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Conserved domains on  [gi|1622852885|ref|XP_028687109|]
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leucine-rich repeat flightless-interacting protein 1 isoform X22 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
162-491 1.59e-88

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: 275.42  E-value: 1.59e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 162 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSN 232
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 233 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEeirqlqqkq 312
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE--------- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 313 assireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHGIILNSEIATNGEtsdTLNNVGYQG 392
Cdd:pfam09738 181 -----------------------------------------------------KHGLVIVPDENTNGE---EENSPADAK 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 393 PTKMTKAELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRD 470
Cdd:pfam09738 205 RALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQRE 282
                         330       340
                  ....*....|....*....|.
gi 1622852885 471 ANRQISDLKFKLAKSEQEITA 491
Cdd:pfam09738 283 ANKQISDYKFKLQKAEQEITT 303
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
268-385 1.14e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


The actual alignment was detected with superfamily member COG2433:

Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 268 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 347
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622852885 348 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 385
Cdd:COG2433   458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
162-491 1.59e-88

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: 275.42  E-value: 1.59e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 162 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSN 232
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 233 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEeirqlqqkq 312
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE--------- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 313 assireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHGIILNSEIATNGEtsdTLNNVGYQG 392
Cdd:pfam09738 181 -----------------------------------------------------KHGLVIVPDENTNGE---EENSPADAK 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 393 PTKMTKAELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRD 470
Cdd:pfam09738 205 RALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQRE 282
                         330       340
                  ....*....|....*....|.
gi 1622852885 471 ANRQISDLKFKLAKSEQEITA 491
Cdd:pfam09738 283 ANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
185-541 1.62e-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: 57.76  E-value: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  185 TLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESR 264
Cdd:TIGR02168  653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  265 RQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEirqLQQKQASSIREISDLQETIewkdkkigalERQKEFFD 344
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQI----------EQLKEELK 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  345 SVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKAELNALKSTGDgTLDIRLKKLVDERE 424
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELE 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  425 CLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS 504
Cdd:TIGR02168  877 ALLNERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1622852885  505 -RYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 541
Cdd:TIGR02168  947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
289-515 2.44e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 289 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 368
Cdd:COG4942    41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 369 IILNSEIATNGETSDTLNNVG--YQGPTKMTKAELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 446
Cdd:COG4942   118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852885 447 DNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEK 515
Cdd:COG4942   191 EALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
268-385 1.14e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 268 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 347
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622852885 348 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 385
Cdd:COG2433   458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
208-559 1.44e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 208 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlLELEEQLAESRRQYEEKNKEFEREKHAH-SILQF 286
Cdd:PRK03918  390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGRELTEEHRKELLEEYTAElKRIEK 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 287 QFAEVKEALKEREEMLEEIRQLQQKQA--SSIREISDLQETIEWKDKKIGA--LERQKEFFDSVRSERDDLREEVVMLKE 362
Cdd:PRK03918  467 ELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 363 ELKKHGIILNSEIATN----------GETSDTLNNVGYqGPTKMTKAELNALKSTGDGTldIRLKKLVDERECLLEQIKK 432
Cdd:PRK03918  547 ELEKLEELKKKLAELEkkldeleeelAELLKELEELGF-ESVEELEERLKELEPFYNEY--LELKDAEKELEREEKELKK 623
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 433 LKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQNVIRLESQVSRYKSAAEN 512
Cdd:PRK03918  624 LEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEE 684
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1622852885 513 AEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 559
Cdd:PRK03918  685 LEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
287-366 4.86e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 39.67  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 287 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 364
Cdd:PRK05431   10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                  ..
gi 1622852885 365 KK 366
Cdd:PRK05431   90 DE 91
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
162-491 1.59e-88

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: 275.42  E-value: 1.59e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 162 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSN 232
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 233 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEeirqlqqkq 312
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE--------- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 313 assireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHGIILNSEIATNGEtsdTLNNVGYQG 392
Cdd:pfam09738 181 -----------------------------------------------------KHGLVIVPDENTNGE---EENSPADAK 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 393 PTKMTKAELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRD 470
Cdd:pfam09738 205 RALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQRE 282
                         330       340
                  ....*....|....*....|.
gi 1622852885 471 ANRQISDLKFKLAKSEQEITA 491
Cdd:pfam09738 283 ANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
185-541 1.62e-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: 57.76  E-value: 1.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  185 TLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESR 264
Cdd:TIGR02168  653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  265 RQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEirqLQQKQASSIREISDLQETIewkdkkigalERQKEFFD 344
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQI----------EQLKEELK 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  345 SVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKAELNALKSTGDgTLDIRLKKLVDERE 424
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELE 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  425 CLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS 504
Cdd:TIGR02168  877 ALLNERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1622852885  505 -RYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 541
Cdd:TIGR02168  947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
289-565 2.14e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  289 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGAL----ERQKEFFDSVRSERDDLREEVVMLKEEL 364
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVKSEL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  365 KKhgiiLNSEIAtngETSDTLNNVgyqgptkmtKAELNALKstgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKig 444
Cdd:TIGR02169  761 KE----LEARIE---ELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-- 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  445 KLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEK 524
Cdd:TIGR02169  820 KLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1622852885  525 RKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 565
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
289-565 5.15e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 5.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  289 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 368
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  369 IILNSEIATNGETSDTLNNvgyqgptkmtkaELNALKSTGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQK 442
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKE------------ELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  443 IGKldnlRSEDDVLEngtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKA 522
Cdd:TIGR02168  846 QIE----ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1622852885  523 EKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 565
Cdd:TIGR02168  909 KRSELRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
235-542 2.95e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 2.95e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  235 LDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQAS 314
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  315 sirEISDLQETIEWKDKKIGALERQ--KEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNN-VGYQ 391
Cdd:TIGR02169  766 ---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElQEQR 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  392 GPTKMTKAELNA---LKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDmhvmdlq 468
Cdd:TIGR02169  843 IDLKEQIKSIEKeieNLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA--QLRELERKIEELEAQIE------- 913
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  469 rDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA---AENAEKIE------------------------DELK 521
Cdd:TIGR02169  914 -KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedvQAELQRVEeeiralepvnmlaiqeyeevlkrlDELK 992
                          330       340
                   ....*....|....*....|.
gi 1622852885  522 AEKRKLQRELRSALDKTEELE 542
Cdd:TIGR02169  993 EKRAKLEEERKAILERIEEYE 1013
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
264-541 6.66e-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: 49.28  E-value: 6.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  264 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 339
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  340 KE----FFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgptkmTKAELNALKSTGDgTLDIR 415
Cdd:TIGR02168  318 LEeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE----------------LEAELEELESRLE-ELEEQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  416 LKKLVDERECLLEQIKKLKGQ---LEERQKIGKLDNLRSEDDVLENGTDMHVMDLQrDANRQISDLKFKLAKSEQEITAL 492
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELERL 459
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1622852885  493 EQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 541
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
289-563 6.94e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 6.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  289 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWK-------DKKIGALERQK----------------EFFDS 345
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEDLhkleealndlearlshSRIPE 795
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  346 VRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNN-VGYQGPTKMTKAELNA---LKSTGDGTLDIRLKKLVD 421
Cdd:TIGR02169  796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElQEQRIDLKEQIKSIEKeieNLNGKKEELEEELEELEA 875
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  422 ERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLES 501
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEA--QLRELERKIEELEAQIE--------KKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852885  502 QVSryksaaenAEKIEDELKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 563
Cdd:TIGR02169  946 IPE--------EELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
289-515 2.44e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.68  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 289 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 368
Cdd:COG4942    41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 369 IILNSEIATNGETSDTLNNVG--YQGPTKMTKAELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 446
Cdd:COG4942   118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852885 447 DNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEK 515
Cdd:COG4942   191 EALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
287-566 7.29e-05

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: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 287 QFAEVKEALKERE--EMLEEIRQLQQKQASSIREISDLQETIE----WKDKKIGALERQKEFFDSVRSERDDLREEVVML 360
Cdd:COG1196   214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEeleaELAELEAELEELRLELEELELELEEAQAEEYEL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 361 KEELKKHGIILNSEIATNGETSDTLNNvgyqgpTKMTKAELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEER 440
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEE------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 441 QKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDEL 520
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1622852885 521 KAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 566
Cdd:COG1196   448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
268-385 1.14e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 268 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 347
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1622852885 348 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 385
Cdd:COG2433   458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
279-534 1.50e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.44  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 279 HAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERqkeffdsvrsERDDLREEVV 358
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 359 MLKEELKKhgiiLNSEIATNGETSDTLNNVgyqgptkmtkaeLNAlKSTGD--GTLDIrLKKLVDERECLLEQIKKLKGQ 436
Cdd:COG3883    83 ERREELGE----RARALYRSGGSVSYLDVL------------LGS-ESFSDflDRLSA-LSKIADADADLLEELKADKAE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 437 LEERQKigKLDNLRSEddvlengtdmhVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKI 516
Cdd:COG3883   145 LEAKKA--ELEAKLAE-----------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
                         250
                  ....*....|....*...
gi 1622852885 517 EDELKAEKRKLQRELRSA 534
Cdd:COG3883   212 AAAAAAAAAAAAAAAAAA 229
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
264-522 3.10e-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: 43.90  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  264 RRQYEEKNKEFERekhAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkefF 343
Cdd:TIGR02169  307 ERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE---F 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  344 DSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVgyqgptkmtKAELNALKStgdgtldiRLKKLVDER 423
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL---------NAAIAGIEA--------KINELEEEK 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  424 ECLLEQIKKLKGQLEERQKIGKldnlrseddvlengtdmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLESQV 503
Cdd:TIGR02169  444 EDKALEIKKQEWKLEQLAADLS------------------------KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
                          250
                   ....*....|....*....
gi 1622852885  504 SRYKSAAENAEKIEDELKA 522
Cdd:TIGR02169  500 RASEERVRGGRAVEEVLKA 518
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
201-565 3.60e-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: 3.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  201 TSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQ-----------------LDNEK---TNFMYQVDTLKDMLLELEEQL 260
Cdd:pfam15921  485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEitklrsrvdlklqelqhLKNEGdhlRNVQTECEALKLQMAEKDKVI 564
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  261 AESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI--GALER 338
Cdd:pfam15921  565 EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnAGSER 644
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  339 QKEFFDsVRSERDDLREEVvmlkeelkkhgiilnseiatngetsdtlnnvgyqgptKMTKAELNALKSTgdgtLDIRLKK 418
Cdd:pfam15921  645 LRAVKD-IKQERDQLLNEV-------------------------------------KTSRNELNSLSED----YEVLKRN 682
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  419 LVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLEnGTDMHVMDLQRDANRQIsdlkfklakseqeiTALEQNVIR 498
Cdd:pfam15921  683 FRNKSEEMETTTNKLKMQLKSAQS--ELEQTRNTLKSME-GSDGHAMKVAMGMQKQI--------------TAKRGQIDA 745
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622852885  499 LESQVSRYKSAAENAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 565
Cdd:pfam15921  746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
309-562 4.34e-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: 42.83  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 309 QQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKhgiilnseiatngetsdtlnnv 388
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA---------------------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 389 gyqgptkmTKAELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLrsedDVLENGTDMhv 464
Cdd:COG4942    74 --------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL----ALLLSPEDF-- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 465 mdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVS 544
Cdd:COG4942   132 ----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
                         250
                  ....*....|....*...
gi 1622852885 545 NGHLVKRLEKMKANRSAL 562
Cdd:COG4942   208 LAELAAELAELQQEAEEL 225
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
266-557 4.44e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 4.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  266 QYEEKNKEFEREKHAHSILQFQFAEvkealKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALER-----QK 340
Cdd:TIGR02168  214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEeieelQK 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  341 EFFdSVRSERDDLREEVVMLKEELKKhgiiLNSEIatngetsdtlnnvgyqgptKMTKAELNALKSTGDgtldiRLKKLV 420
Cdd:TIGR02168  289 ELY-ALANEISRLEQQKQILRERLAN----LERQL-------------------EELEAQLEELESKLD-----ELAEEL 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  421 DERECLLEQIKKLKGQLEErqkigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLE 500
Cdd:TIGR02168  340 AELEEKLEELKEELESLEA-----ELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622852885  501 SQVSRYKSAAENA-EKIEDELK----AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 557
Cdd:TIGR02168  407 ARLERLEDRRERLqQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEALEELRE 468
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
268-458 4.87e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 268 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 347
Cdd:COG4717    53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 348 sERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGptKMTKAELNALKSTGDGTLDIRLKKLVDERECLL 427
Cdd:COG4717   133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1622852885 428 EQIKKLKGQLEERQKigKLDNLRSEDDVLEN 458
Cdd:COG4717   206 QRLAELEEELEEAQE--ELEELEEELEQLEN 234
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
293-529 5.08e-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: 43.13  E-value: 5.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  293 EALKEREEMLE---EIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFD----SVRSERDDLREEVVMLKEELK 365
Cdd:TIGR02169  288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  366 KHGIILNSEIATNGETSDTLnnVGYQGPTKMTKAELNALKSTGDGTLDiRLKKLVDERECLLEQIKKLKGQLEERqkigk 445
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDEL--KDYREKLEKLKREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINEL----- 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  446 ldnlrseDDVLEngtdmhvmdlqrdanrqisDLKFKLAKSEQEITALEQNVIRLESQVSRYKsaaENAEKIEDELKAEKR 525
Cdd:TIGR02169  440 -------EEEKE-------------------DKALEIKKQEWKLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQR 490

                   ....
gi 1622852885  526 KLQR 529
Cdd:TIGR02169  491 ELAE 494
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
287-557 6.19e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 6.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  287 QFAEVKEA------LKEREEMLEEIRQLQQKQASSIREISDLQETIEWkdkkiGALERQKEFFDSVRSERDDLREEVVML 360
Cdd:COG4913    233 HFDDLERAhealedAREQIELLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARL 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  361 KEELKkhgiilnseiatngetsdtlnnvgyqgptkmtkaelnalkstgdgTLDIRLKKLVDERECLLEQIKKLKGQleer 440
Cdd:COG4913    308 EAELE---------------------------------------------RLEARLDALREELDELEAQIRGNGGD---- 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  441 qkigKLDNLRSEDDVLENGTDmHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAekiEDEL 520
Cdd:COG4913    339 ----RLEQLEREIERLERELE-ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LAEA 410
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1622852885  521 KAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 557
Cdd:COG4913    411 EAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
289-542 1.02e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 289 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 368
Cdd:COG1340     8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 369 IILNSEIATNGETSDTLNNVGYQGPTKMT-KAELNALKSTGDgTLDIRLKKlvdEREcLLEQIKKLKGQLEERQKI---- 443
Cdd:COG1340    85 EKLNELREELDELRKELAELNKAGGSIDKlRKEIERLEWRQQ-TEVLSPEE---EKE-LVEKIKELEKELEKAKKAlekn 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 444 GKLDNLRSEDDVLENGTDMHVMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAE 523
Cdd:COG1340   160 EKLKELRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
                         250
                  ....*....|....*....
gi 1622852885 524 KRKLQRELRSALDKTEELE 542
Cdd:COG1340   239 LRELRKELKKLRKKQRALK 257
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
289-562 1.12e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  289 AEVKEALKEREEMLEEIRQLQQK------QASSIREISDLQETIEWKD--KKIGALERQKEffdSVRSERDDLREEVVML 360
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERlrrereKAERYQALLKEKREYEGYEllKEKEALERQKE---AIERQLASLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  361 KEELKKhgiiLNSEIATNGETSDTLN------NVGYQGPTKMTKAELNALKSTGDGT----------LDIRLKKLVDERE 424
Cdd:TIGR02169  257 TEEISE----LEKRLEEIEQLLEELNkkikdlGEEEQLRVKEKIGELEAEIASLERSiaekereledAEERLAKLEAEID 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  425 CLLEQIKKLKGQLEERQK-----IGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISDLKFKLAKSEQEITALE 493
Cdd:TIGR02169  333 KLLAEIEELEREIEEERKrrdklTEEYAELKEELEDLRAeleevdKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852885  494 QNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 562
Cdd:TIGR02169  413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
208-559 1.44e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 208 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlLELEEQLAESRRQYEEKNKEFEREKHAH-SILQF 286
Cdd:PRK03918  390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGRELTEEHRKELLEEYTAElKRIEK 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 287 QFAEVKEALKEREEMLEEIRQLQQKQA--SSIREISDLQETIEWKDKKIGA--LERQKEFFDSVRSERDDLREEVVMLKE 362
Cdd:PRK03918  467 ELKEIEEKERKLRKELRELEKVLKKESelIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 363 ELKKHGIILNSEIATN----------GETSDTLNNVGYqGPTKMTKAELNALKSTGDGTldIRLKKLVDERECLLEQIKK 432
Cdd:PRK03918  547 ELEKLEELKKKLAELEkkldeleeelAELLKELEELGF-ESVEELEERLKELEPFYNEY--LELKDAEKELEREEKELKK 623
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 433 LKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQNVIRLESQVSRYKSAAEN 512
Cdd:PRK03918  624 LEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEE 684
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1622852885 513 AEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 559
Cdd:PRK03918  685 LEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
397-562 1.53e-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: 41.58  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  397 TKAELNALKSTgdgtLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQIS 476
Cdd:TIGR02168  696 LEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  477 DLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 556
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851

                   ....*.
gi 1622852885  557 ANRSAL 562
Cdd:TIGR02168  852 EDIESL 857
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
303-561 3.15e-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: 40.13  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 303 EEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkeffdsvrseRDDLREEVVMLKEELKKhgiilnseiatngets 382
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----------LAALERRIAALARRIRA---------------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 383 dtlnnvgyqgptkmTKAELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLR---SEDDV 455
Cdd:COG4942    74 --------------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPLAlllSPEDF 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 456 LENGTDMHVMD-LQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSA 534
Cdd:COG4942   132 LDAVRRLQYLKyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
                         250       260
                  ....*....|....*....|....*..
gi 1622852885 535 LDKTEELEVSNGHLVKRLEKMKANRSA 561
Cdd:COG4942   212 AAELAELQQEAEELEALIARLEAEAAA 238
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
287-366 4.86e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 39.67  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 287 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 364
Cdd:PRK05431   10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                  ..
gi 1622852885 365 KK 366
Cdd:PRK05431   90 DE 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
206-355 5.76e-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: 39.65  E-value: 5.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  206 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLkdmllelEEQLAESRRQYEEKNKEFEREKHAHSILQ 285
Cdd:TIGR02168  863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL-------ESKRSELRRELEELREKLAQLELRLEGLE 935
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622852885  286 FQFAEVKEALKEREEM-LEEIRQLQQKQASSIREISDLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 355
Cdd:TIGR02168  936 VRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
415-566 5.96e-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: 39.65  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  415 RLKKLVDERECLLEQIKKLKGQLEE-----RQKIGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISDLKFKLA 483
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEEltaelQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885  484 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALL 563
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                   ...
gi 1622852885  564 SQQ 566
Cdd:TIGR02168  393 LQI 395
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
412-540 6.28e-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: 38.37  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 412 LDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMHVMDLQRD--------ANRQISDLKFKLA 483
Cdd:COG1579    22 LEHRLKELPAELAELEDELAALEARLEAAKT--ELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEALQKEIE 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622852885 484 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 540
Cdd:COG1579   100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
265-566 9.08e-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: 38.85  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 265 RQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEE--IRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEf 342
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS- 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 343 fdSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVgyqgptkmtKAELNALKSTGDGT------LDIRL 416
Cdd:TIGR04523 346 --QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL---------ESQINDLESKIQNQeklnqqKDEQI 414
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 417 KKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMH----------VMDLQRDANRQISDLKFK---LA 483
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNS--EIKDLTNQDSVKELIIKNLdntresletqLKVLSRSINKIKQNLEQKqkeLK 492
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622852885 484 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALD---------KTEELEVSNGHLVKRLEK 554
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEE 572
                         330
                  ....*....|..
gi 1622852885 555 MKANRSALLSQQ 566
Cdd:TIGR04523 573 LKQTQKSLKKKQ 584
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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