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Conserved domains on  [gi|212276078|ref|NP_001131022|]
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leucine-rich repeat flightless-interacting protein 1 isoform 1 [Homo sapiens]

Protein Classification

leucine-rich repeat flightless-interacting protein( domain architecture ID 12101455)

leucine-rich repeat flightless-interacting protein (LRRFIP) similar to human LRRFIP2 that may function as activator of the canonical Wnt signaling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin

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 ...
212-565 8.06e-87

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: 273.11  E-value: 8.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  212 VEERPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 282
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  283 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 362
Cdd:pfam09738  93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  363 AEVKEALKQREEMLEeirqlqqkqassireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHG 442
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  443 IILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKL 520
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 212276078  521 DNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 565
Cdd:pfam09738 261 SSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
342-459 5.72e-05

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: 46.39  E-value: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 342 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 421
Cdd:COG2433  388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 212276078 422 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 459
Cdd:COG2433  458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
DUF3450 super family cl26418
Protein of unknown function (DUF3450); This family of proteins are functionally ...
581-640 7.73e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


The actual alignment was detected with superfamily member pfam11932:

Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 38.37  E-value: 7.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  581 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:pfam11932  27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
212-565 8.06e-87

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: 273.11  E-value: 8.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  212 VEERPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 282
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  283 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 362
Cdd:pfam09738  93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  363 AEVKEALKQREEMLEeirqlqqkqassireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHG 442
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  443 IILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKL 520
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 212276078  521 DNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 565
Cdd:pfam09738 261 SSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
262-615 1.28e-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: 58.14  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   262 REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESRRQY 341
Cdd:TIGR02168  677 REIEELEEK--------------IEELEEKIAELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   342 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEirqLQQKQASSIREISDLQETIewkdkkigalERQKEFFDSVR 421
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQI----------EQLKEELKALR 802
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   422 SERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKEELNALKSTGDgTLDIRLKKLVDERECLL 501
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELEALL 879
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   502 EQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-RY 580
Cdd:TIGR02168  880 NERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEY 949
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 212276078   581 KSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 615
Cdd:TIGR02168  950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
363-589 6.51e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 6.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 363 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 442
Cdd:COG4942   41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 443 IILNSEIATNGETSDTLNNVG--YQGPTKMTKEELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 520
Cdd:COG4942  118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212276078 521 DNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEK 589
Cdd:COG4942  191 EALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
265-633 2.80e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 265 KELNELKDQIQDVE-GKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlLELEEQLAESRRQYEE 343
Cdd:PRK03918 372 EELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGRELTEE 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 344 KNKEFEREKHAH-SILQFQFAEVKEALKQREEMLEEIRQL--QQKQASSIREISDLQETIEWKDKKIGA--LERQKEFFD 418
Cdd:PRK03918 449 HRKELLEEYTAElKRIEKELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYE 528
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 419 SVRSERDDLREEVVMLKEELKKHGIILNSEIATN----------GETSDTLNNVGYqGPTKMTKEELNALKSTGDGTldI 488
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEkkldeleeelAELLKELEELGF-ESVEELEERLKELEPFYNEY--L 605
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 489 RLKKLVDERECLLEQIKKLKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQ 568
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELRE 666
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212276078 569 NVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 633
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
342-459 5.72e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.39  E-value: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 342 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 421
Cdd:COG2433  388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 212276078 422 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 459
Cdd:COG2433  458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
361-440 3.14e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.44  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 361 QFAEVKEALKQR--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 438
Cdd:PRK05431  10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                 ..
gi 212276078 439 KK 440
Cdd:PRK05431  90 DE 91
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
581-640 7.73e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 38.37  E-value: 7.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  581 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:pfam11932  27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
212-565 8.06e-87

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: 273.11  E-value: 8.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  212 VEERPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 282
Cdd:pfam09738  30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  283 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 362
Cdd:pfam09738  93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  363 AEVKEALKQREEMLEeirqlqqkqassireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHG 442
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  443 IILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKL 520
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 212276078  521 DNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 565
Cdd:pfam09738 261 SSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
262-615 1.28e-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: 58.14  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   262 REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESRRQY 341
Cdd:TIGR02168  677 REIEELEEK--------------IEELEEKIAELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL 735
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   342 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEirqLQQKQASSIREISDLQETIewkdkkigalERQKEFFDSVR 421
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQI----------EQLKEELKALR 802
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   422 SERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKEELNALKSTGDgTLDIRLKKLVDERECLL 501
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELEALL 879
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   502 EQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-RY 580
Cdd:TIGR02168  880 NERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEY 949
                          330       340       350
                   ....*....|....*....|....*....|....*
gi 212276078   581 KSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 615
Cdd:TIGR02168  950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
361-639 4.35e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 56.61  E-value: 4.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   361 QFAEVKEALK-QREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGAL----ERQKEFFDSVRSERDDLREEVVMLK 435
Cdd:TIGR02169  678 RLRERLEGLKrELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVK 757
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   436 EELKKhgiiLNSEIAtngETSDTLNNVgyqgptkmtKEELNALKstgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ 515
Cdd:TIGR02169  758 SELKE----LEARIE---ELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   516 KigKLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELK 595
Cdd:TIGR02169  819 Q--KLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 212276078   596 AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 639
Cdd:TIGR02169  889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
363-639 5.04e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 5.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   363 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkefFDSVRSERDDLREEVVMLKEELKKhg 442
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   443 iiLNSEIATNGETSDTLnnvgyQGPTKMTKEELNALKSTGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQK 516
Cdd:TIGR02168  773 --AEEELAEAEAEIEEL-----EAQIEQLKEELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   517 IGKldnlRSEDDVLEngtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKA 596
Cdd:TIGR02168  846 QIE----ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 212276078   597 EKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 639
Cdd:TIGR02168  909 KRSELRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
309-616 4.45e-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: 53.15  E-value: 4.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   309 LDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQAS 388
Cdd:TIGR02169  686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   389 sirEISDLQETIEWKDKKIGALERQ--KEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVgyQG 466
Cdd:TIGR02169  766 ---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL--QE 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   467 PTKMTKEELNALKSTGDgTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMHVMDLQRdAN 546
Cdd:TIGR02169  841 QRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDLKK--ERDELEAQLRELERKIEELEAQIEK-KR 916
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   547 RQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA---AENAEKIE------------------------DELKAEKR 599
Cdd:TIGR02169  917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedvQAELQRVEeeiralepvnmlaiqeyeevlkrlDELKEKRA 996
                          330
                   ....*....|....*..
gi 212276078   600 KLQRELRSALDKTEELE 616
Cdd:TIGR02169  997 KLEEERKAILERIEEYE 1013
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
363-637 1.00e-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: 51.99  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   363 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWK-------DKKIGALER-----QKEFFDSVRSERDDLREE 430
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEdlhklEEALNDLEARLSHSRIPE 795
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   431 VVMLKEELKK-HGIILNSEIATNGETSDTLNNVGYQGPTKMTKEELNALkstgdgtLDIRLKKLVDERECLLEQIKKLKG 509
Cdd:TIGR02169  796 IQAELSKLEEeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-------LKEQIKSIEKEIENLNGKKEELEE 868
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   510 QLEE-----RQKIGKLDNLRSEDDVLENgtDMHVM-DLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA 583
Cdd:TIGR02169  869 ELEEleaalRDLESRLGDLKKERDELEA--QLRELeRKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212276078   584 AENAEKIEDeLKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 637
Cdd:TIGR02169  947 PEEELSLED-VQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
338-615 2.04e-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: 2.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 413
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   414 KE----FFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgpTKMTKEELNALKStgdgTLDIR 489
Cdd:TIGR02168  318 LEeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE-------------LEAELEELESRLE----ELEEQ 380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   490 LKKLVDERECLLEQIKKLKGQ---LEERQKIGKLDNLRSEDDVLENGTDMHVMDLQrDANRQISDLKFKLAKSEQEITAL 566
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELERL 459
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 212276078   567 EQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 615
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
363-589 6.51e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 6.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 363 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 442
Cdd:COG4942   41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 443 IILNSEIATNGETSDTLNNVG--YQGPTKMTKEELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 520
Cdd:COG4942  118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212276078 521 DNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEK 589
Cdd:COG4942  191 EALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
265-639 1.09e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.48  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  265 KELNELKDQIQDVEGKYMQGL-KEMKDSLAEVEEKYKkamvsnaQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEE 343
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  344 KNKEFErEKHAhsilqfqfaEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSE 423
Cdd:TIGR04523 361 KQRELE-EKQN---------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---LLEKE 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  424 RDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGPTKM--TKEELNALKSTGDgtldiRLKKLVDERECLL 501
Cdd:TIGR04523 428 IERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNTRESLETQLkvLSRSINKIKQNLE-----QKQKELKSKEKEL 498
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  502 EQIKKLKGQLEERQK---------IGKLDNLRSEDDVLENGTDmhvmDLQRDANRQISDLKFKLAksEQEITALEQNVIR 572
Cdd:TIGR04523 499 KKLNEEKKELEEKVKdltkkisslKEKIEKLESEKKEKESKIS----DLEDELNKDDFELKKENL--EKEIDEKNKEIEE 572
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212276078  573 LESQVSRYKSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 639
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSI 632
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
363-616 1.63e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.21  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 363 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 442
Cdd:COG1340    8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 443 IILNSEIATNGETSDTLNNVGYQGPTKMT-KEELNALKSTGDgTLDIRLKKlvdEREcLLEQIKKLKGQLEERQKI---- 517
Cdd:COG1340   85 EKLNELREELDELRKELAELNKAGGSIDKlRKEIERLEWRQQ-TEVLSPEE---EKE-LVEKIKELEKELEKAKKAlekn 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 518 GKLDNLRSEDDVLENGTDMHVMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAE 597
Cdd:COG1340  160 EKLKELRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
                        250
                 ....*....|....*....
gi 212276078 598 KRKLQRELRSALDKTEELE 616
Cdd:COG1340  239 LRELRKELKKLRKKQRALK 257
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
280-640 1.90e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 1.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  280 KYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQ 359
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  360 FQFAEVKEAL------KQREEMLEEIRQLQQKQassiREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVM 433
Cdd:TIGR04523 288 KQLNQLKSEIsdlnnqKEQDWNKELKSELKNQE----KKLEEIQNQISQNNKIISQLNEQIS---QLKKELTNSESENSE 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  434 LKEELKKHGIILNSEIATNGETSDTLNNVGYQGPTKMTK----EELNALKstgdgtlDIRLKKLVDERECLLEQIKKLKG 509
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnqEKLNQQK-------DEQIKKLQQEKELLEKEIERLKE 433
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  510 QLEERQKigKLDNLRSEDDVLENGTDMH----------VMDLQRDANRQISDLKFK---LAKSEQEITALEQNVIRLESQ 576
Cdd:TIGR04523 434 TIIKNNS--EIKDLTNQDSVKELIIKNLdntresletqLKVLSRSINKIKQNLEQKqkeLKSKEKELKKLNEEKKELEEK 511
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276078  577 VSRYKSAAENAEKIEDELKAEKRKLQRELRSALD---------KTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
256-596 1.93e-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: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   256 DTEASIREI-KELNELKDQIQDVEgkymqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVdtlKDMLLELEEQL 334
Cdd:TIGR02169  234 ALERQKEAIeRQLASLEEELEKLT-------EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEI 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   335 AESRRQYEEKNKEFERekhAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQk 414
Cdd:TIGR02169  304 ASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   415 efFDSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQgptkmTKEELNALKStgdgtldiRLKKLV 494
Cdd:TIGR02169  380 --FAETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELAD-----LNAAIAGIEA--------KINELE 440
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   495 DERECLLEQIKKLKGQLEERQKIGKldnlrseddvlengtdmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLE 574
Cdd:TIGR02169  441 EEKEDKALEIKKQEWKLEQLAADLS------------------------KYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
                          330       340
                   ....*....|....*....|..
gi 212276078   575 SQVSRYKSAAENAEKIEDELKA 596
Cdd:TIGR02169  497 AQARASEERVRGGRAVEEVLKA 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
361-640 2.58e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 361 QFAEVKEALKQRE--EMLEEIRQLQQKQASSIREISDLQETIE----WKDKKIGALERQKEFFDSVRSERDDLREEVVML 434
Cdd:COG1196  214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEeleaELAELEAELEELRLELEELELELEEAQAEEYEL 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 435 KEELKKHGIILNSEIATNGETSDTLNNvgyqgptkmTKEELNALKSTGDG------TLDIRLKKLVDERECLLEQIKKLK 508
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEE---------LEEELAELEEELEEleeeleELEEELEEAEEELEEAEAELAEAE 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 509 GQLEERQKIgKLDNLRSEDDVLENgtDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAE 588
Cdd:COG1196  365 EALLEAEAE-LAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 212276078 589 KIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:COG1196  442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
367-603 2.63e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   367 EALKQREEMLE---EIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFD----SVRSERDDLREEVVMLKEELK 439
Cdd:TIGR02169  288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   440 KHGIILNSEIATNGETSDTLnnVGYQGPTKMTKEELNALKSTGDGTLDiRLKKLVDERECLLEQIKKLKGQLEERqkigk 519
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDEL--KDYREKLEKLKREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINEL----- 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   520 ldnlrseDDVLEngtdmhvmdlqrdanrqisDLKFKLAKSEQEITALEQNVIRLESQVSRYKsaaENAEKIEDELKAEKR 599
Cdd:TIGR02169  440 -------EEEKE-------------------DKALEIKKQEWKLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQR 490

                   ....
gi 212276078   600 KLQR 603
Cdd:TIGR02169  491 ELAE 494
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
265-633 2.80e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 265 KELNELKDQIQDVE-GKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlLELEEQLAESRRQYEE 343
Cdd:PRK03918 372 EELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGRELTEE 448
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 344 KNKEFEREKHAH-SILQFQFAEVKEALKQREEMLEEIRQL--QQKQASSIREISDLQETIEWKDKKIGA--LERQKEFFD 418
Cdd:PRK03918 449 HRKELLEEYTAElKRIEKELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYE 528
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 419 SVRSERDDLREEVVMLKEELKKHGIILNSEIATN----------GETSDTLNNVGYqGPTKMTKEELNALKSTGDGTldI 488
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEkkldeleeelAELLKELEELGF-ESVEELEERLKELEPFYNEY--L 605
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 489 RLKKLVDERECLLEQIKKLKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQ 568
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELRE 666
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212276078 569 NVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 633
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
261-636 3.02e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 261 IREIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEK---YKKAMVSNAQLDNEKTNFM-YQVDTLKDMLLELEEQlae 336
Cdd:PRK03918 327 EERIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKA--- 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 337 sRRQYEEKNKEFEREKhahsilqfqfAEVKEALKQREEMLEEIRQLQQK----------------QASSIREISDLQETI 400
Cdd:PRK03918 400 -KEEIEEEISKITARI----------GELKKEIKELKKAIEELKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKEL 468
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 401 EWKDKKIGALERQKEFFDSVRSERDDLR------EEVVMLKEELKKHGIilnSEIATNGETSDTLNN--VGYQGPTKMTK 472
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIklkelaEQLKELEEKLKKYNL---EELEKKAEEYEKLKEklIKLKGEIKSLK 545
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 473 EELNALKStgdgtLDIRLKKLVDERECLLEQIKKLKGQLEERqKIGKLDNLRSEDDVLENGTDMHVMdlQRDANRQISDL 552
Cdd:PRK03918 546 KELEKLEE-----LKKKLAELEKKLDELEEELAELLKELEEL-GFESVEELEERLKELEPFYNEYLE--LKDAEKELERE 617
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 553 KFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDE-----LKAEKRKLQRELRSALDKTEELEVSNGHLVKRLE 627
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLE 697

                 ....*....
gi 212276078 628 KMKANRSAL 636
Cdd:PRK03918 698 KLKEELEER 706
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
340-631 5.49e-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: 5.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   340 QYEEKNKEFEREKHAHSILQFQFAEvkealKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALER-----QK 414
Cdd:TIGR02168  214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEeieelQK 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   415 EFFdSVRSERDDLREEVVMLKEELK---KHGIILNSEIATNGETSDTLnnvgyqgptkmtKEELNALKstgdgtldirlk 491
Cdd:TIGR02168  289 ELY-ALANEISRLEQQKQILRERLAnleRQLEELEAQLEELESKLDEL------------AEELAELE------------ 343
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   492 klvderecllEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVI 571
Cdd:TIGR02168  344 ----------EKLEELKEELESLEA--ELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIE 403
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212276078   572 RLESQVSRYKSAAENA-EKIEDELK----AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 631
Cdd:TIGR02168  404 RLEARLERLEDRRERLqQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEALEELRE 468
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
342-459 5.72e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.39  E-value: 5.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 342 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 421
Cdd:COG2433  388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 212276078 422 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 459
Cdd:COG2433  458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
353-608 8.08e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.21  E-value: 8.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 353 HAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERqkeffdsvrsERDDLREEVV 432
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 433 MLKEELKKhgiiLNSEIATNGETSDTLNNVgyqgptkmtkeeLNAlKSTGD--GTLDIrLKKLVDERECLLEQIKKLKGQ 510
Cdd:COG3883   83 ERREELGE----RARALYRSGGSVSYLDVL------------LGS-ESFSDflDRLSA-LSKIADADADLLEELKADKAE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 511 LEERQKigKLDNLRSEddvlengtdmhVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKI 590
Cdd:COG3883  145 LEAKKA--ELEAKLAE-----------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
                        250
                 ....*....|....*...
gi 212276078 591 EDELKAEKRKLQRELRSA 608
Cdd:COG3883  212 AAAAAAAAAAAAAAAAAA 229
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
342-532 1.19e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 342 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 421
Cdd:COG4717   53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 422 sERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGptKMTKEELNALKSTGDGTLDIRLKKLVDERECLL 501
Cdd:COG4717  133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
                        170       180       190
                 ....*....|....*....|....*....|.
gi 212276078 502 EQIKKLKGQLEERQKigKLDNLRSEDDVLEN 532
Cdd:COG4717  206 QRLAELEEELEEAQE--ELEELEEELEQLEN 234
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
383-636 1.69e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 383 QQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKhgiilnseiatngetsdtlnnv 462
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA---------------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 463 gyqgptkmTKEELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLrsedDVLENGTDMhv 538
Cdd:COG4942   74 --------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL----ALLLSPEDF-- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 539 mdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVS 618
Cdd:COG4942  132 ----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
                        250
                 ....*....|....*...
gi 212276078 619 NGHLVKRLEKMKANRSAL 636
Cdd:COG4942  208 LAELAAELAELQQEAEEL 225
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
364-631 2.82e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  364 EVKEALKQREeMLEEIRQLQQKQASSIREISDLQETIEWkdkkiGALERQKEFFDSVRSERDDLREEVVMLKEELKkhgi 443
Cdd:COG4913   243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELE---- 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  444 ilnseiatngetsdtlnnvgyqgptkmtkeelnalkstgdgTLDIRLKKLVDERECLLEQIKKLKGQleerqkigKLDNL 523
Cdd:COG4913   313 -----------------------------------------RLEARLDALREELDELEAQIRGNGGD--------RLEQL 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  524 RSEDDVLENGTDmHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAekiEDELKAEKRKLQR 603
Cdd:COG4913   344 EREIERLERELE-ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRR 419
                         250       260
                  ....*....|....*....|....*...
gi 212276078  604 ELRSALDKTEELEVSNGHLVKRLEKMKA 631
Cdd:COG4913   420 ELRELEAEIASLERRKSNIPARLLALRD 447
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
338-639 9.04e-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: 42.41  E-value: 9.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI--GALERQKE 415
Cdd:pfam15921  568 RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnAGSERLRA 647
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   416 FFDsVRSERDDLREEVvmlkeelkkhgiilnseiatngetsdtlnnvgyqgptKMTKEELNALKSTgdgtLDIRLKKLVD 495
Cdd:pfam15921  648 VKD-IKQERDQLLNEV-------------------------------------KTSRNELNSLSED----YEVLKRNFRN 685
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   496 ERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLEnGTDMHVMDLQRDANRQIsdlkfklakseqeiTALEQNVIRLES 575
Cdd:pfam15921  686 KSEEMETTTNKLKMQLKSAQS--ELEQTRNTLKSME-GSDGHAMKVAMGMQKQI--------------TAKRGQIDALQS 748
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212276078   576 QVSRYKSAAENAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 639
Cdd:pfam15921  749 KIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
486-636 1.05e-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: 42.35  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   486 LDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMHVMDLQR-------------DANRQISDL 552
Cdd:TIGR02168  696 LEKALAELRKELEELEEELEQLRKELEELSR--QISALRKDLARLEAEVEQLEERIAQlskelteleaeieELEERLEEA 773
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   553 KFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKAN 632
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853

                   ....
gi 212276078   633 RSAL 636
Cdd:TIGR02168  854 IESL 857
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
485-614 1.39e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 485 TLDIRLKKLVDERECLLEQIKKLKGQLEERQK-----IGKLDNLRSEDDVLENGTDMHVMDLQRD--------ANRQISD 551
Cdd:COG1579   14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276078 552 LKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 614
Cdd:COG1579   94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
308-630 1.49e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.03  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   308 QLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREkhahsiLQFQFAEVKEALKQREEMLEEI----RQLQ 383
Cdd:pfam15921  307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ------LVLANSELTEARTERDQFSQESgnldDQLQ 380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   384 QKQASSIREISDLQETIEwKDKKIGALERQKEF-FDSVRSERDDLREEVVMLKEELKKhgiiLNSEiaTNGETSDTLNNV 462
Cdd:pfam15921  381 KLLADLHKREKELSLEKE-QNKRLWDRDTGNSItIDHLRRELDDRNMEVQRLEALLKA----MKSE--CQGQMERQMAAI 453
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   463 gyQGPTKmTKEELNALKSTGDGTLDIrLKKLVDE---RECLLEQ----IKKLKGQLEERQKIGKLDNlrSEDDVLENGTD 535
Cdd:pfam15921  454 --QGKNE-SLEKVSSLTAQLESTKEM-LRKVVEEltaKKMTLESsertVSDLTASLQEKERAIEATN--AEITKLRSRVD 527
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   536 MHVMDLQ---------RDANRQISDLKFKLAKSEQEITALEQ---NVIRLESQVSRyKSAAENAEKIEDELKAEKRKLQ- 602
Cdd:pfam15921  528 LKLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQqieNMTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLEl 606
                          330       340       350
                   ....*....|....*....|....*....|..
gi 212276078   603 RELRSALDKTE----ELEVSNGHLvkRLEKMK 630
Cdd:pfam15921  607 QEFKILKDKKDakirELEARVSDL--ELEKVK 636
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
321-634 1.86e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.50  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   321 DTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQEti 400
Cdd:pfam02463  208 KALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE-- 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   401 EWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgpTKMTKEELNALKS 480
Cdd:pfam02463  286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE-------------LEKELKELEIKRE 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   481 TGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNlrseddvlENGTDMHVMDLQRDANRQISDLKFKLAKSE 560
Cdd:pfam02463  353 AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE--------EELELKSEEEKEAQLLLELARQLEDLLKEE 424
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212276078   561 QEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 634
Cdd:pfam02463  425 KKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
368-566 1.90e-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: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  368 ALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF------DSVRSERDDLREEVVMLKEElkkh 441
Cdd:COG4913   608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS---- 683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  442 giilNSEIATNGETSDTLnnvgyqgptkmtKEELNALKSTGDGtLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKL- 520
Cdd:COG4913   684 ----SDDLAALEEQLEEL------------EAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLe 746
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 212276078  521 DNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITAL 566
Cdd:COG4913   747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
338-637 2.15e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.19  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 417
Cdd:TIGR00606  195 RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKAL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   418 DSVRSERDDLREEVVMLKEELKKhgiilnseiATNGETSDTLNNvgyQGPTKMTKEELNALKSTGDGTLDIRLKKLVDER 497
Cdd:TIGR00606  275 KSRKKQMEKDNSELELKMEKVFQ---------GTDEQLNDLYHN---HQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   498 ECLLEQIKKLKGQLEERQ-KIGKLDNLRseddvLENGTDMHVMDLQRDA--NRQISD-LKFKLAKSEQEITALEQNVIRL 573
Cdd:TIGR00606  343 TELLVEQGRLQLQADRHQeHIRARDSLI-----QSLATRLELDGFERGPfsERQIKNfHTLVIERQEDEAKTAAQLCADL 417
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212276078   574 ESQVsryKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEvsngHLVKRLEKMKANRSALL 637
Cdd:TIGR00606  418 QSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK----FVIKELQQLEGSSDRIL 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
489-640 2.52e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   489 RLKKLVDERECLLEQIKKLKGQLEE-----RQKIGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISDLKFKLA 557
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEEltaelQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   558 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALL 637
Cdd:TIGR02168  313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392

                   ...
gi 212276078   638 SQQ 640
Cdd:TIGR02168  393 LQI 395
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
361-440 3.14e-03

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.44  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 361 QFAEVKEALKQR--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 438
Cdd:PRK05431  10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89

                 ..
gi 212276078 439 KK 440
Cdd:PRK05431  90 DE 91
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
358-630 3.56e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 358 LQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEE 437
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 438 LKKHGIILnseiatnGETSDTLNNVgyqgptkmtKEELNALKST--------GDGTLDIRLKKLVDERECLLEQIKKLKG 509
Cdd:PRK03918 254 KRKLEEKI-------RELEERIEEL---------KKEIEELEEKvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLS 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 510 QLEER-----QKIGKLDNLRSEDDVLENgtdmhvmdLQRDANRQISDLKfKLAKSEQEITALEQNVIRLESQVSRYKsaA 584
Cdd:PRK03918 318 RLEEEingieERIKELEEKEERLEELKK--------KLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRLTGLT--P 386
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 212276078 585 ENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 630
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
236-429 6.33e-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: 6.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   236 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 315
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   316 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEM-LEEIRQLQQKQASSIREIS 394
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 212276078   395 DLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 429
Cdd:TIGR02168  972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
262-614 6.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 262 REIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES--RR 339
Cdd:PRK03918 228 KEVKELEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSefYE 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 340 QYEEKNKEFEREKhahSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEW---------------KD 404
Cdd:PRK03918 304 EYLDELREIEKRL---SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkKR 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 405 KKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGP------TKMTKEELNAL 478
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPvcgrelTEEHRKELLEE 456
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 479 KSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAK 558
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 212276078 559 SEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 614
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
258-440 6.66e-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: 6.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   258 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 337
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREemlEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 417
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
                          170       180       190
                   ....*....|....*....|....*....|..
gi 212276078   418 DS---------VRSERDDLREEVVMLKEELKK 440
Cdd:TIGR02168  420 QQeieellkklEEAELKELQAELEELEEELEE 451
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
581-640 7.73e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 38.37  E-value: 7.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  581 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:pfam11932  27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
469-640 7.78e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 39.65  E-value: 7.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  469 KMTKEELNALKSTGDGTLDIRLKKLVDEREcllEQIKKLKGQLEE--RQKIGKLDNLRSEDDVLEngtdmHVMDLQRDAN 546
Cdd:PRK10929   79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLLEksRQAQQEQDRAREISDSLS-----QLPQQQTEAR 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078  547 RQISDLKFKL--------AKSEQEITALEQNVIRLESQVSRYKSA--------------AENAEKIEDELKAEKRKL--- 601
Cdd:PRK10929  151 RQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELELAqlsannrqelarlrSELAKKRSQQLDAYLQALrnq 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 212276078  602 -----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 640
Cdd:PRK10929  231 lnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
264-640 8.89e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 39.26  E-value: 8.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   264 IKELNELKDQIQDVE---GKYMQGLKEMkDSLAEVEEKYKKAMVSNAQLDNEKTNF----------MYQVDTLKDMLLEL 330
Cdd:TIGR01612 1249 IEDLDEIKEKSPEIEnemGIEMDIKAEM-ETFNISHDDDKDHHIISKKHDENISDIrekslkiiedFSEESDINDIKKEL 1327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   331 EEQLAESRRQYEEKNKEFEREKHAHSILQFQ-----FAEVKEALKQREEMLEEIRQLQQKQASSIREISD---------- 395
Cdd:TIGR01612 1328 QKNLLDAQKHNSDINLYLNEIANIYNILKLNkikkiIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDdinleecksk 1407
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   396 LQETIEWKDKKiGALERQKEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQGPTKMtKEEL 475
Cdd:TIGR01612 1408 IESTLDDKDID-ECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDH-DFNI 1485
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   476 NALKSTGDGTldirlKKLVDERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVLENgtdmhVMDLQRDANRQISDLK- 553
Cdd:TIGR01612 1486 NELKEHIDKS-----KGCKDEADKNAKAIEKNKELFEQyKKDVTELLNKYSALAIKNK-----FAKTKKDSEIIIKEIKd 1555
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078   554 ------FKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKL------QRELRSALDKTEELE--VSN 619
Cdd:TIGR01612 1556 ahkkfiLEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFlkisdiKKKINDCLKETESIEkkISS 1635
                          410       420
                   ....*....|....*....|.
gi 212276078   620 GHLVKRLEKMKANRSALLSQQ 640
Cdd:TIGR01612 1636 FSIDSQDTELKENGDNLNSLQ 1656
 
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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