSNAQLDNEknnliyqvDTLKDVIEEQEEqm 414
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEELQL---EELEQEIAALLAEAGVEDE--------EELRAALEQAEE-- 396
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462593701 415 aefYRENEEKSKELERQkhmcsvLQHKMEELKEGLRQRD--ELIEALEKQKEYIACLRNERDMLREELADLQETVKT 489
Cdd:COG4717 397 ---YQELKEELEELEEQ------LEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
350-680 |
5.29e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.10 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 350 LKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMvsnaqldneknnliyqvDTLKDVIEEQEEQMAEFYRENEEKSKELE 429
Cdd:pfam15921 304 IQEQARNQNSMYMRQLSDLESTVSQLRSELREAK-----------------RMYEDKIEELEKQLVLANSELTEARTERD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 430 RQKHMCSVLQHKMEELKEGLRQRDELIeALEKQKEYIACLRNER-----DMLREELADLQETVKTGEkhGLVIIPDGTPN 504
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHKREKEL-SLEKEQNKRLWDRDTGnsitiDHLRRELDDRNMEVQRLE--ALLKAMKSECQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 505 GDVSHEPVA-----GAITVVSQEAAQvLESAGEGPLDVrLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAG 579
Cdd:pfam15921 444 GQMERQMAAiqgknESLEKVSSLTAQ-LESTKEMLRKV-VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 580 LQNGSDLQFIEMQ---------RDANRQISEYKFKLSKAEQDITTLEQSI---SRLEGQVLRyKTAAENAEKVEDELKAE 647
Cdd:pfam15921 522 LRSRVDLKLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIenmTQLVGQHGR-TAGAMQVEKAQLEKEIN 600
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462593701 648 KRKLQ-RELRTALD----KIEEMEMTNSHLakRLEKMK 680
Cdd:pfam15921 601 DRRLElQEFKILKDkkdaKIRELEARVSDL--ELEKVK 636
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
345-491 |
6.57e-03 |
|
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: 40.04 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 345 RDIYDLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEK 424
Cdd:TIGR02168 316 RQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462593701 425 SKELERQKHMCSVLQHKMEELKEGLRQRDELIEALEKQKEY--IACLRNERDMLREELADLQETVKTGE 491
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaeLKELQAELEELEEELEELQEELERLE 460
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
350-492 |
8.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 350 LKDQIQDVEGRYMQGLKELKESLSEVEEKYKKaMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELE 429
Cdd:PRK03918 572 LAELLKELEELGFESVEELEERLKELEPFYNE-YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE 650
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462593701 430 RQKHMCSVLQHkmEELKEGLRQRDELIEALEKQKEYiacLRNERDMLREELADLQETVKTGEK 492
Cdd:PRK03918 651 ELEKKYSEEEY--EELREEYLELSRELAGLRAELEE---LEKRREEIKKTLEKLKEELEEREK 708
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
343-537 |
9.37e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.07 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 343 ELRDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLI--YQVDTlkDVIEEQ---EEQMAEF 417
Cdd:pfam06160 264 ALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQqsYTLNE--NELERVrglEKQLEEL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462593701 418 YRENEEKSKELERQKHMCSVLQHKMEELKEGLrqrDELIEALEKQKEYIACLRNERDMLREELA----DLQETVKTGEKH 493
Cdd:pfam06160 342 EKRYDEIVERLEEKEVAYSELQEELEEILEQL---EEIEEEQEEFKESLQSLRKDELEAREKLDefklELREIKRLVEKS 418
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2462593701 494 GLVIIPDGTPNgdvshepvagAITVVSQEAAQVLESAGEGPLDV 537
Cdd:pfam06160 419 NLPGLPESYLD----------YFFDVSDEIEDLADELNEVPLNM 452
|
|
| |
