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Conserved domains on  [gi|2462578511|ref|XP_054200518|]
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leucine-rich repeat flightless-interacting protein 1 isoform X36 [Homo sapiens]

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 ...
52-445 5.00e-90

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: 278.12  E-value: 5.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  52 MKELERQQKEIyqvqkkyygldtkwgdieqwmedserysrrsrrntsaSDEDERMSVGSRGSLRVeerpekdfTEKGSRN 131
Cdd:pfam09738  20 MRELERQQKEV-------------------------------------EENADRVFDMSSSSGAD--------TASGSPT 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 132 MPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELE 211
Cdd:pfam09738  55 ASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEME 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 212 EQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEeirqlqqkqassireisdlqetiewkdkkigale 291
Cdd:pfam09738 135 ESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE---------------------------------- 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 292 rqkeffdsvrserddlreevvmlkeelkKHGIILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLK 371
Cdd:pfam09738 181 ----------------------------KHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLK 229
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578511 372 KLVDERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 445
Cdd:pfam09738 230 KLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
222-339 1.29e-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: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 222 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 301
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462578511 302 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 339
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 ...
52-445 5.00e-90

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: 278.12  E-value: 5.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  52 MKELERQQKEIyqvqkkyygldtkwgdieqwmedserysrrsrrntsaSDEDERMSVGSRGSLRVeerpekdfTEKGSRN 131
Cdd:pfam09738  20 MRELERQQKEV-------------------------------------EENADRVFDMSSSSGAD--------TASGSPT 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 132 MPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELE 211
Cdd:pfam09738  55 ASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEME 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 212 EQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEeirqlqqkqassireisdlqetiewkdkkigale 291
Cdd:pfam09738 135 ESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE---------------------------------- 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 292 rqkeffdsvrserddlreevvmlkeelkKHGIILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLK 371
Cdd:pfam09738 181 ----------------------------KHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLK 229
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578511 372 KLVDERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 445
Cdd:pfam09738 230 KLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
139-495 5.36e-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: 55.83  E-value: 5.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  139 TLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESR 218
Cdd:TIGR02168  653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  219 RQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEirqLQQKQASSIREISDLQETIewkdkkigalERQKEFFD 298
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQI----------EQLKEELK 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  299 SVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKEELNALKSTGDgTLDIRLKKLVDERE 378
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELE 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  379 CLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS 458
Cdd:TIGR02168  877 ALLNERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2462578511  459 -RYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 495
Cdd:TIGR02168  947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
243-469 5.38e-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: 45.53  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 243 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 322
Cdd:COG4942    41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 323 IILNSEIATNGETSDTLNNVG--YQGPTKMTKEELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 400
Cdd:COG4942   118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578511 401 DNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEK 469
Cdd:COG4942   191 EALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
222-339 1.29e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 222 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 301
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462578511 302 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 339
Cdd:COG2433   458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
241-320 3.46e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 39.67  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 241 QFAEVKEALKQR--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 318
Cdd:PRK05431   10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                  ..
gi 2462578511 319 KK 320
Cdd:PRK05431   90 DE 91
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
162-513 8.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 8.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 162 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlLELEEQLAESRRQYEEKNKEFEREKHAH-SILQF 240
Cdd:PRK03918  390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGRELTEEHRKELLEEYTAElKRIEK 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 241 QFAEVKEALKQREEMLEEIRQL--QQKQASSIREISDLQETIEWKDKKIGA--LERQKEFFDSVRSERDDLREEVVMLKE 316
Cdd:PRK03918  467 ELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 317 ELKKHGIILNSEIATN----------GETSDTLNNVGYqGPTKMTKEELNALKSTGDGTldIRLKKLVDERECLLEQIKK 386
Cdd:PRK03918  547 ELEKLEELKKKLAELEkkldeleeelAELLKELEELGF-ESVEELEERLKELEPFYNEY--LELKDAEKELEREEKELKK 623
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 387 LKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQNVIRLESQVSRYKSAAEN 466
Cdd:PRK03918  624 LEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEE 684
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2462578511 467 AEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 513
Cdd:PRK03918  685 LEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
52-445 5.00e-90

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: 278.12  E-value: 5.00e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  52 MKELERQQKEIyqvqkkyygldtkwgdieqwmedserysrrsrrntsaSDEDERMSVGSRGSLRVeerpekdfTEKGSRN 131
Cdd:pfam09738  20 MRELERQQKEV-------------------------------------EENADRVFDMSSSSGAD--------TASGSPT 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 132 MPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELE 211
Cdd:pfam09738  55 ASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEME 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 212 EQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEeirqlqqkqassireisdlqetiewkdkkigale 291
Cdd:pfam09738 135 ESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE---------------------------------- 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 292 rqkeffdsvrserddlreevvmlkeelkKHGIILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLK 371
Cdd:pfam09738 181 ----------------------------KHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLK 229
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578511 372 KLVDERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 445
Cdd:pfam09738 230 KLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
139-495 5.36e-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: 55.83  E-value: 5.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  139 TLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESR 218
Cdd:TIGR02168  653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  219 RQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEirqLQQKQASSIREISDLQETIewkdkkigalERQKEFFD 298
Cdd:TIGR02168  733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQI----------EQLKEELK 799
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  299 SVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKEELNALKSTGDgTLDIRLKKLVDERE 378
Cdd:TIGR02168  800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELE 876
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  379 CLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS 458
Cdd:TIGR02168  877 ALLNERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 2462578511  459 -RYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 495
Cdd:TIGR02168  947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
243-519 1.39e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  243 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGAL----ERQKEFFDSVRSERDDLREEVVMLKEEL 318
Cdd:TIGR02169  681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVKSEL 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  319 KKhgiiLNSEIAtngETSDTLNNVgyqgptkmtKEELNALKstgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKig 398
Cdd:TIGR02169  761 KE----LEARIE---ELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQ-- 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  399 KLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEK 478
Cdd:TIGR02169  820 KLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2462578511  479 RKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 519
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
243-519 1.42e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 1.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  243 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 322
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  323 IILNSEIATNGETSDTLnnvgyqgptkmtKEELNALKSTGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQK 396
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQL------------KEELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  397 IGKldnlRSEDDVLEngtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKA 476
Cdd:TIGR02168  846 QIE----ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 2462578511  477 EKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 519
Cdd:TIGR02168  909 KRSELRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
189-496 1.29e-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: 48.14  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  189 LDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQAS 268
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  269 sirEISDLQETIEWKDKKIGALERQ--KEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVgyQG 346
Cdd:TIGR02169  766 ---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL--QE 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  347 PTKMTKEELNALKSTGDgTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMHVMDLQRdAN 426
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDLKK--ERDELEAQLRELERKIEELEAQIEK-KR 916
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  427 RQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIE---------------------------DELKAEKR 479
Cdd:TIGR02169  917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQrveeeiralepvnmlaiqeyeevlkrlDELKEKRA 996
                          330
                   ....*....|....*..
gi 2462578511  480 KLQRELRSALDKTEELE 496
Cdd:TIGR02169  997 KLEEERKAILERIEEYE 1013
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
243-517 3.21e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 3.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  243 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWK-------DKKIGALER-----QKEFFDSVRSERDDLREE 310
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEdlhklEEALNDLEARLSHSRIPE 795
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  311 VVMLKEELKK-HGIILNSEIATNGETSDTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLkg 389
Cdd:TIGR02169  796 IQAELSKLEEeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL-- 873
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  390 QLEERQKIGKLDNLRSEDDVLENgtDMHVM-DLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAE 468
Cdd:TIGR02169  874 EAALRDLESRLGDLKKERDELEA--QLRELeRKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462578511  469 KIEDeLKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 517
Cdd:TIGR02169  952 SLED-VQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
218-495 4.02e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 4.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  218 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 293
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  294 KE----FFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgpTKMTKEELNALKStgdgTLDIR 369
Cdd:TIGR02168  318 LEeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE-------------LEAELEELESRLE----ELEEQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  370 LKKLVDERECLLEQIKKLKGQ---LEERQKIGKLDNLRSEDDVLENGTDMHVMDLQrDANRQISDLKFKLAKSEQEITAL 446
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELERL 459
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 2462578511  447 EQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 495
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
243-469 5.38e-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: 45.53  E-value: 5.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 243 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 322
Cdd:COG4942    41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 323 IILNSEIATNGETSDTLNNVG--YQGPTKMTKEELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 400
Cdd:COG4942   118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578511 401 DNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEK 469
Cdd:COG4942   191 EALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
222-339 1.29e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.85  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 222 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 301
Cdd:COG2433   388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462578511 302 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 339
Cdd:COG2433   458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
241-520 2.27e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 241 QFAEVKEALKQRE--EMLEEIRQLQQKQASSIREISDLQETIE----WKDKKIGALERQKEFFDSVRSERDDLREEVVML 314
Cdd:COG1196   214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEeleaELAELEAELEELRLELEELELELEEAQAEEYEL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 315 KEELKKHGIILNSEIATNGETSDTLNNvgyqgpTKMTKEELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEER 394
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEE------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 395 QKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDEL 474
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2462578511 475 KAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 520
Cdd:COG1196   448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
233-488 4.79e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 233 HAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERqkeffdsvrsERDDLREEVV 312
Cdd:COG3883    13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 313 MLKEELKKhgiiLNSEIATNGETSDTLNNVgyqgptkmtkeeLNAlKSTGD--GTLDIrLKKLVDERECLLEQIKKLKGQ 390
Cdd:COG3883    83 ERREELGE----RARALYRSGGSVSYLDVL------------LGS-ESFSDflDRLSA-LSKIADADADLLEELKADKAE 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 391 LEERQKigKLDNLRSEddvlengtdmhVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKI 470
Cdd:COG3883   145 LEAKKA--ELEAKLAE-----------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
                         250
                  ....*....|....*...
gi 2462578511 471 EDELKAEKRKLQRELRSA 488
Cdd:COG3883   212 AAAAAAAAAAAAAAAAAA 229
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
247-483 6.79e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 6.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  247 EALKQREEMLE---EIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFD----SVRSERDDLREEVVMLKEELK 319
Cdd:TIGR02169  288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  320 KHGIILNSEIATNGETSDTLnnVGYQGPTKMTKEELNALKSTGDGTLDiRLKKLVDERECLLEQIKKLKGQLEERqkigk 399
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDEL--KDYREKLEKLKREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINEL----- 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  400 ldnlrseDDVLEngtdmhvmdlqrdanrqisDLKFKLAKSEQEITALEQNVIRLESQVSRYKsaaENAEKIEDELKAEKR 479
Cdd:TIGR02169  440 -------EEEKE-------------------DKALEIKKQEWKLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQR 490

                   ....
gi 2462578511  480 KLQR 483
Cdd:TIGR02169  491 ELAE 494
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
244-511 1.68e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  244 EVKEALKQREeMLEEIRQLQQKQASSIREISDLQETIEWkdkkiGALERQKEFFDSVRSERDDLREEVVMLKEELKkhgi 323
Cdd:COG4913    243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELE---- 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  324 ilnseiatngetsdtlnnvgyqgptkmtkeelnalkstgdgTLDIRLKKLVDERECLLEQIKKLKGQleerqkigKLDNL 403
Cdd:COG4913    313 -----------------------------------------RLEARLDALREELDELEAQIRGNGGD--------RLEQL 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  404 RSEDDVLENGTDmHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAekiEDELKAEKRKLQR 483
Cdd:COG4913    344 EREIERLERELE-ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRR 419
                          250       260
                   ....*....|....*....|....*...
gi 2462578511  484 ELRSALDKTEELEVSNGHLVKRLEKMKA 511
Cdd:COG4913    420 ELRELEAEIASLERRKSNIPARLLALRD 447
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
263-516 1.74e-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: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 263 QQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKhgiilnseiatngetsdtlnnv 342
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA---------------------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 343 gyqgptkmTKEELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLrsedDVLENGTDMhv 418
Cdd:COG4942    74 --------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL----ALLLSPEDF-- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 419 mdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVS 498
Cdd:COG4942   132 ----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
                         250
                  ....*....|....*...
gi 2462578511 499 NGHLVKRLEKMKANRSAL 516
Cdd:COG4942   208 LAELAAELAELQQEAEEL 225
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
222-412 2.17e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 222 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 301
Cdd:COG4717    53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 302 sERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGptKMTKEELNALKSTGDGTLDIRLKKLVDERECLL 381
Cdd:COG4717   133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2462578511 382 EQIKKLKGQLEERQKigKLDNLRSEDDVLEN 412
Cdd:COG4717   206 QRLAELEEELEEAQE--ELEELEEELEQLEN 234
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
218-476 2.79e-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: 40.44  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  218 RRQYEEKNKEFERekhAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkefF 297
Cdd:TIGR02169  307 ERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE---F 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  298 DSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVgyqgptkmtKEELNALKStgdgtldiRLKKLVDER 377
Cdd:TIGR02169  381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL---------NAAIAGIEA--------KINELEEEK 443
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  378 ECLLEQIKKLKGQLEERQKIGKldnlrseddvlengtdmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLESQV 457
Cdd:TIGR02169  444 EDKALEIKKQEWKLEQLAADLS------------------------KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
                          250
                   ....*....|....*....
gi 2462578511  458 SRYKSAAENAEKIEDELKA 476
Cdd:TIGR02169  500 RASEERVRGGRAVEEVLKA 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
220-511 2.99e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  220 QYEEKNKEFEREKHAHSILQFQFAEvkealKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALER-----QK 294
Cdd:TIGR02168  214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEeieelQK 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  295 EFFdSVRSERDDLREEVVMLKEELK---KHGIILNSEIATNGETSDTLnnvgyqgptkmtKEELNALKstgdgtldirlk 371
Cdd:TIGR02168  289 ELY-ALANEISRLEQQKQILRERLAnleRQLEELEAQLEELESKLDEL------------AEELAELE------------ 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  372 klvderecllEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVI 451
Cdd:TIGR02168  344 ----------EKLEELKEELESLEA--ELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIE 403
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578511  452 RLESQVSRYKSAAENA-EKIEDELK----AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 511
Cdd:TIGR02168  404 RLEARLERLEDRRERLqQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEALEELRE 468
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
155-519 3.36e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  155 TSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKT--------------------NFMYQVDTLKDMLLELEEQL 214
Cdd:pfam15921  485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvdlklqelqhlknegdhlrNVQTECEALKLQMAEKDKVI 564
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  215 AESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI--GALER 292
Cdd:pfam15921  565 EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnAGSER 644
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  293 QKEFFDsVRSERDDLREEVvmlkeelkkhgiilnseiatngetsdtlnnvgyqgptKMTKEELNALKSTgdgtLDIRLKK 372
Cdd:pfam15921  645 LRAVKD-IKQERDQLLNEV-------------------------------------KTSRNELNSLSED----YEVLKRN 682
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  373 LVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLEnGTDMHVMDLQRDANRQIsdlkfklakseqeiTALEQNVIR 452
Cdd:pfam15921  683 FRNKSEEMETTTNKLKMQLKSAQS--ELEQTRNTLKSME-GSDGHAMKVAMGMQKQI--------------TAKRGQIDA 745
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578511  453 LESQVSRYKSAAENAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 519
Cdd:pfam15921  746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
241-320 3.46e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 39.67  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 241 QFAEVKEALKQR--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 318
Cdd:PRK05431   10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                  ..
gi 2462578511 319 KK 320
Cdd:PRK05431   90 DE 91
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
351-516 4.87e-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: 4.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  351 TKEELNALKSTgdgtLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQIS 430
Cdd:TIGR02168  696 LEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  431 DLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 510
Cdd:TIGR02168  772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851

                   ....*.
gi 2462578511  511 ANRSAL 516
Cdd:TIGR02168  852 EDIESL 857
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
243-496 7.14e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 7.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 243 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 322
Cdd:COG1340     8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 323 IILNSEIATNGETSDTLNNVGYQGPTKMT-KEELNALKSTGDgTLDIRLKKlvdEREcLLEQIKKLKGQLEERQKI---- 397
Cdd:COG1340    85 EKLNELREELDELRKELAELNKAGGSIDKlRKEIERLEWRQQ-TEVLSPEE---EKE-LVEKIKELEKELEKAKKAlekn 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 398 GKLDNLRSEDDVLENGTDMHVMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAE 477
Cdd:COG1340   160 EKLKELRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
                         250
                  ....*....|....*....
gi 2462578511 478 KRKLQRELRSALDKTEELE 496
Cdd:COG1340   239 LRELRKELKKLRKKQRALK 257
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
248-446 7.48e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 7.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  248 ALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF------DSVRSERDDLREEVVMLKEElkkh 321
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS---- 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511  322 giilNSEIATNGETSDTLnnvgyqgptkmtKEELNALKSTGDGtLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKL- 400
Cdd:COG4913    684 ----SDDLAALEEQLEEL------------EAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLe 746
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2462578511  401 DNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITAL 446
Cdd:COG4913    747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
162-513 8.13e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 8.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 162 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlLELEEQLAESRRQYEEKNKEFEREKHAH-SILQF 240
Cdd:PRK03918  390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGRELTEEHRKELLEEYTAElKRIEK 466
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 241 QFAEVKEALKQREEMLEEIRQL--QQKQASSIREISDLQETIEWKDKKIGA--LERQKEFFDSVRSERDDLREEVVMLKE 316
Cdd:PRK03918  467 ELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 317 ELKKHGIILNSEIATN----------GETSDTLNNVGYqGPTKMTKEELNALKSTGDGTldIRLKKLVDERECLLEQIKK 386
Cdd:PRK03918  547 ELEKLEELKKKLAELEkkldeleeelAELLKELEELGF-ESVEELEERLKELEPFYNEY--LELKDAEKELEREEKELKK 623
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578511 387 LKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQNVIRLESQVSRYKSAAEN 466
Cdd:PRK03918  624 LEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEE 684
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2462578511 467 AEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 513
Cdd:PRK03918  685 LEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
 
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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