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Conserved domains on  [gi|568924180|ref|XP_006502203|]
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spindle assembly abnormal protein 6 homolog isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HD_SAS6_N cd10142
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; ...
 4-144 8.25e-58

N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; Spindle assembly abnormal protein 6 (SAS6) is a central scaffolding component of the centrioles that ensures their 9-fold symmetry. It is required for centrosome biogenesis and duplication, and is required for both mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. It is also required for the recruitment of microcephaly protein STIL to the procentriole and for STIL-mediated centriole amplification. SAS6 is comprised of an N-terminal globular head domain, a centrally located coiled-coil domain, and a disordered C-terminus. These monomers homodimerize symmetrically, through two dimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These homodimers can self-assemble into a 9-fold symmetric cartwheel structure comprised of nine SAS6 homodimers associated via their head domains; the dimerized coiled-coil domains being the spokes, the central hub being the head domains. This model corresponds to the N-terminal head domain of SAS6, which is structurally related to other XRCC4-superfamily members, XRCC4, PAXX, XLF and CCDC61.


:

Pssm-ID: 408998  Cd Length: 137  Bit Score: 191.23  E-value: 8.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   4 VLFQQLVPLLVKCKDCEERRGSVRVSIELQSlSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAF 83
Cdd:cd10142    1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568924180  84 PQKFIDLLQQCMQEHAKETPRFLLQLLSSAtllENSPVLLNVVETNPFKHLIHLSLKLLPG 144
Cdd:cd10142   80 PQKLIDLLELCIKEESKEPPKFLLVLVISS---DKGRATLEIVETNPFKHLTHLSLKFLPG 137
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-471 5.96e-13

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.40  E-value: 5.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   167 LTRsLDDVTRQLHITQETL---SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL- 242
Cdd:TIGR02168  188 LDR-LEDILNELERQLKSLerqAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELe 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   243 -----HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHI 317
Cdd:TIGR02168  267 ekleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   318 NQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ------KQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKL 391
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQletlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   392 Q-----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEE------ 460
Cdd:TIGR02168  427 LkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfse 506

                          330
                   ....*....|..
gi 568924180   461 -SKQLLKNNEKL 471
Cdd:TIGR02168  507 gVKALLKNQSGL 518
Sas6_CC super family cl39913
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of ...
 146-171 7.51e-03

Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of spindle assembly abnormal protein 6 (Sas6). The highly conserved protein SAS-6 constitutes the center of the cartwheel assembly that scaffolds centrioles early in their biogenesis.Structural analysis of Sas6 show that similar to XLF, and XRCC4 it forms a parallel coiled-coil dimer.


The actual alignment was detected with superfamily member pfam18594:

Pssm-ID: 408377 [Multi-domain]  Cd Length: 30  Bit Score: 34.57  E-value: 7.51e-03
                          10        20
                  ....*....|....*....|....*.
gi 568924180  146 DVEIKKFLAGCLKCSKEEKLSLTRSL 171
Cdd:pfam18594   1 DSEVKKYLADCLKSLKEEKQLLEQKL 26
 
Name Accession Description Interval E-value
HD_SAS6_N cd10142
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; ...
 4-144 8.25e-58

N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; Spindle assembly abnormal protein 6 (SAS6) is a central scaffolding component of the centrioles that ensures their 9-fold symmetry. It is required for centrosome biogenesis and duplication, and is required for both mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. It is also required for the recruitment of microcephaly protein STIL to the procentriole and for STIL-mediated centriole amplification. SAS6 is comprised of an N-terminal globular head domain, a centrally located coiled-coil domain, and a disordered C-terminus. These monomers homodimerize symmetrically, through two dimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These homodimers can self-assemble into a 9-fold symmetric cartwheel structure comprised of nine SAS6 homodimers associated via their head domains; the dimerized coiled-coil domains being the spokes, the central hub being the head domains. This model corresponds to the N-terminal head domain of SAS6, which is structurally related to other XRCC4-superfamily members, XRCC4, PAXX, XLF and CCDC61.


Pssm-ID: 408998  Cd Length: 137  Bit Score: 191.23  E-value: 8.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   4 VLFQQLVPLLVKCKDCEERRGSVRVSIELQSlSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAF 83
Cdd:cd10142    1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568924180  84 PQKFIDLLQQCMQEHAKETPRFLLQLLSSAtllENSPVLLNVVETNPFKHLIHLSLKLLPG 144
Cdd:cd10142   80 PQKLIDLLELCIKEESKEPPKFLLVLVISS---DKGRATLEIVETNPFKHLTHLSLKFLPG 137
SAS-6_N pfam16531
Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar ...
 44-141 7.50e-28

Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar protein, both in C.elegans and in humans. The N-terminal domain is the region through which the 9 rod-shaped homodimers that SAS-6 forms on oligomerization interact with each other. Proper functioning of the centriole requires this correct oligomerization.


Pssm-ID: 465163  Cd Length: 88  Bit Score: 107.28  E-value: 7.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   44 LVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCMQEhaketprfllQLLSSATLLENSPVLL 123
Cdd:pfam16531   1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKE----------PNLLVFLIQDDGTATL 70

                          90
                  ....*....|....*...
gi 568924180  124 NVVETNPFKHLIHLSLKL 141
Cdd:pfam16531  71 VFIENNEFKNLEHLSLDF 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-471 5.96e-13

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: 72.40  E-value: 5.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   167 LTRsLDDVTRQLHITQETL---SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL- 242
Cdd:TIGR02168  188 LDR-LEDILNELERQLKSLerqAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELe 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   243 -----HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHI 317
Cdd:TIGR02168  267 ekleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   318 NQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ------KQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKL 391
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQletlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   392 Q-----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEE------ 460
Cdd:TIGR02168  427 LkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfse 506

                          330
                   ....*....|..
gi 568924180   461 -SKQLLKNNEKL 471
Cdd:TIGR02168  507 gVKALLKNQSGL 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-483 6.66e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.28  E-value: 6.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 184 TLSEKMQELDK----LRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEA 259
Cdd:COG1196  217 ELKEELKELEAelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 260 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVL 339
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 340 RTKEAFDTIQEQKQVALEENGEKNQiQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEK 419
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568924180 420 EEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE-KLITWLNKELNENQ 483
Cdd:COG1196  455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
160-489 8.15e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 8.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 160 SKEEKLS-LTRSLDDVTRQL------HITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKalqtqvqcqqqh 232
Cdd:PRK03918 335 EKEERLEeLKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE------------ 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 233 eqQKKELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVREL------------KAKLAGVEEELQRAKQEVLSLR 300
Cdd:PRK03918 403 --IEEEISKITAR-IGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrkelleeyTAELKRIEKELKEIEEKERKLR 479

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 301 RENCTLDTECHEKEKHINQLQtkvavLEQEIKDkdqlvlrTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAE 380
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKE-----LAEQLKE-------LEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 381 LLKANEIIKKL----------QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQ 450
Cdd:PRK03918 548 LEKLEELKKKLaelekkldelEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE 627

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 568924180 451 LETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 489
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE 666
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 236-488 3.04e-07

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: 53.82  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   236 KKELETLHQ--RNIHQLQSRLSELEAANKELTERKYKgdsTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEK 313
Cdd:pfam02463  172 KEALKKLIEetENLAELIIDLEELKLQELKLKEQAKK---ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   314 EKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQG 393
Cdd:pfam02463  249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   394 DLKTLMG----KLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE 469
Cdd:pfam02463  329 ELKKEKEeieeLEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408

                          250
                   ....*....|....*....
gi 568924180   470 KLITWLNKELNENQLVRKQ 488
Cdd:pfam02463  409 LLLELARQLEDLLKEEKKE 427
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 286-408 4.62e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 286 EEELQRAKQEVLSLrrenctLDTEchekEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVAL-EENGEKNQ 364
Cdd:cd22656  109 DEELEEAKKTIKAL------LDDL----LKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLtDEGGAIAR 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568924180 365 IQLGKLEATIKSLSAELL-KANEIIKKLQGDLKTLMGKLKLKNTV 408
Cdd:cd22656  179 KEIKDLQKELEKLNEEYAaKLKAKIDELKALIADDEAKLAAALRL 223
Sas6_CC pfam18594
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of ...
 146-171 7.51e-03

Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of spindle assembly abnormal protein 6 (Sas6). The highly conserved protein SAS-6 constitutes the center of the cartwheel assembly that scaffolds centrioles early in their biogenesis.Structural analysis of Sas6 show that similar to XLF, and XRCC4 it forms a parallel coiled-coil dimer.


Pssm-ID: 408377 [Multi-domain]  Cd Length: 30  Bit Score: 34.57  E-value: 7.51e-03
                          10        20
                  ....*....|....*....|....*.
gi 568924180  146 DVEIKKFLAGCLKCSKEEKLSLTRSL 171
Cdd:pfam18594   1 DSEVKKYLADCLKSLKEEKQLLEQKL 26
 
Name Accession Description Interval E-value
HD_SAS6_N cd10142
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; ...
 4-144 8.25e-58

N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; Spindle assembly abnormal protein 6 (SAS6) is a central scaffolding component of the centrioles that ensures their 9-fold symmetry. It is required for centrosome biogenesis and duplication, and is required for both mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. It is also required for the recruitment of microcephaly protein STIL to the procentriole and for STIL-mediated centriole amplification. SAS6 is comprised of an N-terminal globular head domain, a centrally located coiled-coil domain, and a disordered C-terminus. These monomers homodimerize symmetrically, through two dimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These homodimers can self-assemble into a 9-fold symmetric cartwheel structure comprised of nine SAS6 homodimers associated via their head domains; the dimerized coiled-coil domains being the spokes, the central hub being the head domains. This model corresponds to the N-terminal head domain of SAS6, which is structurally related to other XRCC4-superfamily members, XRCC4, PAXX, XLF and CCDC61.


Pssm-ID: 408998  Cd Length: 137  Bit Score: 191.23  E-value: 8.25e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   4 VLFQQLVPLLVKCKDCEERRGSVRVSIELQSlSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAF 83
Cdd:cd10142    1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568924180  84 PQKFIDLLQQCMQEHAKETPRFLLQLLSSAtllENSPVLLNVVETNPFKHLIHLSLKLLPG 144
Cdd:cd10142   80 PQKLIDLLELCIKEESKEPPKFLLVLVISS---DKGRATLEIVETNPFKHLTHLSLKFLPG 137
SAS-6_N pfam16531
Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar ...
 44-141 7.50e-28

Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar protein, both in C.elegans and in humans. The N-terminal domain is the region through which the 9 rod-shaped homodimers that SAS-6 forms on oligomerization interact with each other. Proper functioning of the centriole requires this correct oligomerization.


Pssm-ID: 465163  Cd Length: 88  Bit Score: 107.28  E-value: 7.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   44 LVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCMQEhaketprfllQLLSSATLLENSPVLL 123
Cdd:pfam16531   1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKE----------PNLLVFLIQDDGTATL 70

                          90
                  ....*....|....*...
gi 568924180  124 NVVETNPFKHLIHLSLKL 141
Cdd:pfam16531  71 VFIENNEFKNLEHLSLDF 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-471 5.96e-13

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: 72.40  E-value: 5.96e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   167 LTRsLDDVTRQLHITQETL---SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL- 242
Cdd:TIGR02168  188 LDR-LEDILNELERQLKSLerqAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELe 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   243 -----HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHI 317
Cdd:TIGR02168  267 ekleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   318 NQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ------KQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKL 391
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQletlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   392 Q-----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEE------ 460
Cdd:TIGR02168  427 LkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfse 506

                          330
                   ....*....|..
gi 568924180   461 -SKQLLKNNEKL 471
Cdd:TIGR02168  507 gVKALLKNQSGL 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-483 6.66e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 72.28  E-value: 6.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 184 TLSEKMQELDK----LRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEA 259
Cdd:COG1196  217 ELKEELKELEAelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLA 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 260 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVL 339
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 340 RTKEAFDTIQEQKQVALEENGEKNQiQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEK 419
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568924180 420 EEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE-KLITWLNKELNENQ 483
Cdd:COG1196  455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-483 2.72e-12

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: 70.09  E-value: 2.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   243 HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQT 322
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   323 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQV------ALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 396
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   397 TLMGKLK-LKNTVTI---QQEKLLAEKEEMLQK-ERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 471
Cdd:TIGR02168  397 SLNNEIErLEARLERledRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          250
                   ....*....|..
gi 568924180   472 ITWLNKELNENQ 483
Cdd:TIGR02168  477 LDAAERELAQLQ 488
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-481 1.09e-11

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: 68.17  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   162 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWAS---HTASLTNKHSQELT---AEKEKALQTQVQCQQQHEQQ 235
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaerYQALLKEKREYEGYellKEKEALERQKEAIERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   236 KKELETLhQRNIHQLQSRLSELEAANKELTER-KYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE 314
Cdd:TIGR02169  250 EEELEKL-TEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLE 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   315 KHINQLQTKVAVLEQEI----KDKDQLVLRTKEAFDTIqEQKQVALEENGEKNQIQLGKLeatiKSLSAELLKANEIIKK 390
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIeeerKRRDKLTEEYAELKEEL-EDLRAELEEVDKEFAETRDEL----KDYREKLEKLKREINE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   391 LQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEK 470
Cdd:TIGR02169  404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483

                          330
                   ....*....|.
gi 568924180   471 LITWLNKELNE 481
Cdd:TIGR02169  484 ELSKLQRELAE 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 162-451 1.42e-11

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: 67.77  E-value: 1.42e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   162 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWAShtasltnkHSQELTAEKEKAlqtqvqcqqqhEQQKKELET 241
Cdd:TIGR02168  684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE--------LSRQISALRKDL-----------ARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   242 LHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQ 321
Cdd:TIGR02168  745 LEER-IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   322 TKVAVLEQEIKDKDQLVLRTKEAFDTIQEQkQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK 401
Cdd:TIGR02168  824 ERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 568924180   402 LKLKNTVTIQQEKLLAEKEEMLQKERKESQDAgqflrakEQEVCRLQEQL 451
Cdd:TIGR02168  903 LRELESKRSELRRELEELREKLAQLELRLEGL-------EVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 247-488 2.39e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 247 IHQLQSRLSELEA-ANKELTERKYKGDSTVRELK---AKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQT 322
Cdd:COG1196  195 LGELERQLEPLERqAEKAERYRELKEELKELEAElllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 323 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQV------ALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 396
Cdd:COG1196  275 ELEELELELEEAQAEEYELLAELARLEQDIARleerrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 397 TLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLN 476
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434

                        250
                 ....*....|..
gi 568924180 477 KELNENQLVRKQ 488
Cdd:COG1196  435 EEEEEEEEALEE 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 262-488 7.47e-10

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: 62.38  E-value: 7.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   262 KELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKEKHINQLQTKVAVLEQEIKDKDQLVLRT 341
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL-------EELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   342 KEAFDTIQEQKQVALEengeknqiQLGKLEATIKSLSAELLKANEIIKKLQGDLKTlmgklkLKNTVTIQQEKLLAEKEE 421
Cdd:TIGR02168  753 SKELTELEAEIEELEE--------RLEEAEEELAEAEAEIEELEAQIEQLKEELKA------LREALDELRAELTLLNEE 818

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568924180   422 MLQKERKESQDAGQfLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 488
Cdd:TIGR02168  819 AANLRERLESLERR-IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 157-481 9.38e-10

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: 61.96  E-value: 9.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  157 LKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNkhsqeLTAEKEKALQTQVQCQQQHEQQK 236
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-----LKDEQNKIKKQLSEKQKELEQNN 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  237 KELETLhQRNIHQLQSRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECH 311
Cdd:TIGR04523 281 KKIKEL-EKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  312 EKEKHINQLQTKVAVLEQEIKDKDQ----LVLRTKEAFDTIQEQKQVA--LEENGEKNQIQLGKLEATIKSLSAELLKAN 385
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQeiknLESQINDLESKIQNQEKLNqqKDEQIKKLQQEKELLEKEIERLKETIIKNN 439

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  386 EIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQ---LETTVQKLEESK 462
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKI 519

                         330
                  ....*....|....*....
gi 568924180  463 QLLKNNEKLitwLNKELNE 481
Cdd:TIGR04523 520 SSLKEKIEK---LESEKKE 535
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-427 2.13e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 2.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 161 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQtqvqcqqqheqqkKELE 240
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL-------------EERR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 241 TLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKEKHINQL 320
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-------AEAEEELEEL 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQiQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG 400
Cdd:COG1196  385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE-ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                        250       260
                 ....*....|....*....|....*..
gi 568924180 401 KLKLKNTVTIQQEKLLAEKEEMLQKER 427
Cdd:COG1196  464 LLAELLEEAALLEAALAELLEELAEAA 490
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 236-487 7.50e-09

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: 58.93  E-value: 7.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   236 KKELETLHQ------RNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTE 309
Cdd:TIGR02169  687 KRELSSLQSelrrieNRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   310 CHEKEKHINQLQTKVAVLEQEIKDkdqlvlrtkEAFDTIQEQKQvALEENGEKNQIQLGKLEATIKSLSAELLKANEIIK 389
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELS-KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   390 KLQGDLKTLMGKlklKNTVTIQQEKLLAEKEEMLQKERKesqdagqfLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE 469
Cdd:TIGR02169  837 ELQEQRIDLKEQ---IKSIEKEIENLNGKKEELEEELEE--------LEAALRDLESRLGDLKKERDELEAQLRELERKI 905

                          250
                   ....*....|....*...
gi 568924180   470 KLITWLNKELNENQLVRK 487
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELK 923
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 276-479 2.16e-08

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: 56.70  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 276 RELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQ-- 353
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEaq 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 354 --------VALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQK 425
Cdd:COG4942  103 keelaellRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568924180 426 ERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKEL 479
Cdd:COG4942  183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 272-556 3.98e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 55.99  E-value: 3.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 272 DSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDK-DQLVLRTKEAFdtiqe 350
Cdd:COG3883   22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERrEELGERARALY----- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 351 qkqvaleengeKNQIQLGKLEATIKSLS-AELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKEEMLQKERKE 429
Cdd:COG3883   97 -----------RSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELK-------ADKAELEAKKAELEAKLAE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 430 SQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNneklitWLNKELNENQLVRKQDTLGTSATPHSTSNSTIRSGL 509
Cdd:COG3883  159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEA------QLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568924180 510 SPNLNVVDRLNYPSCGIGYPVSSALTFQNAFPHVVAAKNTSHPISGP 556
Cdd:COG3883  233 AAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAA 279
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 243-444 4.51e-08

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: 54.55  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 243 HQRNIHQLQ---SRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQRAKQEVLSLRREnctldtechekekhinq 319
Cdd:COG1579    5 DLRALLDLQeldSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKE----------------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 320 lqtkVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQV-ALeengeknQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTL 398
Cdd:COG1579   61 ----IKRLELEIEEVEARIKKYEEQLGNVRNNKEYeAL-------QKEIESLKRRISDLEDEILELMERIEELEEELAEL 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568924180 399 MGKLKlkntvtiQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEV 444
Cdd:COG1579  130 EAELA-------ELEAELEEKKAELDEELAELEAELEELEAEREEL 168
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
160-489 8.15e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 8.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 160 SKEEKLS-LTRSLDDVTRQL------HITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKalqtqvqcqqqh 232
Cdd:PRK03918 335 EKEERLEeLKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE------------ 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 233 eqQKKELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVREL------------KAKLAGVEEELQRAKQEVLSLR 300
Cdd:PRK03918 403 --IEEEISKITAR-IGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrkelleeyTAELKRIEKELKEIEEKERKLR 479

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 301 RENCTLDTECHEKEKHINQLQtkvavLEQEIKDkdqlvlrTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAE 380
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKE-----LAEQLKE-------LEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 381 LLKANEIIKKL----------QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQ 450
Cdd:PRK03918 548 LEKLEELKKKLaelekkldelEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE 627

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 568924180 451 LETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 489
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE 666
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
190-453 2.87e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 2.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  190 QELDKLRSEWASHTASLtnkhsQELTAEKEKALQTQVQCQQQHEQQKKELETL-HQRNIHQLQSRLSELEAANKELterk 268
Cdd:COG4913   617 AELAELEEELAEAEERL-----EALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDDL---- 687

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  269 ykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVL---RTKEAF 345
Cdd:COG4913   688 -------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerFAAALG 760

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  346 DTIQEQKQVALEENGEKNQIQLGKLEATI---------------KSLSAELLKANEIIKKLQgdlktlmgklklkntvTI 410
Cdd:COG4913   761 DAVERELRENLEERIDALRARLNRAEEELeramrafnrewpaetADLDADLESLPEYLALLD----------------RL 824

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 568924180  411 QQEKLLAEKEEMLQ-KERKESQDAGQFLRAKEQEVCRLQEQLET 453
Cdd:COG4913   825 EEDGLPEYEERFKElLNENSIEFVADLLSKLRRAIREIKERIDP 868
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 236-488 3.04e-07

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: 53.82  E-value: 3.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   236 KKELETLHQ--RNIHQLQSRLSELEAANKELTERKYKgdsTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEK 313
Cdd:pfam02463  172 KEALKKLIEetENLAELIIDLEELKLQELKLKEQAKK---ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   314 EKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQG 393
Cdd:pfam02463  249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   394 DLKTLMG----KLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE 469
Cdd:pfam02463  329 ELKKEKEeieeLEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408

                          250
                   ....*....|....*....
gi 568924180   470 KLITWLNKELNENQLVRKQ 488
Cdd:pfam02463  409 LLLELARQLEDLLKEEKKE 427
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 249-463 4.54e-07

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: 52.46  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 249 QLQSRLSELEAANKELTERKYKgdstVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 328
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKE----LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 329 QEIKDKDQLVLRTKEAFDTIQEQKQVALEENGE------KNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKL 402
Cdd:COG4942   97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEdfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568924180 403 K-LKNTVTIQQEKL---LAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQ 463
Cdd:COG4942  177 EaLLAELEEERAALealKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
249-463 1.37e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 249 QLQSRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQ--RAKQEVLSLRRENCTLDTEchekekhINQLQTKVAV 326
Cdd:COG3206  165 NLELRREEARKALEFLEEQ-------LPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQ-------LSELESQLAE 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 327 LEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKN-QIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-- 403
Cdd:COG3206  231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQlRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqe 310

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568924180 404 -------LKNTVTI--QQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQ 463
Cdd:COG3206  311 aqrilasLEAELEAlqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 250-471 1.72e-06

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 51.05  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  250 LQSRLSELEAANKELterkykgdstVRELKAKLAGVEEELQRAKqevlslrRENCTLDTECHEKEKHINQLQTKVAVLEQ 329
Cdd:pfam07888  32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYK-------RDREQWERQRRELESRVAELKEELRQSRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  330 EIKDKDQLVLRTKEAFDTIQEQKQVALEENGEkNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 409
Cdd:pfam07888  95 KHEELEEKYKELSASSEELSEEKDALLAQRAA-HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568924180  410 IQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 471
Cdd:pfam07888 174 KQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 158-483 2.24e-06

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: 50.89  E-value: 2.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   158 KCSKEEKLSLTRSLDDVTRQLHITQETL---------------SEKMQELDKLRSEWASHTASLTNKHSQELTAE----K 218
Cdd:pfam15921  158 KCLKEDMLEDSNTQIEQLRKMMLSHEGVlqeirsilvdfeeasGKKIYEHDSMSTMHFRSLGSAISKILRELDTEisylK 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   219 EKALQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEElqrakqevls 298
Cdd:pfam15921  238 GRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ---------- 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   299 LRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDK-----DQLVLRTKEAFDTIQEQKQVALEENGEKNQIQ--LGKLE 371
Cdd:pfam15921  308 ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKieeleKQLVLANSELTEARTERDQFSQESGNLDDQLQklLADLH 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   372 ATIKSLSAELLKANEIIKKLQGDLKT---LMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQ 448
Cdd:pfam15921  388 KREKELSLEKEQNKRLWDRDTGNSITidhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 568924180   449 EQLETT-------VQKLEESKQLLKNNEKLITWLNKELNENQ 483
Cdd:pfam15921  468 AQLESTkemlrkvVEELTAKKMTLESSERTVSDLTASLQEKE 509
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
160-472 2.36e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 160 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasLTNKHSQELTAEKEKAlqtqvqcqqQHEQQKKEL 239
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEE-------IEELEKELESLEGSKR---------KLEEKIREL 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 240 EtlhqRNIHQLQSRLSELEAANKELTERKYKGDSTVR------ELKAKLAGVEEELQRAKQEVLSLRRENctldTECHEK 313
Cdd:PRK03918 265 E----ERIEELKKEIEELEEKVKELKELKEKAEEYIKlsefyeEYLDELREIEKRLSRLEEEINGIEERI----KELEEK 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 314 EKHINQLQTKvavlEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQG 393
Cdd:PRK03918 337 EERLEELKKK----LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568924180 394 DLKTLMGKLKLKNTVTIQQEKllAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLI 472
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 183-485 3.74e-06

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: 50.50  E-value: 3.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   183 ETL-SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQK------KELETLHQRNIHQLQSRLS 255
Cdd:pfam15921  248 EALkSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqeqaRNQNSMYMRQLSDLESTVS 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   256 ELEAankELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECH---------EKEKHINQLQTK--- 323
Cdd:pfam15921  328 QLRS---ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQklladlhkrEKELSLEKEQNKrlw 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   324 ---------VAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEaTIKSLSAELLKANEIIKKLQGD 394
Cdd:pfam15921  405 drdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEE 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   395 LKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQ---EQLETTVQKLEESKQLLKNNEKL 471
Cdd:pfam15921  484 LTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKV 563

                          330
                   ....*....|....*
gi 568924180   472 ITWLNKEL-NENQLV 485
Cdd:pfam15921  564 IEILRQQIeNMTQLV 578
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 153-472 6.43e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 6.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   153 LAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEK---MQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQ 229
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELekrLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   230 QQHEQQKKELETLHQR------NIHQLQSRLSELEAAnkelterkykgdstVRELKAKLAGVEEELQRAKQEVLSLRREN 303
Cdd:TIGR02169  308 RSIAEKERELEDAEERlakleaEIDKLLAEIEELERE--------------IEEERKRRDKLTEEYAELKEELEDLRAEL 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   304 CTLDTECHEKEKHINQLQTKVAVLEQEIKDkdqlvlrTKEAFDTIQEQKQVALEENGEKNQiQLGKLEATIKSLSAELLK 383
Cdd:TIGR02169  374 EEVDKEFAETRDELKDYREKLEKLKREINE-------LKRELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKED 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   384 ANEIIKKLQGDLKTLMGKLKlkntvtIQQEKLLAEKEEMLQKERKesqdagqfLRAKEQEVcrlqEQLETTVQKLEESKQ 463
Cdd:TIGR02169  446 KALEIKKQEWKLEQLAADLS------KYEQELYDLKEEYDRVEKE--------LSKLQREL----AEAEAQARASEERVR 507


                   ....*....
gi 568924180   464 LLKNNEKLI 472
Cdd:TIGR02169  508 GGRAVEEVL 516
HD_XRCC4-like_N cd22210
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ...
 41-144 1.07e-05

N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily includes five families: XRCC4, XLF, PAXX, SAS6 and CCDC61. XRCC4 (X-ray repair cross-complementing protein 4), XLF (XRCC4-like factor) and PAXX (paralog of XRCC4 and XLF) play crucial roles in the non-homologous end-joining (NHEJ) DNA repair pathway. SAS6 (spindle assembly abnormal protein 6) and CCDC61 (coiled-coil domain-containing protein 61) have a centrosomal/centriolar function. Members of this superfamily have an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal low-complexity region. They form homodimers through two homodimerization domains: an N-terminal globular head domain and a parallel coiled-coil domain. In addition, some members such as XRCC4 and XLF form symmetric heterodimers that interact through their globular head domains at the opposite end of the homodimer interface, and may form XLF-XRCC4 filaments. This model corresponds to the N-terminal head domain of XRCC4 superfamily proteins.


Pssm-ID: 408999  Cd Length: 115  Bit Score: 44.84  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  41 RKDLVIRLTDDtdpFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCmqehAKETPRFLLQLlssaTLLENSP 120
Cdd:cd22210   25 ERGLRLHVSDD---AFLWTGEVSESDISQLKNDQGILVDFASFPGKLRSALEKC----ILASDRFTFVL----TIRGDEA 93

                         90       100
                 ....*....|....*....|....
gi 568924180 121 VLlnVVETNPFKHLIHLSLKLLPG 144
Cdd:cd22210   94 YL--KLVEILDEQLPHITFALRKV 115
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
249-493 2.13e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 249 QLQSRLSELEAANKELterkykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 328
Cdd:COG4372   32 QLRKALFELDKLQEEL-----------EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 329 QEIKDKDQLVLRTKEAFDTIQEQKQvALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTV 408
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQ-DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 409 TIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 488
Cdd:COG4372  180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259


                 ....*
gi 568924180 489 DTLGT 493
Cdd:COG4372  260 IEELE 264
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
217-386 2.54e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 217 EKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEAANKELT--ERKYKGDSTVRELKAKLAGVEEELQRAKQ 294
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEE 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 295 EVLSLRRenctLDTECHEKEKHINQLQTKVAVLEQEIK-DKDQLVLRTKEAFDTIQEQKQvALEENGEKNQIQLGKLEAT 373
Cdd:COG4717  154 RLEELRE----LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLA-ELEEELEEAQEELEELEEE 228

                        170
                 ....*....|...
gi 568924180 374 IKSLSAELLKANE 386
Cdd:COG4717  229 LEQLENELEAAAL 241
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
236-427 3.32e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 236 KKELETLHQRNIHQLQSRLSELEAANKELTERKykgdSTVRELKAKLAGVEEELQRAKQEVLSLRRE---------NCTL 306
Cdd:COG4717   55 ADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREEleklekllqLLPL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 307 DTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQV---ALEENGEKNQIQLGKLEATIKSLSAELLK 383
Cdd:COG4717  131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEleeLLEQLSLATEEELQDLAEELEELQQRLAE 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 568924180 384 ANEIIKKLQGDLKTLMGKLKlkntvTIQQEKLLAEKEEMLQKER 427
Cdd:COG4717  211 LEEELEEAQEELEELEEELE-----QLENELEAAALEERLKEAR 249
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-481 4.51e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 4.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 236 KKELETLHQRNiHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQR----------AKQEVLSLRRENCT 305
Cdd:PRK03918 178 IERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleelkeeieeLEKELESLEGSKRK 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 306 LDTECHEKEKHINQLQTKVAVLEQEIKDKDQLvlrtKEAFDTIQEQKQVALEENGEKNQIQ--LGKLEATIKSLSAELLK 383
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKEL----KEKAEEYIKLSEFYEEYLDELREIEkrLSRLEEEINGIEERIKE 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 384 ANEI---IKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEE 460
Cdd:PRK03918 333 LEEKeerLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412

                        250       260
                 ....*....|....*....|.
gi 568924180 461 SKQLLKNNEKLitwLNKELNE 481
Cdd:PRK03918 413 RIGELKKEIKE---LKKAIEE 430
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 246-480 4.75e-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: 46.55  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  246 NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVA 325
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  326 VLEQEIkdkdqLVLRTKeafdtIQEQKQVALEENGEKNQIQlgKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK---- 401
Cdd:TIGR04523 198 KLELLL-----SNLKKK-----IQKNKSLESQISELKKQNN--QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEqnki 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  402 ---LKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQflrAKEQEVCR-LQEQLETTVQKLEESKQLLKNNEKLITWLNK 477
Cdd:TIGR04523 266 kkqLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN---QKEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNE 342


                  ...
gi 568924180  478 ELN 480
Cdd:TIGR04523 343 QIS 345
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 236-486 4.87e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.46  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 236 KKELETLHQRNIHQLQSRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLslrrenctldtec 310
Cdd:PRK05771  37 KEELSNERLRKLRSLLTKLSEAldklrSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIK------------- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 311 hEKEKHINQLQTKVAVLEQEIKDKDQLvlrtkEAFDTiqeqkQVALEENGEKNQIQLGKLEATIKS-LSAELLKANEIIK 389
Cdd:PRK05771 104 -ELEEEISELENEIKELEQEIERLEPW-----GNFDL-----DLSLLLGFKYVSVFVGTVPEDKLEeLKLESDVENVEYI 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 390 KlqgdlktlmgKLKLKNTVTIQQEKLLAEK-EEMLQK---ERKESQDAG---QFLRAKEQEVCRLQEQLETTVQKLEESK 462
Cdd:PRK05771 173 S----------TDKGYVYVVVVVLKELSDEvEEELKKlgfERLELEEEGtpsELIREIKEELEEIEKERESLLEELKELA 242

                        250       260
                 ....*....|....*....|....
gi 568924180 463 QllKNNEKLITWlnKELNENQLVR 486
Cdd:PRK05771 243 K--KYLEELLAL--YEYLEIELER 262
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 167-469 4.96e-05

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: 46.65  E-value: 4.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   167 LTRSLDD----VTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSqeLTAEKEKALQTQVQCQQQHEQQKKELETl 242
Cdd:pfam15921  417 LRRELDDrnmeVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS--LTAQLESTKEMLRKVVEELTAKKMTLES- 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   243 HQRNIHQLQSRLSE----LEAANKELTERKYKGDSTVRELKaKLAGVEEELQRAKQEVLSLRrenctldTECHEKEKHIN 318
Cdd:pfam15921  494 SERTVSDLTASLQEkeraIEATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALK-------LQMAEKDKVIE 565

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   319 qlqtkvaVLEQEIKDKDQLVLRTKEAFDTIQ-EQKQVALEENGEKNQIQ------------LGKLEATIKSLSAELLK-A 384
Cdd:pfam15921  566 -------ILRQQIENMTQLVGQHGRTAGAMQvEKAQLEKEINDRRLELQefkilkdkkdakIRELEARVSDLELEKVKlV 638

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   385 NEIIKKLQGDLKTLMGKLKLKNTVTIQQEKL--LAEKEEMLQKE-RKESQDAgqflrakEQEVCRLQEQLETTVQKLEES 461
Cdd:pfam15921  639 NAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNfRNKSEEM-------ETTTNKLKMQLKSAQSELEQT 711


                   ....*...
gi 568924180   462 KQLLKNNE 469
Cdd:pfam15921  712 RNTLKSME 719
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
215-488 5.08e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 5.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 215 TAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRE----LKAKLAGVEEELQ 290
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKEL-AEQLKELEEKLKKYNLEELEKKAEEYEKLKEklikLKGEIKSLKKELE 549

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 291 RAKQevlsLRRENCTLDTECHEKEKHINQLQTKVAVLEQE-IKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQlgK 369
Cdd:PRK03918 550 KLEE----LKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLELKDAEKELEREEKELK--K 623

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 370 LEATIKSLSAELLKANEIIKKLQGDLKTLMGKLklkntvtiQQEKLLAEKEEMLQKERKESQdagqfLRAKEQEVCRLQE 449
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKY--------SEEEYEELREEYLELSRELAG-----LRAELEELEKRRE 690

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 568924180 450 QLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 488
Cdd:PRK03918 691 EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
PTZ00121 PTZ00121
MAEBL; Provisional
 186-485 5.13e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  186 SEKMQELDKlRSEWASHTASLTNKHSQELTAE--KEKA--LQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAAN 261
Cdd:PTZ00121 1456 AKKAEEAKK-KAEEAKKADEAKKKAEEAKKADeaKKKAeeAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  262 KELTERKYKGDSTVREL-KAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR 340
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  341 TKEAFDTIQEQKQvalEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKE 420
Cdd:PTZ00121 1615 AEEAKIKAEELKK---AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568924180  421 EMLQKERKESQDAGQfLRAKEQEVCRLQEQL----ETTVQKLEESKQLLKNNEKLITWLNKELNENQLV 485
Cdd:PTZ00121 1692 EALKKEAEEAKKAEE-LKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
166-367 5.36e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.55  E-value: 5.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 166 SLTRSLDDVTRQLHITQETLSEKMQELDKLRSE----WASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELET 241
Cdd:COG3206  172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 242 LHQ--------RNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVL-SLRRENCTLDTECHE 312
Cdd:COG3206  252 GPDalpellqsPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREAS 331

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568924180 313 KEKHINQLQTKVAVL---EQEIKDKDQLVLRTKEAFDTIQEQ-KQVALEENGEKNQIQL 367
Cdd:COG3206  332 LQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRlEEARLAEALTVGNVRV 390
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 157-477 6.47e-05

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 46.32  E-value: 6.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   157 LKCSKEEKLSLTRSLDDVTRQlhiTQETLSEKMQELDKLRSEwashtasltnkhsQELTAEKEKalqtqvqCQQQHEQQK 236
Cdd:pfam01576   14 LQKVKERQQKAESELKELEKK---HQQLCEEKNALQEQLQAE-------------TELCAEAEE-------MRARLAARK 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   237 KELETLhqrnIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAgvEEELQRAKqevlsLRRENCTLDTECHEKEKH 316
Cdd:pfam01576   71 QELEEI----LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLD--EEEAARQK-----LQLEKVTTEAKIKKLEED 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   317 INQLQTKVAVLEQEIKdkdqlvlrtkeafdtiqeqkqvALEENGEKNQIQLGKLEATIKSLSaellkaneiikklqgdlk 396
Cdd:pfam01576  140 ILLLEDQNSKLSKERK----------------------LLEERISEFTSNLAEEEEKAKSLS------------------ 179

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   397 tlmgklKLKNtvtiQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESK-QLLKNNEKLITWL 475
Cdd:pfam01576  180 ------KLKN----KHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaQLAKKEEELQAAL 249


                   ..
gi 568924180   476 NK 477
Cdd:pfam01576  250 AR 251
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 317-488 6.95e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 6.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 317 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQvALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 396
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 397 TLMGKLKlKNTVTIQQ------EKLLAEKEEMLQKERKES--QDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNN 468
Cdd:COG4942  101 AQKEELA-ELLRALYRlgrqppLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                        170       180
                 ....*....|....*....|
gi 568924180 469 EKLITWLNKELNENQLVRKQ 488
Cdd:COG4942  180 LAELEEERAALEALKAERQK 199
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 157-459 8.35e-05

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 8.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   157 LKCSKEEKLSLTRSLDDVTRQLHITQETLSE-------KMQELDKLRSEwashtasltNKHSQELTAEKEKALQTQVQCQ 229
Cdd:pfam15921  491 LESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlKLQELQHLKNE---------GDHLRNVQTECEALKLQMAEKD 561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   230 QQHEQQKKELETL------HQRNIHQLQSRLSELEaanKELTER----------KYKGDSTVRELKAKLAGVEEE---LQ 290
Cdd:pfam15921  562 KVIEILRQQIENMtqlvgqHGRTAGAMQVEKAQLE---KEINDRrlelqefkilKDKKDAKIRELEARVSDLELEkvkLV 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   291 RAKQE----VLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEEN------- 359
Cdd:pfam15921  639 NAGSErlraVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTrntlksm 718

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   360 ------------GEKNQI-----QLGKLEATIKSLSAELLKAN-------EIIKKLQGDLKTLM---GKLKLKNTVTIQQ 412
Cdd:pfam15921  719 egsdghamkvamGMQKQItakrgQIDALQSKIQFLEEAMTNANkekhflkEEKNKLSQELSTVAtekNKMAGELEVLRSQ 798

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568924180   413 EKLLAEK----EEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLE 459
Cdd:pfam15921  799 ERRLKEKvanmEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 238-333 1.64e-04

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.


Pssm-ID: 428400 [Multi-domain]  Cd Length: 188  Bit Score: 43.03  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  238 ELETlHQRNIHQLQSRLSEL----EAANKELTERKyKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEK 313
Cdd:pfam05266  79 ELEK-HGFDVKAPQSRINKLlslkDRQTKLLEELK-KLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAA 156

                          90       100
                  ....*....|....*....|
gi 568924180  314 EKHINQLQTKVAVLEQEIKD 333
Cdd:pfam05266 157 DKEIARLKSEAEKLEQEIQD 176
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 148-477 1.67e-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: 45.01  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  148 EIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKA------ 221
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykqei 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  222 --LQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVREL--------------------- 278
Cdd:TIGR04523 387 knLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLtnqdsvkeliiknldntresl 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  279 --------------KAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEA 344
Cdd:TIGR04523 467 etqlkvlsrsinkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  345 FDTI-QEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKntvTIQQEKLLAEKEEML 423
Cdd:TIGR04523 547 LNKDdFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK---EKKISSLEKELEKAK 623

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568924180  424 QKERKESQDAGQFLRAKE---QEVCRLQEQLETTVQKLEEskqLLKNNEKLITWLNK 477
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNklkQEVKQIKETIKEIRNKWPE---IIKKIKESKTKIDD 677
PRK12704 PRK12704
phosphodiesterase; Provisional
 260-443 1.73e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 260 ANKELTERKYKGDSTVRELKAKL-AGVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTKVavleqeikdkdqlv 338
Cdd:PRK12704  29 AEAKIKEAEEEAKRILEEAKKEAeAIKKEALLEAKEEIHKLRNE---FEKELRERRNELQKLEKRL-------------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 339 lrtkeafdtiqEQKqvalEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKlklkntvtiQQEKLL-- 416
Cdd:PRK12704  92 -----------LQK----EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---------QLQELEri 147

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568924180 417 ----AE--KEEMLQKERKESQ-DAGQFLRAKEQE 443
Cdd:PRK12704 148 sgltAEeaKEILLEKVEEEARhEAAVLIKEIEEE 181
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 162-470 3.05e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 3.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   162 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLR----SEWASHTASLTN---KHSQELTAEKEKaLQTQVQCQQQHEQ 234
Cdd:pfam01576  299 EELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleEETRSHEAQLQEmrqKHTQALEELTEQ-LEQAKRNKANLEK 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   235 QKKELETLHQrnihQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE 314
Cdd:pfam01576  378 AKQALESENA----ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   315 KHINQLQTKVAVLEQEIKDKDQLV---LRTKEAFDT---IQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLkanEII 388
Cdd:pfam01576  454 GKNIKLSKDVSSLESQLQDTQELLqeeTRQKLNLSTrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS---DMK 530

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   389 KKLQGDLKTLMGKLKLKntvtiqqEKLLAEKEEMLQKERKESQDAGQFLRAKEqevcRLQEQLETTVQKLEESKQLLKNN 468
Cdd:pfam01576  531 KKLEEDAGTLEALEEGK-------KRLQRELEALTQQLEEKAAAYDKLEKTKN----RLQQELDDLLVDLDHQRQLVSNL 599


                   ..
gi 568924180   469 EK 470
Cdd:pfam01576  600 EK 601
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
183-491 3.31e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 183 ETLSEKMQELDKLRSEWASHTASLtnkhsQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRN-IHQLQSRLSELEAAN 261
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQEEL-----EELEEELEELEAELEELREELEKLEKLLQLLPLYQeLEALEAELAELPERL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 262 KELTERKykgdSTVRELKAKLAGVEEELQRAKQEVLSLRREnCTLDTECHEKE--KHINQLQTKVAVLEQEIKDKDQLVL 339
Cdd:COG4717  149 EELEERL----EELRELEEELEELEAELAELQEELEELLEQ-LSLATEEELQDlaEELEELQQRLAELEEELEEAQEELE 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 340 RTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEK 419
Cdd:COG4717  224 ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568924180 420 EEMLQKERK----ESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKlitwLNKELNENQLVRKQDTL 491
Cdd:COG4717  304 AEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEE----LEEELQLEELEQEIAAL 375
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 166-358 3.38e-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: 43.60  E-value: 3.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 166 SLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLtnkhsqeltAEKEKALQTQVQCQQQHEQQKKELETLHQR 245
Cdd:COG4942   59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQPPLALLLSPE 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 246 NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVA 325
Cdd:COG4942  130 DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELA 209

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568924180 326 VLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEE 358
Cdd:COG4942  210 ELAAELAELQQEAEELEALIARLEAEAAAAAER 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
276-463 3.39e-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: 3.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  276 RELKAKLAGVEEELQRAKQEVLSLRREncTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAfdtIQEQKQVA 355
Cdd:COG4913   265 AAARERLAELEYLRAALRLWFAQRRLE--LLEAELEELRAELARLEAELERLEARLDALREELDELEAQ---IRGNGGDR 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  356 LEEngeknqiqlgkLEATIKSLSAELLKANEIIKKLQGDLKTlmgkLKLKNTVTIQQ-EKLLAEKEEMLQKERKESQDAG 434
Cdd:COG4913   340 LEQ-----------LEREIERLERELEERERRRARLEALLAA----LGLPLPASAEEfAALRAEAAALLEALEEELEALE 404

                         170       180
                  ....*....|....*....|....*....
gi 568924180  435 QFLRAKEQEVCRLQEQLETTVQKLEESKQ 463
Cdd:COG4913   405 EALAEAEAALRDLRRELRELEAEIASLER 433
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
160-490 4.57e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 160 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWAShtaslTNKHSQELTAEKEKALQTQVQCQQQHEQQKKEL 239
Cdd:COG4372   29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ-----ARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 240 ETLhQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRREnctldTECHEKEKHINQ 319
Cdd:COG4372  104 ESL-QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE-----LAALEQELQALS 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 320 LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 399
Cdd:COG4372  178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 400 GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQ-----FLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITW 474
Cdd:COG4372  258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALelkllALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337

                        330
                 ....*....|....*.
gi 568924180 475 LNKELNENQLVRKQDT 490
Cdd:COG4372  338 ELADLLQLLLVGLLDN 353
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
254-478 4.59e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 254 LSELEAANKELteRKYKGDSTVRELKaKLAGVEEELQRAKQEVLSLRRenctLDTECHEKEKHINQLQTKVAVLEQEIKD 333
Cdd:COG4717   48 LERLEKEADEL--FKPQGRKPELNLK-ELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEK 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 334 KDQLvlrtKEAFDTIQEQKQvaLEENGEKNQIQLGKLEA---TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 410
Cdd:COG4717  121 LEKL----LQLLPLYQELEA--LEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568924180 411 QQeklLAEKEEMLQKERKEsqdagqflrakeqevcrLQEQLETTVQKLEESKQLLKNNEKLITWLNKE 478
Cdd:COG4717  195 QD---LAEELEELQQRLAE-----------------LEEELEEAQEELEELEEELEQLENELEAAALE 242
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
279-460 6.76e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  279 KAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKdkdqlVLRTKEAFDTIQEQKQVALEE 358
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAELERLDAS 683

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  359 NGEKNQI--QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-----LKNTVTIQQEKLLAEKEEMLQKERKEsQ 431
Cdd:COG4913   684 SDDLAALeeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDelqdrLEAAEDLARLELRALLEERFAAALGD-A 762

                         170       180
                  ....*....|....*....|....*....
gi 568924180  432 DAGQFLRAKEQEVCRLQEQLETTVQKLEE 460
Cdd:COG4913   763 VERELRENLEERIDALRARLNRAEEELER 791
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 148-483 6.90e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 6.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   148 EIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQEL-DKLRSEWASHTASLTNKHSQELTAEKEKALQTQV 226
Cdd:TIGR00618  187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   227 QCQQQHEQQKKELETLHQR-NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCT 305
Cdd:TIGR00618  267 ARIEELRAQEAVLEETQERiNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   306 LDTeCHEKEKHINQlQTKVAVLEQEIKDKdqlvlrtkeafdtiqeqkQVALEENGEKNQIQLGKLEATIKSLSAELlkan 385
Cdd:TIGR00618  347 LQT-LHSQEIHIRD-AHEVATSIREISCQ------------------QHTLTQHIHTLQQQKTTLTQKLQSLCKEL---- 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   386 EIIKKLQGDLKTLMGKLKlkntvTIQQEKLLAEKEEMLQKERKE-----SQDAGQFLRAKEQEVCRLQEQLETTVQKLEE 460
Cdd:TIGR00618  403 DILQREQATIDTRTSAFR-----DLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHLQESAQSLKEREQQLQT 477

                          330       340
                   ....*....|....*....|...
gi 568924180   461 SKQLLKNNEKLITWLNKELNENQ 483
Cdd:TIGR00618  478 KEQIHLQETRKKAVVLARLLELQ 500
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
219-362 7.24e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 7.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 219 EKALQTQVQCQQQHEQQKKELETLH-QRNIHQLQSRLSELEAANKELteRKYkgdstVRELKAKLAGVEEELQRAKQEVL 297
Cdd:COG2433  379 EEALEELIEKELPEEEPEAEREKEHeERELTEEEEEIRRLEEQVERL--EAE-----VEELEAELEEKDERIERLERELS 451

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568924180 298 SLRREnctLDTEcHEKEKHINQLQTKVAVLEQEIKDKDQlvlRTKEAFDTIQEQKQVA-LEENGEK 362
Cdd:COG2433  452 EARSE---ERRE-IRKDREISRLDREIERLERELEEERE---RIEELKRKLERLKELWkLEHSGEL 510
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 182-434 7.34e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 7.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 182 QETLSEKMQELDKLRSEwashtASLTNKHSQELTAEKEKALqtqvqcqqqheqqkKELETLhQRNIHQLQSRLSELEAAN 261
Cdd:COG4942   19 ADAAAEAEAELEQLQQE-----IAELEKELAALKKEEKALL--------------KQLAAL-ERRIAALARRIRALEQEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 262 KELTERkykgdstVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE----KHINQLQTKVAVLEQEIKDKDQL 337
Cdd:COG4942   79 AALEAE-------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 338 VLRTKEAFDTIQEQKQVALEENGEKNQiQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLA 417
Cdd:COG4942  152 AEELRADLAELAALRAELEAERAELEA-LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230

                        250
                 ....*....|....*..
gi 568924180 418 EKEEMLQKERKESQDAG 434
Cdd:COG4942  231 RLEAEAAAAAERTPAAG 247
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-465 8.66e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 8.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 170 SLDDVTRQLHITQETlsEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKalqtqvqcqqqhEQQKKELETLHQRnihq 249
Cdd:PRK02224 188 SLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETR------------DEADEVLEEHEER---- 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 250 lQSRLSELEAANKELTERKYKGDST-------VRELKAKLAGVEEE---------LQRAKQEVLSLRREncTLDTECHEK 313
Cdd:PRK02224 250 -REELETLEAEIEDLRETIAETEREreelaeeVRDLRERLEELEEErddllaeagLDDADAEAVEARRE--ELEDRDEEL 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 314 EKHINQLQTKVAVLEQEIKdkdqlvlRTKEAFDTIQEQKQVALEENGEknqiqlgkLEATIKSLSAELLKANEIIKKLQG 393
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAE-------SLREDADDLEERAEELREEAAE--------LESELEEAREAVEDRREEIEELEE 391

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568924180 394 DLKTLMGKLklkNTVTIQQEKlLAEKEEMLQKERKEsqdagqfLRAKEQEvcrLQEQLETTVQKLEESKQLL 465
Cdd:PRK02224 392 EIEELRERF---GDAPVDLGN-AEDFLEELREERDE-------LREREAE---LEATLRTARERVEEAEALL 449
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 283-470 8.83e-04

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: 42.65  E-value: 8.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   283 AGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEK 362
Cdd:pfam02463  162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   363 NQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQ 442
Cdd:pfam02463  242 LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321

                          170       180
                   ....*....|....*....|....*...
gi 568924180   443 EVCRLQEQLETTVQKLEESKQLLKNNEK 470
Cdd:pfam02463  322 EKKKAEKELKKEKEEIEELEKELKELEI 349
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 183-489 9.37e-04

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: 42.73  E-value: 9.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   183 ETLSEKMQELDKLRSEWASHTASLTNKHS-QELTAEKEKALQTQVQCQQQHEQQKKELETlHQRNIHQLQSRLSELEAAN 261
Cdd:TIGR00606  795 ERFQMELKDVERKIAQQAAKLQGSDLDRTvQQVNQEKQEKQHELDTVVSKIELNRKLIQD-QQEQIQHLKSKTNELKSEK 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   262 KELTERKYKGDSTVRELKAKLAGVEE---ELQRAKQEVLSLRRencTLDTECHEKEKHINQLQTKVAVLEQEIKDK---- 334
Cdd:TIGR00606  874 LQIGTNLQRRQQFEEQLVELSTEVQSlirEIKDAKEQDSPLET---FLEKDQQEKEELISSKETSNKKAQDKVNDIkekv 950

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   335 DQLVLRTKEAFDTIQEQKQValeengeknqiQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtvtiQQEK 414
Cdd:TIGR00606  951 KNIHGYMKDIENKIQDGKDD-----------YLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK----IQER 1015

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568924180   415 LLAEkEEMLQKERKESQDAGQFLRAKEQEVCRLQ-EQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 489
Cdd:TIGR00606 1016 WLQD-NLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKE 1090
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 168-367 9.42e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 9.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   168 TRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLtNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLhQRNI 247
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-EKEIENLNGKKEELEEELEELEAALRDLESRLGDL-KKER 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   248 HQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELqrakQEVLSLRREnctlDTECHEKEKHINQLQTKVAVL 327
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL----SEIEDPKGE----DEEIPEEELSLEDVQAELQRV 963

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 568924180   328 EQEIKDKDQLVLR-------TKEAFDTIQEQKQVaLEEngEKNQIQL 367
Cdd:TIGR02169  964 EEEIRALEPVNMLaiqeyeeVLKRLDELKEKRAK-LEE--ERKAILE 1007
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
183-476 9.76e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 9.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 183 ETLSEKMQELDKLRSEWAS---HTASLTNKHsqeltaEKEKALQTQVQCQQQHEQQKKELETLhqrnIHQLQSRLSELEA 259
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDleeEVEEVEERL------ERAEDLVEAEDRIERLEERREDLEEL----IAERRETIEEKRE 537

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 260 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKhINQLQTKVAVLEQEIKDkdqlvL 339
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIER-----L 611

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 340 RTK-EAFDTIQEQKQVALEENGEKNQIQLGKL-EATIKSLSAELLKANEIIKKLQGDLKTLMGKL-KLKNTVTIQQEKLl 416
Cdd:PRK02224 612 REKrEALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEIGAVENEL- 690

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568924180 417 aEKEEMLQKERKESQDAGQFLRAKEQEVcrlqEQLETTVQKLE-ESKQllKNNEKLITWLN 476
Cdd:PRK02224 691 -EELEELRERREALENRVEALEALYDEA----EELESMYGDLRaELRQ--RNVETLERMLN 744
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 246-491 1.26e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.93  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  246 NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQlqtkva 325
Cdd:TIGR04523  69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDK------ 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  326 VLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQlgKLEATIKSLSAELLKAN---EIIKKLQGDLKTLMGKL 402
Cdd:TIGR04523 143 FLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL--NIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQI 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  403 -KLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVcRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 481
Cdd:TIGR04523 221 sELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN-KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299

                         250
                  ....*....|
gi 568924180  482 NQLVRKQDTL 491
Cdd:TIGR04523 300 LNNQKEQDWN 309
PTZ00121 PTZ00121
MAEBL; Provisional
 186-478 1.51e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  186 SEKMQELDKLRSEWASHTASLTNKHSQELTAEK-EKALQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAANKEL 264
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  265 TERKYKGDSTVRELKAKLAGVEEELQRAKQ----EVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR 340
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEarieEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  341 TKEAFDTIQEQKQValEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLaEKE 420
Cdd:PTZ00121 1642 EAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK-KKA 1718

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568924180  421 EMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKE 478
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 285-485 1.79e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  285 VEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKD-KDQLVLRTKEAFDTIQEQKQVALEENGEKN 363
Cdd:TIGR04523  38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDlNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  364 QI-----QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLR 438
Cdd:TIGR04523 118 QKnklevELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLL 197

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568924180  439 AKEQEVCRLQE------QLETTVQKLEESKQLLKNNeklITWLNKELNENQLV 485
Cdd:TIGR04523 198 KLELLLSNLKKkiqknkSLESQISELKKQNNQLKDN---IEKKQQEINEKTTE 247
PRK12704 PRK12704
phosphodiesterase; Provisional
 351-481 2.02e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 351 QKQVALEENGEKNQIQLGKLEAtiKSLSAE-LLKANEIIKKLQGDLKTlmgKLKLKNTVTIQQEKLLAEKEEMLqKERKE 429
Cdd:PRK12704  30 EAKIKEAEEEAKRILEEAKKEA--EAIKKEaLLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENL-DRKLE 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568924180 430 SqdagqfLRAKEQEvcrLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 481
Cdd:PRK12704 104 L------LEKREEE---LEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 176-423 2.20e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 41.36  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   176 RQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL--HQRNIHQLQSR 253
Cdd:pfam12128  276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaaDQEQLPSWQSE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   254 LSELEAANKELT------ERKYKG--DSTVRELKAKLAGVEEELQRAKQEVlSLRRENCTLDTECHEkekhiNQLQTKVA 325
Cdd:pfam12128  356 LENLEERLKALTgkhqdvTAKYNRrrSKIKEQNNRDIAGIKDKLAKIREAR-DRQLAVAEDDLQALE-----SELREQLE 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   326 VLEQEIKD-KDQLVLRTKEA-FDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK 403
Cdd:pfam12128  430 AGKLEFNEeEYRLKSRLGELkLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR 509

                          250       260
                   ....*....|....*....|
gi 568924180   404 LKNTVTIQQEKLLAEKEEML 423
Cdd:pfam12128  510 QASRRLEERQSALDELELQL 529
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
244-385 2.58e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  244 QRNIHQLQSRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQRAKQEVLS--------LRRENCTLDTECHEKEK 315
Cdd:COG4913   287 QRRLELLEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERER 359

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568924180  316 HINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQE---QKQVALEENGEKNQIQLGKLEATIKSLSAEL--LKAN 385
Cdd:COG4913   360 RRARLEALLAALGLPLPASAEEFAALRAEAAALLEaleEELEALEEALAEAEAALRDLRRELRELEAEIasLERR 434
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 250-466 2.83e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.59  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 250 LQSRLSELEAANKELTERKYKGDSTvrELKAKLAGVEEELQRAKQEVLSLRrenctLDtECHEKEKHIN-QLQTKVAVLE 328
Cdd:PRK04778 228 LPDQLQELKAGYRELVEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELD-----LD-EAEEKNEEIQeRIDQLYDILE 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 329 QEIKDK---DQLVLRTKEAFDTIQEQKQVALEEN---GEKNQIQLGKLEaTIKSLSAELlkaNEIIKKLQGDLKTLMGKL 402
Cdd:PRK04778 300 REVKARkyvEKNSDTLPDFLEHAKEQNKELKEEIdrvKQSYTLNESELE-SVRQLEKQL---ESLEKQYDEITERIAEQE 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568924180 403 KLKNTVTIQQEKLLaEKEEMLQKERKESQDAGQFLRAKEQEVcrlQEQLETTVQKLEESKQLLK 466
Cdd:PRK04778 376 IAYSELQEELEEIL-KQLEEIEKEQEKLSEMLQGLRKDELEA---REKLERYRNKLHEIKRYLE 435
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 243-483 2.88e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  243 HQRNI--HQLQSRLSELEAAN-KELTERKYKGDSTVRELKAKLAGVEEELQR-----AKQEVLSLRRENCTLDTECHEKE 314
Cdd:pfam17380 280 HQKAVseRQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERK 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  315 KHINQL-QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ----KQVALEENGEKNQIQLGKLEatIKSLSAELLKANEI-I 388
Cdd:pfam17380 360 RELERIrQEEIAMEISRMRELERLQMERQQKNERVRQEleaaRKVKILEEERQRKIQQQKVE--MEQIRAEQEEARQReV 437

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  389 KKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQdagqflraKEQEVCRLQEQLETTV--QKLEESKQLLK 466
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--------KEKRDRKRAEEQRRKIleKELEERKQAMI 509

                         250
                  ....*....|....*..
gi 568924180  467 NNEKLITWLNKELNENQ 483
Cdd:pfam17380 510 EEERKRKLLEKEMEERQ 526
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 157-480 3.19e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.86  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  157 LKCSKEEKLSLTRSLDDVTRQLH---ITQETLSEKMQeldklrsewashtasLTNKHSQELTAEKEKALQTQVQCQQQHE 233
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQrsmSTQKALEEDLQ---------------IATKTICQLTEEKEAQMEELNKAKAAHS 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  234 QQKKELETLH--------------QRNIHQLQSRLSELEAANKELTE-RKYKGDSTVR--ELKAKLAGVEEELQRAKQ-- 294
Cdd:pfam05483 349 FVVTEFEATTcsleellrteqqrlEKNEDQLKIITMELQKKSSELEEmTKFKNNKEVEleELKKILAEDEKLLDEKKQfe 428

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  295 ---EVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIqeqKQVALEENGEKNQIQLGKLE 371
Cdd:pfam05483 429 kiaEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL---KNIELTAHCDKLLLENKELT 505

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  372 ATIKSLSAELLKANEII-------KKLQGDLKTLMGK-LKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQF------- 436
Cdd:pfam05483 506 QEASDMTLELKKHQEDIinckkqeERMLKQIENLEEKeMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIeyevlkk 585

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 568924180  437 ---LRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELN 480
Cdd:pfam05483 586 ekqMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 161-475 3.57e-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: 40.73  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   161 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKE-- 238
Cdd:pfam02463  222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKse 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   239 ---LETLHQRNIHQLQSRLSELEAANKELTERKykgdstvrELKAKLAGVEEELQRAKQEVLslrrenctldtechEKEK 315
Cdd:pfam02463  302 llkLERRKVDDEEKLKESEKEKKKAEKELKKEK--------EEIEELEKELKELEIKREAEE--------------EEEE 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   316 HINQLQTKVAVLEQEIKDKdqlVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDL 395
Cdd:pfam02463  360 ELEKLQEKLEQLEEELLAK---KKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   396 KTLmgkLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVcRLQEQLETTVQKLEESKQLLKNNEKLITWL 475
Cdd:pfam02463  437 ESI---ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL-QEQLELLLSRQKLEERSQKESKARSGLKVL 512
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 157-488 4.23e-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: 40.42  E-value: 4.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   157 LKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHsqeltaEKEKALQTQVQCQQQHEQQK 236
Cdd:TIGR00606  212 LKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM------KLDNEIKALKSRKKQMEKDN 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   237 KELEtlhqrnihqlQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTE------- 309
Cdd:TIGR00606  286 SELE----------LKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEqgrlqlq 355

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   310 -----CH----EKEKHINQLQTKVAVLEQ------EIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATI 374
Cdd:TIGR00606  356 adrhqEHirarDSLIQSLATRLELDGFERgpfserQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEK 435

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   375 KSLSAELLKANEIIKKLQGDLKTLMGKLKlknTVTIQQEKLLAEKEEMLQKERKESQdagqfLRAKEQEVCRLQEQLETT 454
Cdd:TIGR00606  436 KGLGRTIELKKEILEKKQEELKFVIKELQ---QLEGSSDRILELDQELRKAERELSK-----AEKNSLTETLKKEVKSLQ 507

                          330       340       350
                   ....*....|....*....|....*....|....
gi 568924180   455 VQKLEESKQLLKNNEKlitwlNKELNENQLVRKQ 488
Cdd:TIGR00606  508 NEKADLDRKLRKLDQE-----MEQLNHHTTTRTQ 536
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 286-408 4.62e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.66  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 286 EEELQRAKQEVLSLrrenctLDTEchekEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVAL-EENGEKNQ 364
Cdd:cd22656  109 DEELEEAKKTIKAL------LDDL----LKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLtDEGGAIAR 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568924180 365 IQLGKLEATIKSLSAELL-KANEIIKKLQGDLKTLMGKLKLKNTV 408
Cdd:cd22656  179 KEIKDLQKELEKLNEEYAaKLKAKIDELKALIADDEAKLAAALRL 223
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 160-444 4.70e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.34  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   160 SKEEKLSLTRSLDDVTRQLHITQetlseKMQELDKLRSEWASHTASLTN---KHSQELTAEKEKALQTQVQCQQQHEQQK 236
Cdd:TIGR00618  614 QHALLRKLQPEQDLQDVRLHLQQ-----CSQELALKLTALHALQLTLTQervREHALSIRVLPKELLASRQLALQKMQSE 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   237 KELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCtldteCHEKEKH 316
Cdd:TIGR00618  689 KEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVL-----KARTEAH 763

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   317 INQLQTKVAVLE--QEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAE---LLKANEIIKKL 391
Cdd:TIGR00618  764 FNNNEEVTAALQtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEeeqFLSRLEEKSAT 843

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568924180   392 QGDLKTLMGKL----KLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEV 444
Cdd:TIGR00618  844 LGEITHQLLKYeecsKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHEI 900
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
169-477 5.25e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 169 RSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLT--NKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQrN 246
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE-D 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 247 IHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEV--LSLRRENctLDTECHEKEKHINQLQTKV 324
Cdd:PRK02224 351 ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFgdAPVDLGN--AEDFLEELREERDELRERE 428

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 325 AVLEQEIKDKDQLVLRTKEAFDT---------IQEQKQV-ALEENGEKN---QIQLGKLEATIKSLSAELLKANEIiKKL 391
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLEAgkcpecgqpVEGSPHVeTIEEDRERVeelEAELEDLEEEVEEVEERLERAEDL-VEA 507

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 392 QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 471
Cdd:PRK02224 508 EDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER 587


                 ....*.
gi 568924180 472 ITWLNK 477
Cdd:PRK02224 588 IESLER 593
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 247-423 5.42e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 38.73  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  247 IHQLQSRLSELEAANKELTERKY-------KGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQ 319
Cdd:pfam15619  20 LAELQSKLEELRKENRLLKRLQKrqekalgKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLR 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  320 LQTKVAVLEQEIKDKDqlvLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 399
Cdd:pfam15619 100 LRDQLKRLEKLSEDKN---LAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKKHKEAQEEVKILQ 176

                         170       180
                  ....*....|....*....|....
gi 568924180  400 GKLKLKNTvtiqqekLLAEKEEML 423
Cdd:pfam15619 177 EEIERLQQ-------KLKEKEREL 193
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 244-449 6.74e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 39.02  E-value: 6.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  244 QRNIHQLQSRLSELEAANkELTERKYKGDSTVRELKAKLAGVEEELQR--AKQEVLSLRRENCTLDTEchEKEKHINQLQ 321
Cdd:pfam15905 121 SASVASLEKQLLELTRVN-ELLKAKFSEDGTQKKMSSLSMELMKLRNKleAKMKEVMAKQEGMEGKLQ--VTQKNLEHSK 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  322 TKVAVLEQEIKDKDQLVLRTK----EAFDTIQEQKQVAleENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 397
Cdd:pfam15905 198 GKVAQLEEKLVSTEKEKIEEKseteKLLEYITELSCVS--EQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSK 275

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568924180  398 LMGKLKLK-NTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQE 449
Cdd:pfam15905 276 QIKDLNEKcKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
Sas6_CC pfam18594
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of ...
 146-171 7.51e-03

Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of spindle assembly abnormal protein 6 (Sas6). The highly conserved protein SAS-6 constitutes the center of the cartwheel assembly that scaffolds centrioles early in their biogenesis.Structural analysis of Sas6 show that similar to XLF, and XRCC4 it forms a parallel coiled-coil dimer.


Pssm-ID: 408377 [Multi-domain]  Cd Length: 30  Bit Score: 34.57  E-value: 7.51e-03
                          10        20
                  ....*....|....*....|....*.
gi 568924180  146 DVEIKKFLAGCLKCSKEEKLSLTRSL 171
Cdd:pfam18594   1 DSEVKKYLADCLKSLKEEKQLLEQKL 26
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 152-385 7.70e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 7.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 152 FLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASL--TNKHSQELTAEKEKALQTQVQCQ 229
Cdd:COG4942   10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIaaLARRIRALEQELAALEAELAELE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 230 QQHEQQKKELETLHQRNIHQL-----QSRLSELEA-ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRREn 303
Cdd:COG4942   90 KEIAELRAELEAQKEELAELLralyrLGRQPPLALlLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE- 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180 304 ctLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQvALEENGEKNQIQLGKLEATIKSLSAELLK 383
Cdd:COG4942  169 --LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA-ELQQEAEELEALIARLEAEAAAAAERTPA 245


                 ..
gi 568924180 384 AN 385
Cdd:COG4942  246 AG 247
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 147-481 7.73e-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: 39.64  E-value: 7.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   147 VEIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSE-------KMQELDKLRSEWASHTASLTNK-----HSQEL 214
Cdd:TIGR00606  496 TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQmemltkdKMDKDEQIRKIKSRHSDELTSLlgyfpNKKQL 575

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   215 TAEKEKALQTQVQCQQQHEQQKKELETLHQrNIHQLQSRLSELEAANKELTERKYKGDSTvRELKAKLAGVEEELQRAKQ 294
Cdd:TIGR00606  576 EDWLHSKSKEINQTRDRLAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSK 653

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   295 EVLSLRRENCTLD---TECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLE 371
Cdd:TIGR00606  654 QRAMLAGATAVYSqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP 733

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   372 A----------TIKSLSAELLKANEIIKKLQGD-------LKTLMGKLKLKN------TVTIQQEKLLAEKEEMLQKERK 428
Cdd:TIGR00606  734 GrqsiidlkekEIPELRNKLQKVNRDIQRLKNDieeqetlLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAA 813

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 568924180   429 ESQDAGQFLRAKE--QEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 481
Cdd:TIGR00606  814 KLQGSDLDRTVQQvnQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 250-465 8.19e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.42  E-value: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  250 LQSRLSELEAANKELTERKYKGDstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQ 329
Cdd:pfam10174 441 LEEALSEKERIIERLKEQRERED---RERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDS 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180  330 EIKDKDQLVLRTKEAFDTIQEQKQVAleENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 409
Cdd:pfam10174 518 KLKSLEIAVEQKKEECSKLENQLKKA--HNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENEK 595

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568924180  410 IQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEV--------------------CRLQEQLETTVQKLEESKQLL 465
Cdd:pfam10174 596 NDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMkkkgaqlleearrrednladNSQQLQLEELMGALEKTRQEL 671
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 163-482 9.35e-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: 39.18  E-value: 9.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   163 EKLSLTRSLDDVTRQLHITQETLSEKMQELDKlrsewashtasltNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL 242
Cdd:pfam02463  660 EKSEVKASLSELTKELLEIQELQEKAESELAK-------------EEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   243 HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAgvEEELQRAKQEVLSLRRENCTLDTECHEKEKhinqlqt 322
Cdd:pfam02463  727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS--ELSLKEKELAEEREKTEKLKVEEEKEEKLK------- 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   323 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKQVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKL 402
Cdd:pfam02463  798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEE 877

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568924180   403 KLKntvtiqQEKLLAEKEEMLQKERKESQdagqflrAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNEN 482
Cdd:pfam02463  878 ELE------EQKLKDELESKEEKEKEEKK-------ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEE 944
 
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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