|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
242-533 |
1.16e-104 |
|
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: 318.56 E-value: 1.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 242 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 312
Cdd:pfam09738 30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 313 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 392
Cdd:pfam09738 93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 393 AEVKEALKEREEMLEKHGIILNSEIATNGEtsdTLNNVGYQGPTKMTKAELNALKSTGDGTLDIRLKKLVDERECLLEQI 472
Cdd:pfam09738 166 AELKEQLKQRDELIEKHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEV 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622852877 473 KKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 533
Cdd:pfam09738 243 RKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
316-607 |
3.56e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 316 KEMKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEV 395
Cdd:TIGR02169 670 RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 396 KEALKEREEMLEKHGIILNSEIATNGETSDTLNNVgyqgptkmtKAELNALKstgDGTLDIRLKKLVDERECLLEQIKKL 475
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRI 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 476 KGQLEERQKigKLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENA 555
Cdd:TIGR02169 811 EARLREIEQ--KLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622852877 556 EKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 607
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-583 |
1.30e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 288 EASIREI-KELNELKDQIQDVEGK----------YMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDM 356
Cdd:TIGR02168 690 EEKIAELeKALAELRKELEELEEEleqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 357 LLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLNNVGYQgpT 436
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--I 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 437 KMTKAELNALKSTGDgTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQ 516
Cdd:TIGR02168 848 EELSEDIESLAAEIE-ELEELIEELESELEALLNERASLEEALALLRS--ELEELSEELRELESK--------RSELRRE 916
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852877 517 ISDLKFKLAKSEQEITALEQNVIRLESQVS-RYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 583
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
264-607 |
1.72e-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: 54.68 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 264 ATLASLGGTSSRRGSGDTSISIDTEASI----REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQL 339
Cdd:TIGR02168 645 YRIVTLDGDLVRPGGVITGGSAKTNSSIlerrREIEELEEK--------------IEELEEKIAELEKALAELRKELEEL 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 340 DNEktnfmyqVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKhgiiLNSEIAT 419
Cdd:TIGR02168 711 EEE-------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE----AEEELAE 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 420 NGETSDTLnnvgyQGPTKMTKAELNALKSTGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKldnlRS 493
Cdd:TIGR02168 780 AEAEIEEL-----EAQIEQLKEELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE----EL 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 494 EDDVLEngtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQREL 573
Cdd:TIGR02168 851 SEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
330 340 350
....*....|....*....|....*....|....
gi 1622852877 574 rsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 607
Cdd:TIGR02168 918 -------EELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
295-608 |
3.18e-07 |
|
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: 53.49 E-value: 3.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 295 KELNELKDQIQDVEGKYMQGL-KEMKDSLAEVEEKY---KKAMVSNAQLDNEKTNfmyQVDTLKDMLLELEEQLAESRRQ 370
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLeeiQNQISQNNKIISQLNE---QISQLKKELTNSESENSEKQRE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 371 YEEKNKEFEREKhahsilqfqfaEVKEALKEREEMLEKHGIILNSEIATNGETSDTLnnvgyqgptkmtkaelnalkstg 450
Cdd:TIGR04523 365 LEEKQNEIEKLK-----------KENQSYKQEIKNLESQINDLESKIQNQEKLNQQK----------------------- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 451 dgtlDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMH----------VMDLQRDANRQISDL 520
Cdd:TIGR04523 411 ----DEQIKKLQQEKELLEKEIERLKETIIKNNS--EIKDLTNQDSVKELIIKNLdntresletqLKVLSRSINKIKQNL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 521 KFK---LAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALD---------KTEELEVSNG 588
Cdd:TIGR04523 485 EQKqkeLKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEID 564
|
330 340
....*....|....*....|
gi 1622852877 589 HLVKRLEKMKANRSALLSQQ 608
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQ 584
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
453-607 |
5.88e-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: 48.00 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 453 TLDIRLKKLVDERECLLEQIKKLKGQLEERQK-----IGKLDNLRSEDDVLENGTDMHVMDLQRD--------ANRQISD 519
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 520 LKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEelevsnghlvKRLEKMKA 599
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE----------AELEELEA 163
|
....*...
gi 1622852877 600 NRSALLSQ 607
Cdd:COG1579 164 EREELAAK 171
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
457-608 |
1.64e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 457 RLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENgtdmhvmdLQRDANRQISDLKFKLAKSEQEITALEQ 536
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEE--ELEQARSELEQLEE--------ELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852877 537 NVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 608
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
310-601 |
2.86e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 310 KYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN---FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHS 386
Cdd:PRK03918 456 EYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeseLIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 387 ILQFQFAEVKEALKEREEmLEKHGIILNSEIAT----NGETSDTLNNVGYqGPTKMTKAELNALKSTGDGTldIRLKKLV 462
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEE-LKKKLAELEKKLDEleeeLAELLKELEELGF-ESVEELEERLKELEPFYNEY--LELKDAE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 463 DERECLLEQIKKLKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQNVIRLE 542
Cdd:PRK03918 612 KELEREEKELKKLEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELREEYLELS 672
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852877 543 SQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 601
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-604 |
3.67e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 295 KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNE-KTNFM--YQVDtLKDMLLELEEQLAESRRQY 371
Cdd:PRK03918 405 EEISKITARIGELKKE----IKELKKAIEELKKAKGKCPVCGRELTEEhRKELLeeYTAE-LKRIEKELKEIEEKERKLR 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 372 EEKnKEFEREKHAHSILqFQFAEVKEALKEREEMLEKHGIilnSEIATNGETSDTLNN--VGYQGPTKMTKAELNALKSt 449
Cdd:PRK03918 480 KEL-RELEKVLKKESEL-IKLKELAEQLKELEEKLKKYNL---EELEKKAEEYEKLKEklIKLKGEIKSLKKELEKLEE- 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 450 gdgtLDIRLKKLVDERECLLEQIKKLKGQLEERqKIGKLDNLRSEDDVLENGTDMHVMdlQRDANRQISDLKFKLAKSEQ 529
Cdd:PRK03918 554 ----LKKKLAELEKKLDELEEELAELLKELEEL-GFESVEELEERLKELEPFYNEYLE--LKDAEKELEREEKELKKLEE 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 530 EITALEQNVIRLESQVSRYKSAAENAEKIEDE-----LKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 604
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
286-588 |
6.36e-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: 46.21 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 286 DTEASIREI--------KELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVS--------NAQLDNEKTNFMYQ 349
Cdd:TIGR02169 234 ALERQKEAIerqlasleEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekigelEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 350 VDTLKDMLLELEEQLAEsRRQYEEKNKEFEREKHAhsiLQFQFAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLnn 429
Cdd:TIGR02169 314 ERELEDAEERLAKLEAE-IDKLLAEIEELEREIEE---ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL-- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 430 VGYQGPTKMTKAELNALKSTGDgtldirlkKLVDERECLLEQIKKLKGQLEerqkigkldnlRSEDDVLENGTDMHVMDL 509
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELD--------RLQEELQRLSEELADLNAAIA-----------GIEAKINELEEEKEDKAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 510 Q-RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRyksaaenAEKIEDELKAEKRKLQRELRSALDKTEELEVSNG 588
Cdd:TIGR02169 449 EiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-------LQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
457-608 |
9.44e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 457 RLKKLVDERECLLEQIKKLKGQLEE-----RQKIGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISDLKFKLA 525
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEEltaelQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 526 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALL 605
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
...
gi 1622852877 606 SQQ 608
Cdd:TIGR02168 393 LQI 395
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
297-599 |
1.19e-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: 45.49 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 297 LNELKDQIQDVEGKY---MQGLKEMKDSLAEVEEKYKKAM-VSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYE 372
Cdd:pfam15921 262 LQQHQDRIEQLISEHeveITGLTEKASSARSQANSIQSQLeIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 373 EKNKEFEREkhahsiLQFQFAEVKEALKEREEMLEKHGIILNS-------------EIATNGETS------DTLNNVGYQ 433
Cdd:pfam15921 342 DKIEELEKQ------LVLANSELTEARTERDQFSQESGNLDDQlqklladlhkrekELSLEKEQNkrlwdrDTGNSITID 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 434 G----------PTKMTKAELNALKSTGDGTLDIRLKKLVDEREClLEQIKKLKGQLEERQKIGK--LDNLRSEDDVLENg 501
Cdd:pfam15921 416 HlrrelddrnmEVQRLEALLKAMKSECQGQMERQMAAIQGKNES-LEKVSSLTAQLESTKEMLRkvVEELTAKKMTLES- 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 502 tdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQV-------SRYKSAAENAEKIEDELKA------EKRK 568
Cdd:pfam15921 494 -----------SERTVSDLTASLQEKERAIEATNAEITKLRSRVdlklqelQHLKNEGDHLRNVQTECEAlklqmaEKDK 562
|
330 340 350
....*....|....*....|....*....|.
gi 1622852877 569 LQRELRSALDKTEELEVSNGHLVKRLEKMKA 599
Cdd:pfam15921 563 VIEILRQQIENMTQLVGQHGRTAGAMQVEKA 593
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
288-574 |
1.35e-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: 45.10 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 288 EASIREIKELNE----LKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLkdmlleleeq 363
Cdd:pfam05483 530 ERMLKQIENLEEkemnLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL---------- 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 364 laesRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKHGIILNSEIATNGETSDTlnnvgYQGptkmtkael 443
Cdd:pfam05483 600 ----KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDN-----YQK--------- 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 444 nalkstgdgtlDIRLKKLVDERecLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFK 523
Cdd:pfam05483 662 -----------EIEDKKISEEK--LLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622852877 524 LAKS-EQEITALEqnvIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELR 574
Cdd:pfam05483 729 LYKNkEQEQSSAK---AALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-566 |
1.55e-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: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 288 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 367
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 368 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKhgiiLNSEIATNGETSDTLNNvgyqgptkmtkaELNalk 447
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNN------------EIE--- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 448 stgdgTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHvmdlqRDANRQISDLKFKLAKS 527
Cdd:TIGR02168 404 -----RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL-----ERLEEALEELREELEEA 473
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622852877 528 EQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEK 566
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALL 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-604 |
1.65e-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: 44.37 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 368 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKhgiilnseiatngetsdtlnnvgyqgptkmTKAELNALK 447
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA------------------------------LEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 448 StgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLrsedDVLENGTDMhvmdlqRDANRQISDLKFK 523
Cdd:COG4942 83 A--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL----ALLLSPEDF------LDAVRRLQYLKYL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 524 LAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSA 603
Cdd:COG4942 145 APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
.
gi 1622852877 604 L 604
Cdd:COG4942 225 L 225
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
289-607 |
1.69e-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: 44.72 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 289 ASIREIKELneLKDQIQDVEGKYM---QGLKEMKDSLAEVEEKYKKAMVSNAQ-----------------LDNEKT---N 345
Cdd:pfam15921 468 AQLESTKEM--LRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEitklrsrvdlklqelqhLKNEGDhlrN 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 346 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKHGIILNSEIATNGETSd 425
Cdd:pfam15921 546 VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELE- 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 426 tlnnvgyqgpTKMTKAELNALKSTGDGTLDIR-LKKLVDERECLLEQIKKLKGQL----EERQKIGKldNLRSEDDVLEN 500
Cdd:pfam15921 625 ----------ARVSDLELEKVKLVNAGSERLRaVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKR--NFRNKSEEMET 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 501 GTD---MHVMDLQRDANRQISDLK---------FKLAKSEQ-EITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKR 567
Cdd:pfam15921 693 TTNklkMQLKSAQSELEQTRNTLKsmegsdghaMKVAMGMQkQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKN 772
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1622852877 568 KLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 607
Cdd:pfam15921 773 KLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
368-577 |
2.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 368 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEKHGIILNSEiatngetsdtlnnvgyqgptkmtkaelnalk 447
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------------------------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 448 stgdgTLDIRLKKLVDERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAK 526
Cdd:COG4717 129 -----PLYQELEALEAELAELPERLEELEERLEElRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622852877 527 SEQEITALEQNVIRLESQVSRYKSAAENAEKiEDELKAEKRKLQRELRSAL 577
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLL 253
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
299-600 |
2.72e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 299 ELKDQIQDVEGK-YMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNfmyqvdtlkdmlleLEEQLAESRRQYEEKNKE 377
Cdd:TIGR02168 217 ELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQE--------------LEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 378 FEREKH---AHSILQFQFAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLnnvgyqgptkmtKAELNALKsTGDGTL 454
Cdd:TIGR02168 283 IEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL------------AEELAELE-EKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 455 DIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMHVMDLQRdANRQISDLKFKLAKSEQEITAL 534
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELESRLEELEE--QLETLRSKVAQLELQIASLNNEIER-LEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852877 535 -----EQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQ---RELRSALDKTEELEVSNGHLVKRLEKMKAN 600
Cdd:TIGR02168 427 lkkleEAELKELQAELEELEEELEELQEELERLEEALEELReelEEAEQALDAAERELAQLQARLDSLERLQEN 500
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
369-608 |
3.20e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 369 RQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREemLEKHGIILNSEIATNGETSDTLNNvgyqgptkmTKAELNALks 448
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEELEAE--LEELEAELEELEAELAELEAELEE---------LRLELEEL-- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 449 tgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIG-KLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKS 527
Cdd:COG1196 280 --ELELEEAQAEEYELLAELARLEQDIARLEERRRELEeRLEELEEELAELE--------EELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 528 EQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 607
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
.
gi 1622852877 608 Q 608
Cdd:COG1196 430 L 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
457-599 |
3.99e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 457 RLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLE-----NGTDmHVMDLQRD-----------------AN 514
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEA--RLDALREELDELEaqirgNGGD-RLEQLEREierlereleererrrarLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 515 RQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEkieDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 594
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442
|
....*
gi 1622852877 595 EKMKA 599
Cdd:COG4913 443 LALRD 447
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
283-608 |
5.76e-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: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 283 ISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKamvsNAQLDNEKTNFMYQVDTLKDMLLELEE 362
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNK----YNDLKKQKEELENELNLLEKEKLNIQK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 363 QLAESRRQ-------------YEEKNKEFEREkhaHSILQFQFAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLNN 429
Cdd:TIGR04523 188 NIDKIKNKllklelllsnlkkKIQKNKSLESQ---ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 430 VGYQGPTKMTKAELNALKSTgdgTLDIRLKKLVDERECLLEQ-----IKKLKGQLEERQKigKLDNLRSEDDvlengtdm 504
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIK---ELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEK--KLEEIQNQIS-------- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 505 hvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 584
Cdd:TIGR04523 332 -------QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
330 340
....*....|....*....|....
gi 1622852877 585 VSNGHLVKRLEKMKANRSALLSQQ 608
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEI 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
368-608 |
7.02e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 368 RRQYEEKNKEFEREKHAHSILQFQFAEVKEA---LKEREEMLEKHGIILNSEIATNGETSDTLnnvgyqgptkmtKAELN 444
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEeyeLLAELARLEQDIARLEERRRELEERLEEL------------EEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 445 ALKSTGDG------TLDIRLKKLVDERECLLEQIKKLKGQLEERQKIgKLDNLRSEDDVLENgtDMHVMDLQRDANRQIS 518
Cdd:COG1196 327 ELEEELEEleeeleELEEELEEAEEELEEAEAELAEAEEALLEAEAE-LAEAEEELEELAEE--LLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 519 DLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 598
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250
....*....|
gi 1622852877 599 ANRSALLSQQ 608
Cdd:COG1196 484 EELAEAAARL 493
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
549-608 |
8.40e-04 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 41.45 E-value: 8.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 549 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 608
Cdd:pfam11932 27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
286-565 |
1.15e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 286 DTEASIREIKELNELKDQIQDVEGKYMQGLKE----MKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmllele 361
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLALQKMQSEKEqltyWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLG------- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 362 eqlaeSRRQYEEknkeferEKHAHSILQFQfAEVKEALKEREEMLEKHGIILNSEIATNGETSDTLNNVGYQ-------- 433
Cdd:TIGR00618 732 -----SDLAARE-------DALNQSLKELM-HQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrlreedt 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 434 GPTKMTKAELNALKSTGDGTLDIRLKKLVDERECLLEQIKKL-KGQLEERQKIGKL-DNLRSEDDVLENGTDMHVMDLQR 511
Cdd:TIGR00618 799 HLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKsATLGEITHQLLKYeECSKQLAQLTQEQAKIIQLSDKL 878
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622852877 512 DANRQISDLK--FKLAKSEQEITAleQNVIRLESQ-----VSRY--KSAAENAEKIEDELKAE 565
Cdd:TIGR00618 879 NGINQIKIQFdgDALIKFLHEITL--YANVRLANQsegrfHGRYadSHVNARKYQGLALLVAD 939
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
463-604 |
1.33e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 463 DERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVLENgtdmHVMDLQRDANR-----QISDLKFKLAKSEQEITALEQ 536
Cdd:COG4717 71 KELKELEEELKEAEEKEEEyAELQEELEELEEELEELEA----ELEELREELEKlekllQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852877 537 NVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSnghLVKRLEKMKANRSAL 604
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAEL 211
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
473-602 |
1.36e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.16 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 473 KKLKGQLEERQKI-GKLDNLRSEDDVLENGTDMHVMDLQ---RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-- 546
Cdd:pfam04849 171 EKLRGLEEENLKLrSEASHLKTETDTYEEKEQQLMSDCVeqlSEANQQMAELSEELARKMEENLRQQEEITSLLAQIVdl 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622852877 547 --RYKSAAENAEKIEDELKAEK---RKLQRELRSALDKTEELEvsnGHLVKRLEKMKANRS 602
Cdd:pfam04849 251 qhKCKELGIENEELQQHLQASKeaqRQLTSELQELQDRYAECL---GMLHEAQEELKELRK 308
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
353-608 |
1.97e-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: 41.20 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 353 LKDMLLELEEQLAESRRQ------YEEKNKEFEREKHAHSILQFQFA-----EVKEALKEREEMLEKhgiiLNSEIATng 421
Cdd:TIGR02168 191 LEDILNELERQLKSLERQaekaerYKELKAELRELELALLVLRLEELreeleELQEELKEAEEELEE----LTAELQE-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 422 etsdtlnnvgyqgptkmTKAELNALKStGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENg 501
Cdd:TIGR02168 265 -----------------LEEKLEELRL-EVSELEEEIEELQKELYALANEISRLEQQKQILRE--RLANLERQLEELEA- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 502 tdmhvmDLQRDANRQIsDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALdktE 581
Cdd:TIGR02168 324 ------QLEELESKLD-ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE---L 393
|
250 260 270
....*....|....*....|....*....|
gi 1622852877 582 ELEVSNGHLV---KRLEKMKANRSALLSQQ 608
Cdd:TIGR02168 394 QIASLNNEIErleARLERLEDRRERLQQEI 423
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
513-605 |
2.03e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 513 ANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVK 592
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90
....*....|...
gi 1622852877 593 RLEKMKANRSALL 605
Cdd:COG4942 98 ELEAQKEELAELL 110
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
295-584 |
2.27e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 295 KELNELKDQIQDVE---GKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNektnfmyQVDTLKDMLLELEEQLAESRRQY 371
Cdd:TIGR04523 363 RELEEKQNEIEKLKkenQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE-------QIKKLQQEKELLEKEIERLKETI 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 372 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEkhgiILNSEIATNGETSDTLnnvgyQGPTKMTKAELNALKSTgD 451
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK----VLSRSINKIKQNLEQK-----QKELKSKEKELKKLNEE-K 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 452 GTLDIRLKKLVDERECLLEQIKKLKgqLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDA-NRQISDLK--FKLAKSE 528
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDLEDELNKDDFELKKENLEKEIDEkNKEIEELKqtQKSLKKK 583
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622852877 529 QE-----ITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 584
Cdd:TIGR04523 584 QEekqelIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
468-604 |
2.42e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 468 LLEQIKKLKG---QLEE-RQKIGKLDNLRseddvlENGTDMHVMDLQRDANRQIsDLKFKLAKSEQEITALEQNVIRLES 543
Cdd:COG4913 230 LVEHFDDLERaheALEDaREQIELLEPIR------ELAERYAAARERLAELEYL-RAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852877 544 QVSRYKSAAENAEKIEDELKAEKRKLQRELRSA-LDKTEELEVSNGHLVKRLEKMKANRSAL 604
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARL 364
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
464-596 |
3.38e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 464 ERECLLEQIKKLKGQLEErqkigkldnLRSEDDVLENgtDMHVMDlqrdanRQISDLKFKL----------AKSEQEITA 533
Cdd:COG2433 407 ELTEEEEEIRRLEEQVER---------LEAEVEELEA--ELEEKD------ERIERLERELsearseerreIRKDREISR 469
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622852877 534 LEQNVIRLESQVsryksaaenaekieDELKAEKRKLQRELRSaLDKTEELEVSNGHL-VKRLEK 596
Cdd:COG2433 470 LDREIERLEREL--------------EEERERIEELKRKLER-LKELWKLEHSGELVpVKVVEK 518
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
453-599 |
3.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 453 TLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQ--RDANRQISDLKFKLAKSEQE 530
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEelRELEEELEELEAELAELQEE 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852877 531 ITALEQNV-IRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVS--NGHLVKRLEKMKA 599
Cdd:COG4717 179 LEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleAAALEERLKEARL 250
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
268-607 |
4.30e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 268 SLGGTSSRRGSGDTSISIDTEASIREikELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFM 347
Cdd:pfam12128 579 NLYGVKLDLKRIDVPEWAASEEELRE--RLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLR 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 348 YQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHA--HSILQFQFAEVKEALKEREEMLEKHGIILnseiatnGETSD 425
Cdd:pfam12128 657 RLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQldKKHQAWLEEQKEQKREARTEKQAYWQVVE-------GALDA 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 426 TLNNVGYQGPTKMT--KAELNALKSTGDGTLDirlKKLVDErecllEQIKKLKGQLEE-RQKIGKLDNLRSEddVLENGT 502
Cdd:pfam12128 730 QLALLKAAIAARRSgaKAELKALETWYKRDLA---SLGVDP-----DVIAKLKREIRTlERKIERIAVRRQE--VLRYFD 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 503 DMHVMDLQRDANRQIsdlkfKLAKSEQEITALEQNVIRLESQVSRYKSAAEN----AEKIEDELKAEKRKLQRELRS--- 575
Cdd:pfam12128 800 WYQETWLQRRPRLAT-----QLSNIERAISELQQQLARLIADTKLRRAKLEMerkaSEKQQVRLSENLRGLRCEMSKlat 874
|
330 340 350
....*....|....*....|....*....|....
gi 1622852877 576 -ALDKT-EELEVSNGHLVKRLEKMKANRSALLSQ 607
Cdd:pfam12128 875 lKEDANsEQAQGSIGERLAQLEDLKLKRDYLSES 908
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
455-585 |
5.38e-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: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 455 DIRLKKLVDERECLLEQIKKLKGQLEERQK-IGKLDNLRSE--------DDVLENGTDmHVMDL----QRDANRQISDLK 521
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEeLEKLTEEISElekrleeiEQLLEELNK-KIKDLgeeeQLRVKEKIGELE 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622852877 522 FKLAKSEQEITALEQNVIRLE-------SQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEV 585
Cdd:TIGR02169 301 AEIASLERSIAEKERELEDAEerlakleAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
294-598 |
6.01e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 294 IKELNELKDQIQDV---EGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMlleleeqlaesRRQ 370
Cdd:PRK03918 171 IKEIKRRIERLEKFikrTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-----------KEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 371 YEEKNKEFE-REKHAHSIlqfqfaevKEALKEREEMLEKhgiilnseiaTNGETSDTLNNVGyqgptkmtkaELNALKst 449
Cdd:PRK03918 240 IEELEKELEsLEGSKRKL--------EEKIRELEERIEE----------LKKEIEELEEKVK----------ELKELK-- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 450 GDGTLDIRLKKLVDERECLLEQIKKLKGQLEER-----QKIGKLDNLRSEDDVLENgtdmhvmdLQRDANRQISDLKfKL 524
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEingieERIKELEEKEERLEELKK--------KLKELEKRLEELE-ER 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622852877 525 AKSEQEITALEQNVIRLESqvsryKSAAENAEKIEDELKA---EKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 598
Cdd:PRK03918 361 HELYEEAKAKKEELERLKK-----RLTGLTPEKLEKELEElekAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
439-588 |
6.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 439 TKAELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEERQK---------------IGKLDNL---RSEDDVLEN 500
Cdd:COG3883 49 LNEEYNELQA--------ELEALQAEIDKLQAEIAEAEAEIEERREelgeraralyrsggsVSYLDVLlgsESFSDFLDR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 501 --------GTDMHVMDLQRDANRQISDLKFKLAKSEQEITA----LEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRK 568
Cdd:COG3883 121 lsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEAlkaeLEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAE 200
|
170 180
....*....|....*....|
gi 1622852877 569 LQRELRSALDKTEELEVSNG 588
Cdd:COG3883 201 LEAELAAAEAAAAAAAAAAA 220
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
515-596 |
6.56e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 515 RQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKsaaENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 594
Cdd:PRK12704 68 KLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL---ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
..
gi 1622852877 595 EK 596
Cdd:PRK12704 145 ER 146
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
429-608 |
6.66e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 429 NVGYQGPT-KMTKAELNAL-KSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDV--LENGTDM 504
Cdd:COG3206 139 EISYTSPDpELAAAVANALaEAYLEQNLELRREEARKALEFLEEQLPELRKELEEAEA--ALEEFRQKNGLvdLSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 505 HVMDLQrDANRQISDLKFKLAKSEQEITALEQNV---------------------------IRLESQVSRYKSAAENAEK 557
Cdd:COG3206 217 LLQQLS-ELESQLAEARAELAEAEARLAALRAQLgsgpdalpellqspviqqlraqlaeleAELAELSARYTPNHPDVIA 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622852877 558 IEDELKAEKRKLQRELRSALDKTE----ELEVSNGHLVKRLEKMKANRSALLSQQ 608
Cdd:COG3206 296 LRAQIAALRAQLQQEAQRILASLEaeleALQAREASLQAQLAQLEARLAELPELE 350
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
453-573 |
7.27e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 453 TLDIRLKKLVDERECLLEQIKKLKGQLEERQK----IGKLDNLRSEDDVLEnGTDMHVMDLQRD-------------ANR 515
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQErreaLQRLAEYSWDEIDVA-SAEREIAELEAElerldassddlaaLEE 692
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622852877 516 QISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQREL 573
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
291-582 |
9.29e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 291 IREIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEK---YKKAMVSNAQLDNEKTNFmyqvdtlkdmlleleeqLAES 367
Cdd:PRK03918 327 EERIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRL-----------------TGLT 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 368 RRQYEEKNKEFEREKhahsilqfqfaevKEALKEREEMLEKHGIiLNSEIATNGETSDTLNNVGYQGP------TKMTKA 441
Cdd:PRK03918 386 PEKLEKELEELEKAK-------------EEIEEEISKITARIGE-LKKEIKELKKAIEELKKAKGKCPvcgrelTEEHRK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852877 442 ELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLK 521
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLK 531
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622852877 522 FKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 582
Cdd:PRK03918 532 EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| |
