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Conserved domains on  [gi|672065772|ref|XP_008765507|]
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leucine-rich repeat flightless-interacting protein 1 isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRRFIP super family cl26610
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
247-579 1.38e-57

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.


The actual alignment was detected with superfamily member pfam09738:

Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 200.69  E-value: 1.38e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   247 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKelnelkdqiqdvegkym 317
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   318 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQF 397
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   398 AEVKEALRQREEMLEeirqlqqkqagyireisdlqetiewkdkkigalerqkeffdsirserddlreetvklkeelkKHG 477
Cdd:pfam09738  166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   478 IILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKAAGEGTLG--KAKEVEVKKEIVEKVGQREtLQDSEQEQPKLNT 555
Cdd:pfam09738  184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDvrLKKLADEKEELLDEVRKLK-LQLEEEKSKRNST 259
                          330       340
                   ....*....|....*....|....
gi 672065772   556 gkdcvDRGVLHPGEKAENQRPVED 579
Cdd:pfam09738  260 -----RSSQSPDGFGLENGSHVIE 278
COG2433 super family cl43687
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
398-484 3.64e-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: 44.46  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  398 AEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKhg 477
Cdd:COG2433   399 REKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIER-- 476

                  ....*..
gi 672065772  478 iiLNSEI 484
Cdd:COG2433   477 --LEREL 481
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
247-579 1.38e-57

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: 200.69  E-value: 1.38e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   247 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKelnelkdqiqdvegkym 317
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   318 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQF 397
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   398 AEVKEALRQREEMLEeirqlqqkqagyireisdlqetiewkdkkigalerqkeffdsirserddlreetvklkeelkKHG 477
Cdd:pfam09738  166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   478 IILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKAAGEGTLG--KAKEVEVKKEIVEKVGQREtLQDSEQEQPKLNT 555
Cdd:pfam09738  184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDvrLKKLADEKEELLDEVRKLK-LQLEEEKSKRNST 259
                          330       340
                   ....*....|....*....|....
gi 672065772   556 gkdcvDRGVLHPGEKAENQRPVED 579
Cdd:pfam09738  260 -----RSSQSPDGFGLENGSHVIE 278
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
300-554 3.49e-06

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: 51.17  E-value: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   300 KELNELKDQIQDVEGKYMQGL-KEMKDSLAEVEEKYKkamvsnaQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEE 378
Cdd:TIGR04523  288 KQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   379 KNKEFErEKHAhsilqfqfaEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQKEffdSIRSE 458
Cdd:TIGR04523  361 KQRELE-EKQN---------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---LLEKE 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   459 RDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVgyqapTKITKEELNALKAAGEGTlgKAKEVEVKKEIVEKVG 538
Cdd:TIGR04523  428 IERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKI--KQNLEQKQKELKSKEK 496
                          250       260
                   ....*....|....*....|
gi 672065772   539 QRETL----QDSEQEQPKLN 554
Cdd:TIGR04523  497 ELKKLneekKELEEKVKDLT 516
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
296-473 7.89e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  296 IREIKELNELKDQIQDVEGKYmqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaesQRQ 375
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-----EAE 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  376 YEEKNKEFERekhahsiLQFQFAEVKEALRQREEMLEEIRQLQQKQAGYIREIS-----DLQETIEWKDKKIGALERQKE 450
Cdd:COG4717   141 LAELPERLEE-------LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeELQDLAEELEELQQRLAELEE 213
                         170       180
                  ....*....|....*....|...
gi 672065772  451 FFDSIRSERDDLREETVKLKEEL 473
Cdd:COG4717   214 ELEEAQEELEELEEELEQLENEL 236
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
398-484 3.64e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  398 AEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKhg 477
Cdd:COG2433   399 REKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIER-- 476

                  ....*..
gi 672065772  478 iiLNSEI 484
Cdd:COG2433   477 --LEREL 481
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
299-536 1.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  299 IKELNELKDQIQDV---EGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaeSQRQ 375
Cdd:PRK03918  171 IKEIKRRIERLEKFikrTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  376 YEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWK---DKKIGALERQKEFF 452
Cdd:PRK03918  247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGI 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  453 DSIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKAAGEG-TLGKA----KEV 527
Cdd:PRK03918  327 EERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEA------KAKKEELERLKKRLTGlTPEKLekelEEL 396

                  ....*....
gi 672065772  528 EVKKEIVEK 536
Cdd:PRK03918  397 EKAKEEIEE 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
373-473 1.21e-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: 43.12  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   373 QRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----RQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQ 448
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100
                   ....*....|....*....|....*....
gi 672065772   449 KEFFDSIR----SERDDLREETVKLKEEL 473
Cdd:TIGR02168  318 LEELEAQLeeleSKLDELAEELAELEEKL 346
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
397-474 1.00e-02

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 36.80  E-value: 1.00e-02
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   397 FAEVKEALRQR---EEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQKEffdsirsERDDLREETVKLKEEL 473
Cdd:pfam02403   11 PEAVKESLKKRgvdVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE-------DADALIAEVKELKDEL 83

                   .
gi 672065772   474 K 474
Cdd:pfam02403   84 K 84
 
Name Accession Description Interval E-value
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
247-579 1.38e-57

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: 200.69  E-value: 1.38e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   247 VEERPDKDFAE---------KGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKelnelkdqiqdvegkym 317
Cdd:pfam09738   30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   318 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQF 397
Cdd:pfam09738   93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   398 AEVKEALRQREEMLEeirqlqqkqagyireisdlqetiewkdkkigalerqkeffdsirserddlreetvklkeelkKHG 477
Cdd:pfam09738  166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   478 IILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKAAGEGTLG--KAKEVEVKKEIVEKVGQREtLQDSEQEQPKLNT 555
Cdd:pfam09738  184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDvrLKKLADEKEELLDEVRKLK-LQLEEEKSKRNST 259
                          330       340
                   ....*....|....*....|....
gi 672065772   556 gkdcvDRGVLHPGEKAENQRPVED 579
Cdd:pfam09738  260 -----RSSQSPDGFGLENGSHVIE 278
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
300-554 3.49e-06

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: 51.17  E-value: 3.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   300 KELNELKDQIQDVEGKYMQGL-KEMKDSLAEVEEKYKkamvsnaQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEE 378
Cdd:TIGR04523  288 KQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   379 KNKEFErEKHAhsilqfqfaEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQKEffdSIRSE 458
Cdd:TIGR04523  361 KQRELE-EKQN---------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---LLEKE 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   459 RDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVgyqapTKITKEELNALKAAGEGTlgKAKEVEVKKEIVEKVG 538
Cdd:TIGR04523  428 IERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKI--KQNLEQKQKELKSKEK 496
                          250       260
                   ....*....|....*....|
gi 672065772   539 QRETL----QDSEQEQPKLN 554
Cdd:TIGR04523  497 ELKKLneekKELEEKVKDLT 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
321-532 4.21e-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: 47.76  E-value: 4.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   321 KEMKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEV 400
Cdd:TIGR02169  670 RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   401 KEALRQREEMLEEIRQlqqKQAGYIREISDLQETIEWKDKKIGALERQ--KEFFDSIRSERDDLREETVKLKEELKKHGI 478
Cdd:TIGR02169  743 EEDLSSLEQEIENVKS---ELKELEARIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 672065772   479 ILNSEIATNGETSDTVND-VGYQAPTKITKEELNALKAAGEGTLGKAKEVEVKKE 532
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQElQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
296-473 7.89e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  296 IREIKELNELKDQIQDVEGKYmqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaesQRQ 375
Cdd:COG4717    70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAL-----EAE 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  376 YEEKNKEFERekhahsiLQFQFAEVKEALRQREEMLEEIRQLQQKQAGYIREIS-----DLQETIEWKDKKIGALERQKE 450
Cdd:COG4717   141 LAELPERLEE-------LEERLEELRELEEELEELEAELAELQEELEELLEQLSlateeELQDLAEELEELQQRLAELEE 213
                         170       180
                  ....*....|....*....|...
gi 672065772  451 FFDSIRSERDDLREETVKLKEEL 473
Cdd:COG4717   214 ELEEAQEELEELEEELEQLENEL 236
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
291-553 2.65e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   291 DTEASIREI-KELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAmvsNAQLDNEKTNFMYQVdtlKDMLLELEEQL 369
Cdd:TIGR02169  234 ALERQKEAIeRQLASLEEELEKLTEE----ISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRV---KEKIGELEAEI 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   370 AESQRQYEEKNKEFERekhAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQk 449
Cdd:TIGR02169  304 ASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   450 efFDSIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVGYQAPTKIT--KEELNALKAAGEGTLGKAKEV 527
Cdd:TIGR02169  380 --FAETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAIAgiEAKINELEEEKEDKALEIKKQ 453
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 672065772   528 EVK----KEIVEKVGQ-----RETLQDSEQEQPKL 553
Cdd:TIGR02169  454 EWKleqlAADLSKYEQelydlKEEYDRVEKELSKL 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
293-540 3.19e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 3.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   293 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 372
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   373 QRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREemlEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQKEFF 452
Cdd:TIGR02168  343 EEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   453 DSIRSERDDLREETvklkeELKKHGIILNSEIATNGETSDTVNDVgyQAPTKITKEELNALKAAGEGTLGKAKEVEVKKE 532
Cdd:TIGR02168  420 QQEIEELLKKLEEA-----ELKELQAELEELEEELEELQEELERL--EEALEELREELEEAEQALDAAERELAQLQARLD 492

                   ....*...
gi 672065772   533 IVEKVGQR 540
Cdd:TIGR02168  493 SLERLQEN 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
271-464 3.33e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   271 LASLGGTSSRRGSGDTSISMDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKA----MVSNAQLDN 346
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerASLEEALAL 891
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   347 EKTNFMYQVDTLKDMLLELEEqlaeSQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEM-LEEIRQLQQKQAGYI 425
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSE----LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDE 967
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 672065772   426 REISDLQETIEWKDKKIGA--------LERQKEFFDSIRSERDDLRE 464
Cdd:TIGR02168  968 EEARRRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
398-484 3.64e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  398 AEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKhg 477
Cdd:COG2433   399 REKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIER-- 476

                  ....*..
gi 672065772  478 iiLNSEI 484
Cdd:COG2433   477 --LEREL 481
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
291-536 7.59e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 7.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   291 DTEASIREIKELNELKD-QIQDVEGKYMQGLKEMKDSLAEVEEKykKAMVSNaqLDNEKTNFMYQVDTLKDMLLELEEQL 369
Cdd:TIGR04523  395 DLESKIQNQEKLNQQKDeQIKKLQQEKELLEKEIERLKETIIKN--NSEIKD--LTNQDSVKELIIKNLDNTRESLETQL 470
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   370 AESQRQY-------EEKNKEFEREKhahsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKI 442
Cdd:TIGR04523  471 KVLSRSInkikqnlEQKQKELKSKE----------KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   443 GALERQKEFFDS------IRSERDDLREETVKLKEE---LKKHGIILNSEIAtngETSDTVNDVGYQAPTKITK-----E 508
Cdd:TIGR04523  541 SDLEDELNKDDFelkkenLEKEIDEKNKEIEELKQTqksLKKKQEEKQELID---QKEKEKKDLIKEIEEKEKKissleK 617
                          250       260
                   ....*....|....*....|....*...
gi 672065772   509 ELNALKAAGEGTLGKAKEVEVKKEIVEK 536
Cdd:TIGR04523  618 ELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
299-536 1.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  299 IKELNELKDQIQDV---EGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaeSQRQ 375
Cdd:PRK03918  171 IKEIKRRIERLEKFikrTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  376 YEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWK---DKKIGALERQKEFF 452
Cdd:PRK03918  247 LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGI 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  453 DSIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKAAGEG-TLGKA----KEV 527
Cdd:PRK03918  327 EERIKELEEKEERLEELKKKLKE----LEKRLEELEERHELYEEA------KAKKEELERLKKRLTGlTPEKLekelEEL 396

                  ....*....
gi 672065772  528 EVKKEIVEK 536
Cdd:PRK03918  397 EKAKEEIEE 405
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
373-473 1.21e-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: 43.12  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   373 QRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----RQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQ 448
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
                           90       100
                   ....*....|....*....|....*....
gi 672065772   449 KEFFDSIR----SERDDLREETVKLKEEL 473
Cdd:TIGR02168  318 LEELEAQLeeleSKLDELAEELAELEEKL 346
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
377-475 2.13e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  377 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQKEFFDSIR 456
Cdd:COG4717    53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
                          90
                  ....*....|....*....
gi 672065772  457 sERDDLREETVKLKEELKK 475
Cdd:COG4717   133 -ELEALEAELAELPERLEE 150
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
296-536 3.70e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  296 IREIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEK---YKKAMVSNAQLDNEKTnfmyqvdtlkdmlleleeqlaes 372
Cdd:PRK03918  327 EERIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKK----------------------- 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  373 qrqyEEKNKEFEREKhahsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEW--------------- 437
Cdd:PRK03918  380 ----RLTGLTPEKLE----------KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrel 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  438 -KDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILN--SEIATNGETSDTVNDVgYQAPTKITKEELNALK 514
Cdd:PRK03918  446 tEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKEL-EEKLKKYNLEELEKKA 524
                         250       260
                  ....*....|....*....|..
gi 672065772  515 AAGEGTLGKAKEVEVKKEIVEK 536
Cdd:PRK03918  525 EEYEKLKEKLIKLKGEIKSLKK 546
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
269-556 4.80e-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: 4.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   269 ATLASLGGTSSRRGSGDTSISMDTEASI----REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQL 344
Cdd:TIGR02168  645 YRIVTLDGDLVRPGGVITGGSAKTNSSIlerrREIEELEEK--------------IEELEEKIAELEKALAELRKELEEL 710
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   345 DNEktnfmyqVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAgy 424
Cdd:TIGR02168  711 EEE-------LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE-- 781
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   425 iREISDLQETIewkdkkigalERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAptK 504
Cdd:TIGR02168  782 -AEIEELEAQI----------EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--E 848
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 672065772   505 ITKEELNALKA--AGEGTLGKAKEVEVKKEIVEKVGQRETLQDSEQEQPKLNTG 556
Cdd:TIGR02168  849 ELSEDIESLAAeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
290-531 5.35e-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: 40.82  E-value: 5.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   290 MDTEASIREI-KELNELKDQIQDVEGkymqglkemkdSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQ 368
Cdd:TIGR02169  787 RLSHSRIPEIqAELSKLEEEVSRIEA-----------RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE 855
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   369 LAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGYIRE----ISDLQETIEWKDKKIGA 444
Cdd:TIGR02169  856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKkrkrLSELKAKLEALEEELSE 935
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   445 LERQKEFFDSIRSER---DDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVgyqaptkitKEELNALKAAGEGTL 521
Cdd:TIGR02169  936 IEDPKGEDEEIPEEElslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDEL---------KEKRAKLEEERKAIL 1006
                          250
                   ....*....|
gi 672065772   522 GKAKEVEVKK 531
Cdd:TIGR02169 1007 ERIEEYEKKK 1016
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
293-550 7.48e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 7.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  293 EASIREIK-ELNELKDQIQDVEGKYMQGLKEMKD---SLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQ 368
Cdd:COG1196   266 EAELEELRlELEELELELEEAQAEEYELLAELARleqDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  369 LAESQRQYEEKNKEFEREKhahsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQ 448
Cdd:COG1196   346 LEEAEEELEEAEAELAEAE----------EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  449 KEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSdtvndvgyqaptkitKEELNALKAAGEGTLGKAKEVE 528
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE---------------EALLELLAELLEEAALLEAALA 480
                         250       260
                  ....*....|....*....|..
gi 672065772  529 VKKEIVEKVGQRETLQDSEQEQ 550
Cdd:COG1196   481 ELLEELAEAAARLLLLLEAEAD 502
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
291-542 8.48e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  291 DTEASIREIKE----LNELKDQIQDvegkymqgLKEMKDSLAEVEE---KYKKAMVSNAQLDNEKTNFMYQVDtlkdmll 363
Cdd:COG4913   222 DTFEAADALVEhfddLERAHEALED--------AREQIELLEPIRElaeRYAAARERLAELEYLRAALRLWFA------- 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  364 eleeqlaesQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGyiREISDLQETIEWKDKKI- 442
Cdd:COG4913   287 ---------QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELe 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772  443 ---GALERQKEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVND--VGYQAPTKITKEELNALKaAG 517
Cdd:COG4913   356 ereRRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAalRDLRRELRELEAEIASLE-RR 434
                         250       260
                  ....*....|....*....|....*
gi 672065772  518 EGTLGkAKEVEVKKEIVEKVGQRET 542
Cdd:COG4913   435 KSNIP-ARLLALRDALAEALGLDEA 458
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
397-474 1.00e-02

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 36.80  E-value: 1.00e-02
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672065772   397 FAEVKEALRQR---EEMLEEIRQLQQKQAGYIREISDLQETIEWKDKKIGALERQKEffdsirsERDDLREETVKLKEEL 473
Cdd:pfam02403   11 PEAVKESLKKRgvdVLDVDELLELDEKRRELQVELEELQAERNELSKEIGQAKKKKE-------DADALIAEVKELKDEL 83

                   .
gi 672065772   474 K 474
Cdd:pfam02403   84 K 84
 
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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