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Conserved domains on  [gi|1907152297|ref|XP_036019244|]
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spindle assembly abnormal protein 6 homolog isoform X3 [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 7.18e-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: 190.84  E-value: 7.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297   4 VLFQQLVPLLVKCKDCEERRGSVRVSIELQSlSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAF 83
Cdd:cd10142     1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152297  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 ...
 165-450 1.56e-15

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: 80.49  E-value: 1.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  165 LSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasltnkhSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQ 244
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  245 R------NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHIN 318
Cdd:TIGR02168  741 EveqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  319 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907152297  399 GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAgqflrakEQEVCRLQEQL 450
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGL-------EVRIDNLQERL 945
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 8.01e-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: 34.18  E-value: 8.01e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907152297 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 7.18e-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: 190.84  E-value: 7.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297   4 VLFQQLVPLLVKCKDCEERRGSVRVSIELQSlSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAF 83
Cdd:cd10142     1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152297  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 7.21e-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: 106.89  E-value: 7.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  44 LVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCMQEhaketprfllQLLSSATLLENSPVLL 123
Cdd:pfam16531   1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKE----------PNLLVFLIQDDGTATL 70

                          90
                  ....*....|....*...
gi 1907152297 124 NVVETNPFKHLIHLSLKL 141
Cdd:pfam16531  71 VFIENNEFKNLEHLSLDF 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-450 1.56e-15

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: 80.49  E-value: 1.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  165 LSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasltnkhSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQ 244
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  245 R------NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHIN 318
Cdd:TIGR02168  741 EveqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  319 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907152297  399 GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAgqflrakEQEVCRLQEQL 450
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGL-------EVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-482 1.26e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 184 TLSEKMQELDK----LRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEA 259
Cdd:COG1196   217 ELKEELKELEAelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 260 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVL 339
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 340 RTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKE 419
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907152297 420 EMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE-KLITWLNKELNENQ 482
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
160-488 1.43e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.68  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 160 SKEEKLS-LTRSLDDVTRQL------HITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKalqtqvqcqqqh 232
Cdd:PRK03918  335 EKEERLEeLKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE------------ 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 233 eqQKKELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVREL------------KAKLAGVEEELQRAKQEVLSLR 300
Cdd:PRK03918  403 --IEEEISKITAR-IGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrkelleeyTAELKRIEKELKEIEEKERKLR 479

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 301 RENCTLDTECHEKEKHINQLQTkvavLEQEIKDKDQLvlrtkEAFDtIQEQKVALEENgEKNQIQLGKLEATIKSLSAEL 380
Cdd:PRK03918  480 KELRELEKVLKKESELIKLKEL----AEQLKELEEKL-----KKYN-LEELEKKAEEY-EKLKEKLIKLKGEIKSLKKEL 548

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 381 LKANEIIKKL----------QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQL 450
Cdd:PRK03918  549 EKLEELKKKLaelekkldelEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1907152297 451 ETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 488
Cdd:PRK03918  629 DKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE 666
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 250-470 3.20e-07

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: 53.36  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 250 LQSRLSELEAANKELterkykgdstVRELKAKLAGVEEELQRAKqevlslrRENCTLDTECHEKEKHINQLQTKVAVLEQ 329
Cdd:pfam07888  32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYK-------RDREQWERQRRELESRVAELKEELRQSRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 330 EIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 409
Cdd:pfam07888  95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152297 410 QQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 470
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 286-407 7.85e-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: 38.89  E-value: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 286 EEELQRAKQEVLSLrrenctLDTEchekEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVAL--EENGEKNQ 363
Cdd:cd22656   109 DEELEEAKKTIKAL------LDDL----LKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIAR 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907152297 364 IQLGKLEATIKSLSAELL-KANEIIKKLQGDLKTLMGKLKLKNTV 407
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 8.01e-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: 34.18  E-value: 8.01e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907152297 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 7.18e-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: 190.84  E-value: 7.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297   4 VLFQQLVPLLVKCKDCEERRGSVRVSIELQSlSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAF 83
Cdd:cd10142     1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152297  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 7.21e-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: 106.89  E-value: 7.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  44 LVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCMQEhaketprfllQLLSSATLLENSPVLL 123
Cdd:pfam16531   1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKE----------PNLLVFLIQDDGTATL 70

                          90
                  ....*....|....*...
gi 1907152297 124 NVVETNPFKHLIHLSLKL 141
Cdd:pfam16531  71 VFIENNEFKNLEHLSLDF 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-450 1.56e-15

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: 80.49  E-value: 1.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  165 LSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasltnkhSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQ 244
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  245 R------NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHIN 318
Cdd:TIGR02168  741 EveqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  319 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907152297  399 GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAgqflrakEQEVCRLQEQL 450
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGL-------EVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-482 1.26e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 74.20  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 184 TLSEKMQELDK----LRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEA 259
Cdd:COG1196   217 ELKEELKELEAelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 260 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVL 339
Cdd:COG1196   296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 340 RTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKE 419
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907152297 420 EMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE-KLITWLNKELNENQ 482
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-482 1.92e-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: 70.47  E-value: 1.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  243 HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQT 322
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  323 KVAVLEQEI------KDKDQLVL-RTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 395
Cdd:TIGR02168  317 QLEELEAQLeeleskLDELAEELaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  396 TLMGKLK-LKNTVTI---QQEKLLAEKEEMLQK-ERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 470
Cdd:TIGR02168  397 SLNNEIErLEARLERledRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          250
                   ....*....|..
gi 1907152297  471 ITWLNKELNENQ 482
Cdd:TIGR02168  477 LDAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 167-470 2.59e-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: 2.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  167 LTRsLDDVTRQLHITQETL---SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL- 242
Cdd:TIGR02168  188 LDR-LEDILNELERQLKSLerqAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELe 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  243 -----HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHI 317
Cdd:TIGR02168  267 ekleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  318 NQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ------KVA-LEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKL 390
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQletlrsKVAqLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  391 Q-----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEE------ 459
Cdd:TIGR02168  427 LkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfse 506

                          330
                   ....*....|..
gi 1907152297  460 -SKQLLKNNEKL 470
Cdd:TIGR02168  507 gVKALLKNQSGL 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 236-490 1.89e-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: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 236 KKELETL-HQRNIHQLQSRLSELEAANKELTERKykgdSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKE 314
Cdd:COG1196   219 KEELKELeAELLLLKLRELEAELEELEAELEELE----AELEELEAELAELEAELEELRLELEELELEL-------EEAQ 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 315 KHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEEngeknqiQLGKLEATIKSLSAELLKANEIIKKLQGDL 394
Cdd:COG1196   288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEELEEAEAEL 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 395 KTLMGKLKLKNTVTIQ-QEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITW 473
Cdd:COG1196   361 AEAEEALLEAEAELAEaEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440

                         250
                  ....*....|....*..
gi 1907152297 474 LNKELNENQLVRKQDTL 490
Cdd:COG1196   441 EEALEEAAEEEAELEEE 457
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 171-480 5.83e-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: 65.86  E-value: 5.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  171 LDDVTRQLHITQETLSEKMQELDKLRSEwashtasltnkhsqELTAEKEKALQTQVQCQQQHEQQKKELEtlHQRNIHQL 250
Cdd:TIGR02169  179 LEEVEENIERLDLIIDEKRQQLERLRRE--------------REKAERYQALLKEKREYEGYELLKEKEA--LERQKEAI 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  251 QSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEvlslrrENCTLDTECHEKEKHINQLQTKVAVLEQE 330
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERE 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  331 IKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKlknTVTIQ 410
Cdd:TIGR02169  317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK---DYREK 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  411 QEKLLAEKEEM------LQKERKESQDAGQFLRAK-----------EQEVCRLQEQLETTVQKLEESKQLLKNNEKLITW 473
Cdd:TIGR02169  394 LEKLKREINELkreldrLQEELQRLSEELADLNAAiagieakinelEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYD 473


                   ....*..
gi 1907152297  474 LNKELNE 480
Cdd:TIGR02169  474 LKEEYDR 480
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 248-487 8.02e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 65.34  E-value: 8.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 248 HQLQSRLSELEAankELTERKYkgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVL 327
Cdd:COG1196   216 RELKEELKELEA---ELLLLKL------RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 328 EQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTV 407
Cdd:COG1196   287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 408 TIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 487
Cdd:COG1196   367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 161-433 1.69e-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: 64.31  E-value: 1.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  161 KEEKLSLTRSLDDVTRQLHITQETLSEKM-------QELDKLRSEWASHTASLTNKHSQ-ELTAEKEKALQTQVQCQQQH 232
Cdd:TIGR02168  245 QEELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYALANEISRLEQQkQILRERLANLERQLEELEAQ 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  233 EQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHE 312
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  313 KEKHINQLQTKVAVLEQEIKDKDQLVLRTKeaFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQG 392
Cdd:TIGR02168  405 LEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1907152297  393 DLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAG 433
Cdd:TIGR02168  483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-426 3.01e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 161 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQtqvqcqqqheqqkKELE 240
Cdd:COG1196   245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL-------------EERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 241 TLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKEKHINQL 320
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-------AEAEEELEEL 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK 400
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464

                         250       260
                  ....*....|....*....|....*.
gi 1907152297 401 LKLKNTVTIQQEKLLAEKEEMLQKER 426
Cdd:COG1196   465 LAELLEEAALLEAALAELLEELAEAA 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 262-487 3.06e-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: 63.54  E-value: 3.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  262 KELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKEKHINQLQTKVAVLEQEIKDKDQLVLRT 341
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL-------EELSRQISALRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  342 KEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAEllkaneiIKKLQGDLKTlmgklkLKNTVTIQQEKLLAEKEEM 421
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-------IEQLKEELKA------LREALDELRAELTLLNEEA 819

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907152297  422 LQKERKESQDAGQfLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 487
Cdd:TIGR02168  820 ANLRERLESLERR-IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 236-486 1.34e-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: 61.24  E-value: 1.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  236 KKELETLHQ------RNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTE 309
Cdd:TIGR02169  687 KRELSSLQSelrrieNRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  310 CHEKEKHINQLQTKVAVLEQEIKDkdqlvlrtkEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKK 389
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  390 LQGDLKTLMGKlklKNTVTIQQEKLLAEKEEMLQKERKesqdagqfLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEK 469
Cdd:TIGR02169  838 LQEQRIDLKEQ---IKSIEKEIENLNGKKEELEEELEE--------LEAALRDLESRLGDLKKERDELEAQLRELERKIE 906

                          250
                   ....*....|....*..
gi 1907152297  470 LITWLNKELNENQLVRK 486
Cdd:TIGR02169  907 ELEAQIEKKRKRLSELK 923
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-487 3.16e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 244 QRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTK 323
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRREL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 324 VAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM----- 398
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLealra 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 399 --GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNK 476
Cdd:COG1196   395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474

                         250
                  ....*....|.
gi 1907152297 477 ELNENQLVRKQ 487
Cdd:COG1196   475 LEAALAELLEE 485
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 307-555 3.84e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.07  E-value: 3.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 307 DTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELlkaNEI 386
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GER 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 387 IKKLQ---------------GDLKTLMGKLKLKNTVTIQQEKLLAE---KEEMLQKERKESQDAGQFLRAKEQEVCRLQE 448
Cdd:COG3883    92 ARALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 449 QLETTVQKLEESKQLLKNNEK-LITWLNKELNENQLVRKQDTLGTSATPHSTSNSTIRSGLSPNLNVVDRLNYPSCGIGY 527
Cdd:COG3883   172 ELEAQQAEQEALLAQLSAEEAaAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251

                         250       260
                  ....*....|....*....|....*...
gi 1907152297 528 PVSSALTFQNAFPHVVAAKNTSHPISGP 555
Cdd:COG3883   252 AGAAGAAAGSAGAAGAAAGAAGAGAAAA 279
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 249-478 1.40e-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: 57.08  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 249 QLQSRLSELEAANKELTERKYKgdstVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 328
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKE----LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 329 QEIKDKDQLvlrtkeafdtIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 408
Cdd:COG4942    97 AELEAQKEE----------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 409 IQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKEL 478
Cdd:COG4942   167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 157-490 4.70e-08

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: 56.18  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 157 LKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNkhsqeLTAEKEKALQTQVQCQQQHEQQK 236
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-----LKDEQNKIKKQLSEKQKELEQNN 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 237 KELETLhQRNIHQLQSRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECH 311
Cdd:TIGR04523 281 KKIKEL-EKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 312 EKEKHINQLQTKVAVLEQEIKDKDQ----LVLRTKEAFDTIQEQKVA---LEENGEKNQIQLGKLEATIKSLSAELLKAN 384
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQeiknLESQINDLESKIQNQEKLnqqKDEQIKKLQQEKELLEKEIERLKETIIKNN 439

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 385 EIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQ---LETTVQKLEESK 461
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKI 519

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1907152297 462 QLLKNN-----------EKLITWLNKELNENQLVRKQDTL 490
Cdd:TIGR04523 520 SSLKEKieklesekkekESKISDLEDELNKDDFELKKENL 559
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 250-478 7.05e-08

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.84  E-value: 7.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  250 LQSRLSELEAANKELTERKYkgdstvrELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQ 329
Cdd:TIGR02169  665 GILFSRSEPAELQRLRERLE-------GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  330 EIKDK-------DQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEAT-----IKSLSAELLKANEIIKKLQGDLKTL 397
Cdd:TIGR02169  738 RLEELeedlsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREI 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  398 MGKLKlkntvtiqqeKLLAEKeEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETtvqKLEESKQLLKNNEKLITWLNKE 477
Cdd:TIGR02169  818 EQKLN----------RLTLEK-EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG---KKEELEEELEELEAALRDLESR 883


                   .
gi 1907152297  478 L 478
Cdd:TIGR02169  884 L 884
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
249-462 7.30e-08

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 55.41  E-value: 7.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 249 QLQSRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQ--RAKQEVLSLRRENCTLDTEchekekhINQLQTKVAV 326
Cdd:COG3206   165 NLELRREEARKALEFLEEQ-------LPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQ-------LSELESQLAE 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 327 LEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI--QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-- 402
Cdd:COG3206   231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqe 310

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152297 403 -------LKNTVTI--QQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQ 462
Cdd:COG3206   311 aqrilasLEAELEAlqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
160-488 1.43e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.68  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 160 SKEEKLS-LTRSLDDVTRQL------HITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKalqtqvqcqqqh 232
Cdd:PRK03918  335 EKEERLEeLKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE------------ 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 233 eqQKKELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVREL------------KAKLAGVEEELQRAKQEVLSLR 300
Cdd:PRK03918  403 --IEEEISKITAR-IGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrkelleeyTAELKRIEKELKEIEEKERKLR 479

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 301 RENCTLDTECHEKEKHINQLQTkvavLEQEIKDKDQLvlrtkEAFDtIQEQKVALEENgEKNQIQLGKLEATIKSLSAEL 380
Cdd:PRK03918  480 KELRELEKVLKKESELIKLKEL----AEQLKELEEKL-----KKYN-LEELEKKAEEY-EKLKEKLIKLKGEIKSLKKEL 548

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 381 LKANEIIKKL----------QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQL 450
Cdd:PRK03918  549 EKLEELKKKLaelekkldelEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1907152297 451 ETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 488
Cdd:PRK03918  629 DKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE 666
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 250-470 3.20e-07

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: 53.36  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 250 LQSRLSELEAANKELterkykgdstVRELKAKLAGVEEELQRAKqevlslrRENCTLDTECHEKEKHINQLQTKVAVLEQ 329
Cdd:pfam07888  32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYK-------RDREQWERQRRELESRVAELKEELRQSRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 330 EIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 409
Cdd:pfam07888  95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907152297 410 QQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 470
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 272-443 3.87e-07

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: 51.46  E-value: 3.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 272 DSTVRELKAKLAGVEEELQRAKQEVLSLRrenctldTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 351
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALE-------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 352 K--VALeengeknQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKEEMLQKERKES 429
Cdd:COG1579    89 KeyEAL-------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA-------ELEAELEEKKAELDEELAEL 154

                         170
                  ....*....|....
gi 1907152297 430 QDAGQFLRAKEQEV 443
Cdd:COG1579   155 EAELEELEAEREEL 168
PRK12704 PRK12704
phosphodiesterase; Provisional
 260-419 4.12e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 260 ANKELTERKYKGDSTVRELKAKL-AGVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLV 338
Cdd:PRK12704   29 AEAKIKEAEEEAKRILEEAKKEAeAIKKEALLEAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 339 LRTKEAFDTIQEQKVALEEngeknqiQLGKLEATIKSLSAELLKANEIIKKLQGD------LKTLMGKLKLKNTVTIQQE 412
Cdd:PRK12704  106 EKREEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKEI 178


                  ....*..
gi 1907152297 413 KLLAEKE 419
Cdd:PRK12704  179 EEEAKEE 185
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
160-471 9.10e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.99  E-value: 9.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 160 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasLTNKHSQELTAEKEKAlqtqvqcqqQHEQQKKEL 239
Cdd:PRK03918  201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEE-------IEELEKELESLEGSKR---------KLEEKIREL 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 240 EtlhqRNIHQLQSRLSELEAANKELTERKYKGDSTVR------ELKAKLAGVEEELQRAKQEVLSLRRENctldTECHEK 313
Cdd:PRK03918  265 E----ERIEELKKEIEELEEKVKELKELKEKAEEYIKlsefyeEYLDELREIEKRLSRLEEEINGIEERI----KELEEK 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 314 EKHINQLQTKvavlEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI-QLGKLEATIKSLSAELLKANEIIKKLQG 392
Cdd:PRK03918  337 EERLEELKKK----LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITA 412

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152297 393 DLKTLMGKLKLKNTVTIQQEKllAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLI 471
Cdd:PRK03918  413 RIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 153-394 1.70e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  153 LAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEK---MQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQ 229
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELekrLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE 307

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  230 QQHEQQKKELETLHQR------NIHQLQSRLSELEAANKELTERK------YKGDSTVRE-LKAKLAGVEEELQRAKQEV 296
Cdd:TIGR02169  308 RSIAEKERELEDAEERlakleaEIDKLLAEIEELEREIEEERKRRdklteeYAELKEELEdLRAELEEVDKEFAETRDEL 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  297 LSLRREnctLDTECHEKEKHIN----------QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQL 366
Cdd:TIGR02169  388 KDYREK---LEKLKREINELKReldrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464

                          250       260
                   ....*....|....*....|....*...
gi 1907152297  367 GKLEATIKSLSAELLKANEIIKKLQGDL 394
Cdd:TIGR02169  465 SKYEQELYDLKEEYDRVEKELSKLQREL 492
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
249-492 1.79e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 50.67  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 249 QLQSRLSELEAANKELterkykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 328
Cdd:COG4372    32 QLRKALFELDKLQEEL-----------EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 329 QEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 408
Cdd:COG4372   101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 409 IQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 488
Cdd:COG4372   181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260


                  ....
gi 1907152297 489 TLGT 492
Cdd:COG4372   261 EELE 264
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-480 2.92e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.42  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 170 SLDDVTRQLHITQETlsEKMQELDKLRSEWASHTASLTNKHSQELTAEKekALQTQVQCQQQHEQQKKELETLHQrNIHQ 249
Cdd:PRK02224  188 SLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARE--TRDEADEVLEEHEERREELETLEA-EIED 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 250 LQSRLSELEAANKELTERKYKGDSTVRELKAKLAGV--EEELQRAKQEVLSLRRE--------------NCTLDTECHEK 313
Cdd:PRK02224  263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEAVEARREeledrdeelrdrleECRVAAQAHNE 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 314 E-----KHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQ-------IQLGKLEATIKSLSAELL 381
Cdd:PRK02224  343 EaeslrEDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERD 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 382 KANEIIKKLQGDLKTLMGKLKLKNTV--------------------TI-----QQEKLLAEKEEM--LQKERKESQDAGQ 434
Cdd:PRK02224  423 ELREREAELEATLRTARERVEEAEALleagkcpecgqpvegsphveTIeedreRVEELEAELEDLeeEVEEVEERLERAE 502

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1907152297 435 FLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:PRK02224  503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
217-385 4.30e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 217 EKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEAANKELT--ERKYKGDSTVRELKAKLAGVEEELQRAKQ 294
Cdd:COG4717    75 ELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEE 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 295 EVLSLRRenctLDTECHEKEKHINQLQTKVAVLEQEIK-DKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATI 373
Cdd:COG4717   154 RLEELRE----LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                         170
                  ....*....|..
gi 1907152297 374 KSLSAELLKANE 385
Cdd:COG4717   230 EQLENELEAAAL 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
190-452 4.84e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 4.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  190 QELDKLRSEWASHTASLtnkhsQELTAEKEKALQTQVQCQQQHEQQKKELETL-HQRNIHQLQSRLSELEAANKELterk 268
Cdd:COG4913    617 AELAELEEELAEAEERL-----EALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDDL---- 687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  269 ykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIkdKDQLVLRTKEAFDTI 348
Cdd:COG4913    688 -------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAA 758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  349 QEQKV------ALEENGEKNQIQLGKLEATI---------------KSLSAELLKANEIIKKLQgdlktlmgklklkntv 407
Cdd:COG4913    759 LGDAVerelreNLEERIDALRARLNRAEEELeramrafnrewpaetADLDADLESLPEYLALLD---------------- 822

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907152297  408 TIQQEKLLAEKEEMLQ-KERKESQDAGQFLRAKEQEVCRLQEQLET 452
Cdd:COG4913    823 RLEEDGLPEYEERFKElLNENSIEFVADLLSKLRRAIREIKERIDP 868
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 237-476 8.00e-06

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: 49.02  E-value: 8.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  237 KELETLHQRNIHQLQSRLSELEAANKELTERKYKGD---STVRELKAKLAGVEEELQRAKQEvlslrrenctLDTECHEK 313
Cdd:pfam01576   18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHE----------LESRLEEE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  314 EKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGD 393
Cdd:pfam01576   88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  394 LKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESK-QLLKNNEKLIT 472
Cdd:pfam01576  168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaQLAKKEEELQA 247


                   ....
gi 1907152297  473 WLNK 476
Cdd:pfam01576  248 ALAR 251
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 317-487 8.80e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.22  E-value: 8.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 317 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 396
Cdd:COG4942    22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 397 LMGKLKlKNTVTIQQ------EKLLAEKEEMLQKER---------KESQDAGQFLRAKEQEVCRLQEQLETTVQKLEesk 461
Cdd:COG4942   102 QKEELA-ELLRALYRlgrqppLALLLSPEDFLDAVRrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE--- 177

                         170       180
                  ....*....|....*....|....*.
gi 1907152297 462 QLLKNNEKLITWLNKELNENQLVRKQ 487
Cdd:COG4942   178 ALLAELEEERAALEALKAERQKLLAR 203
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-461 9.68e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 9.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 236 KKELETLHQRNiHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQR----------AKQEVLSLRRENCT 305
Cdd:PRK03918  178 IERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleelkeeieeLEKELESLEGSKRK 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 306 LDTECHEKEKHINQLQTKVAVLEQ------EIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAE 379
Cdd:PRK03918  257 LEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 380 LLKANEIIKKLQG----------------DLKTLMGKL-KLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQE 442
Cdd:PRK03918  337 EERLEELKKKLKElekrleeleerhelyeEAKAKKEELeRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416

                         250
                  ....*....|....*....
gi 1907152297 443 VCRLQEQLETTVQKLEESK 461
Cdd:PRK03918  417 LKKEIKELKKAIEELKKAK 435
HD_XRCC4-like_N cd22210
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ...
 41-144 1.26e-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: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  41 RKDLVIRLTDDtdpFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCmqehAKETPRFLLQLlssaTLLENSP 120
Cdd:cd22210    25 ERGLRLHVSDD---AFLWTGEVSESDISQLKNDQGILVDFASFPGKLRSALEKC----ILASDRFTFVL----TIRGDEA 93

                          90       100
                  ....*....|....*....|....
gi 1907152297 121 VLlnVVETNPFKHLIHLSLKLLPG 144
Cdd:cd22210    94 YL--KLVEILDEQLPHITFALRKV 115
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 166-401 1.46e-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: 47.45  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 166 SLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLtnkhsqeltAEKEKALQTQVQCQQQHEQQKKELETLHQR 245
Cdd:COG4942    59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQPPLALLLSPE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 246 NIHQLQSRLSELEAANKELTERkykgdstVRELKAKLagveEELQRAKQEvlslrrenctLDTECHEKEKHINQLQTKVA 325
Cdd:COG4942   130 DFLDAVRRLQYLKYLAPARREQ-------AEELRADL----AELAALRAE----------LEAERAELEALLAELEEERA 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907152297 326 VLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKnqiqlgkLEATIKSLSAELLKANEiiKKLQGDLKTLMGKL 401
Cdd:COG4942   189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEE-------LEALIARLEAEAAAAAE--RTPAAGFAALKGKL 255
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 236-485 1.71e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 48.00  E-value: 1.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 236 KKELETLHQRNIHQLQSRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLslrrenctldtec 310
Cdd:PRK05771   37 KEELSNERLRKLRSLLTKLSEAldklrSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIK------------- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 311 hEKEKHINQLQTKVAVLEQEIKDKDQLvlrtkEAFDTiqeqKVALEENGEKNQIQLGKLEATIKS-LSAELLKANEIIKK 389
Cdd:PRK05771  104 -ELEEEISELENEIKELEQEIERLEPW-----GNFDL----DLSLLLGFKYVSVFVGTVPEDKLEeLKLESDVENVEYIS 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 390 lqgdlktlmgKLKLKNTVTIQQEKLLAEK-EEMLQK---ERKESQDAG---QFLRAKEQEVCRLQEQLETTVQKLEESKQ 462
Cdd:PRK05771  174 ----------TDKGYVYVVVVVLKELSDEvEEELKKlgfERLELEEEGtpsELIREIKEELEEIEKERESLLEELKELAK 243

                         250       260
                  ....*....|....*....|...
gi 1907152297 463 llKNNEKLITWlnKELNENQLVR 485
Cdd:PRK05771  244 --KYLEELLAL--YEYLEIELER 262
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 211-482 2.01e-05

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: 48.04  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  211 SQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKaklagVEEELQ 290
Cdd:pfam02463  165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK-----LNEERI 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  291 RAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE-QEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKL 369
Cdd:pfam02463  240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  370 EATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ----QEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCR 445
Cdd:pfam02463  320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEleklQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1907152297  446 LQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:pfam02463  400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
PTZ00121 PTZ00121
MAEBL; Provisional
 186-484 2.63e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 2.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  186 SEKMQELDKlRSEWASHTASLTNKHSQELTAE--KEKA--LQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAAN 261
Cdd:PTZ00121  1456 AKKAEEAKK-KAEEAKKADEAKKKAEEAKKADeaKKKAeeAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  262 KELTERKYKGDSTVREL-KAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR 340
Cdd:PTZ00121  1535 KADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  341 TKEAfdTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEE 420
Cdd:PTZ00121  1615 AEEA--KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152297  421 MLQKERKESQDAGQfLRAKEQEVCRLQEQL----ETTVQKLEESKQLLKNNEKLITWLNKELNENQLV 484
Cdd:PTZ00121  1693 ALKKEAEEAKKAEE-LKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
215-487 3.78e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 215 TAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRE----LKAKLAGVEEELQ 290
Cdd:PRK03918  471 IEEKERKLRKELRELEKVLKKESELIKLKEL-AEQLKELEEKLKKYNLEELEKKAEEYEKLKEklikLKGEIKSLKKELE 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 291 RAKQevlsLRRENCTLDTECHEKEKHINQLQTKVAVLEQE-IKDKDQLVLRTKEAFDTIQEQKVALEEngeknqiqLGKL 369
Cdd:PRK03918  550 KLEE----LKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLELKDAEKE--------LERE 617

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 370 EATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtVTIQQEKLLAEKEEMLQKERKESQdagqfLRAKEQEVCRLQEQ 449
Cdd:PRK03918  618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELE-KKYSEEEYEELREEYLELSRELAG-----LRAELEELEKRREE 691

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1907152297 450 LETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 487
Cdd:PRK03918  692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 183-482 4.27e-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: 4.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  183 ETL-SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQK------KELETLHQRNIHQLQSRLS 255
Cdd:pfam15921  248 EALkSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqeqaRNQNSMYMRQLSDLESTVS 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  256 ELEAankELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDtechekekhiNQLQTKVAVLEQeikdkd 335
Cdd:pfam15921  328 QLRS---ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD----------DQLQKLLADLHK------ 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  336 qlvlRTKEaFDTIQEQKVALEENGEKNQIqlgkleaTIKSLSAELLKANEIIKKLQGDLKTlmgklkLKNTVTIQQEKLL 415
Cdd:pfam15921  389 ----REKE-LSLEKEQNKRLWDRDTGNSI-------TIDHLRRELDDRNMEVQRLEALLKA------MKSECQGQMERQM 450

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907152297  416 AEKEEMLQKERKESQDAGQFLRAKeqevcrlqEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:pfam15921  451 AAIQGKNESLEKVSSLTAQLESTK--------EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE 509
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 162-469 6.83e-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: 45.94  E-value: 6.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  162 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLR----SEWASHTASLTN---KHSQELTAEKEKaLQTQVQCQQQHEQ 234
Cdd:pfam01576  299 EELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleEETRSHEAQLQEmrqKHTQALEELTEQ-LEQAKRNKANLEK 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  235 QKKELETLHQrnihQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE 314
Cdd:pfam01576  378 AKQALESENA----ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  315 KHINQLQTKVAVLEQEIKDKDQLV---LRTKEAFDT----IQEQKVALEENGEKNQIQLGKLEATIKSLSAELLkanEII 387
Cdd:pfam01576  454 GKNIKLSKDVSSLESQLQDTQELLqeeTRQKLNLSTrlrqLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS---DMK 530

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  388 KKLQGDLKTLMGKLKLKntvtiqqEKLLAEKEEMLQKERKESQDAGQFLRAKEqevcRLQEQLETTVQKLEESKQLLKNN 467
Cdd:pfam01576  531 KKLEEDAGTLEALEEGK-------KRLQRELEALTQQLEEKAAAYDKLEKTKN----RLQQELDDLLVDLDHQRQLVSNL 599


                   ..
gi 1907152297  468 EK 469
Cdd:pfam01576  600 EK 601
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 182-433 7.85e-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: 45.14  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 182 QETLSEKMQELDKLRSEwashtASLTNKHSQELTAEKEKALqtqvqcqqqheqqkKELETLhQRNIHQLQSRLSELEAAN 261
Cdd:COG4942    19 ADAAAEAEAELEQLQQE-----IAELEKELAALKKEEKALL--------------KQLAAL-ERRIAALARRIRALEQEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 262 KELTERkykgdstVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE----KHINQLQTKVAVLEQEIKDKDQL 337
Cdd:COG4942    79 AALEAE-------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 338 VLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAE 417
Cdd:COG4942   152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231

                         250
                  ....*....|....*.
gi 1907152297 418 KEEMLQKERKESQDAG 433
Cdd:COG4942   232 LEAEAAAAAERTPAAG 247
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 204-462 8.13e-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: 45.14  E-value: 8.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 204 ASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELetlhQRNIHQLQSRLSELEAANKELTERkykgdstVRELKAKLA 283
Cdd:COG4942    11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARR-------IRALEQELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 284 GVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTkvavleQEIKDKDQLVLRTKEAFDTIQEQKV------ALEE 357
Cdd:COG4942    80 ALEAELAELEKEIAELRAE---LEAQKEELAELLRALYR------LGRQPPLALLLSPEDFLDAVRRLQYlkylapARRE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 358 NGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtiqqEKLLAEKEEMLQKERKESQDAGQFLR 437
Cdd:COG4942   151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAAL--------------EALKAERQKLLARLEKELAELAAELA 216

                         250       260
                  ....*....|....*....|....*
gi 1907152297 438 AKEQEVCRLQEQLETTVQKLEESKQ 462
Cdd:COG4942   217 ELQQEAEELEALIARLEAEAAAAAE 241
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
236-426 8.80e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 8.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 236 KKELETLHQRNIHQLQSRLSELEAANKELTERKykgdSTVRELKAKLAGVEEELQRAKQEVLSLRRE---------NCTL 306
Cdd:COG4717    55 ADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREEleklekllqLLPL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 307 DTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI----QLGKLEATIKSLSAELLK 382
Cdd:COG4717   131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAE 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907152297 383 ANEIIKKLQGDLKTLMGKLKlkntvTIQQEKLLAEKEEMLQKER 426
Cdd:COG4717   211 LEEELEEAQEELEELEEELE-----QLENELEAAALEERLKEAR 249
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 148-478 9.38e-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: 45.40  E-value: 9.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 148 EIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKAlqtqvq 227
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ------ 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 228 cqqqheqQKKEletlhqrNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLD 307
Cdd:TIGR04523 381 -------SYKQ-------EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 308 TECHEKEKHINQLQTKVAVLEQEIKD---------------KDQLVLRTKEaFDTIQEQKVALEENGEKNQIQLGKLEAT 372
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVlsrsinkikqnleqkQKELKSKEKE-LKKLNEEKKELEEKVKDLTKKISSLKEK 525

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 373 IKSLSAELLKANEIIKKLQGDLKTL---MGKLKLKNTVTIQQEKLL-------------AEKEEMLQKERKESQDAGQFL 436
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDdfeLKKENLEKEIDEKNKEIEelkqtqkslkkkqEEKQELIDQKEKEKKDLIKEI 605

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1907152297 437 RAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKEL 478
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 157-458 9.52e-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: 45.49  E-value: 9.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  157 LKCSKEEKLSLTRSLDDVTRQLHITQETLSE-------KMQELDKLRSEwashtasltNKHSQELTAEKEKALQTQVQCQ 229
Cdd:pfam15921  491 LESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlKLQELQHLKNE---------GDHLRNVQTECEALKLQMAEKD 561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  230 QQHEQQKKELETL------HQRNIHQLQSRLSELEaanKELTER----------KYKGDSTVRELKAKLAGVEEE---LQ 290
Cdd:pfam15921  562 KVIEILRQQIENMtqlvgqHGRTAGAMQVEKAQLE---KEINDRrlelqefkilKDKKDAKIRELEARVSDLELEkvkLV 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  291 RAKQE----VLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDK--------DQLVLRTKEAFDTIQEQKVALEEN 358
Cdd:pfam15921  639 NAGSErlraVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKseemetttNKLKMQLKSAQSELEQTRNTLKSM 718

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  359 ------------GEKNQI-----QLGKLEATIKSLSAELLKAN-------EIIKKLQGDLKTLM---GKLKLKNTVTIQQ 411
Cdd:pfam15921  719 egsdghamkvamGMQKQItakrgQIDALQSKIQFLEEAMTNANkekhflkEEKNKLSQELSTVAtekNKMAGELEVLRSQ 798

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907152297  412 EKLLAEK----EEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLE 458
Cdd:pfam15921  799 ERRLKEKvanmEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 161-356 1.08e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 161 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKAlqtqvQCQQQHEQQKKELE 240
Cdd:COG1196   336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-----ELAAQLEELEEAEE 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 241 TLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQL 320
Cdd:COG1196   411 ALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907152297 321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALE 356
Cdd:COG1196   490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
166-366 1.56e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.62  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 166 SLTRSLDDVTRQLHITQETLSEKMQELDKLRSE----WASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELET 241
Cdd:COG3206   172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 242 LHQ--------RNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVL-SLRRENCTLDTECHE 312
Cdd:COG3206   252 GPDalpellqsPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREAS 331

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152297 313 KEKHINQLQTKVAVL---EQEIKDKDQLVLRTKEAFDTIQE--QKVALEENGEKNQIQL 366
Cdd:COG3206   332 LQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 238-333 1.96e-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: 42.65  E-value: 1.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 238 ELETlHQRNIHQLQSRLSEL----EAANKELTERKyKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEK 313
Cdd:pfam05266  79 ELEK-HGFDVKAPQSRINKLlslkDRQTKLLEELK-KLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAA 156

                          90       100
                  ....*....|....*....|
gi 1907152297 314 EKHINQLQTKVAVLEQEIKD 333
Cdd:pfam05266 157 DKEIARLKSEAEKLEQEIQD 176
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 168-366 3.23e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.90  E-value: 3.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  168 TRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLtNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLhQRNI 247
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-EKEIENLNGKKEELEEELEELEAALRDLESRLGDL-KKER 891

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  248 HQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELqrakQEVLSLRREnctlDTECHEKEKHINQLQTKVAVL 327
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL----SEIEDPKGE----DEEIPEEELSLEDVQAELQRV 963

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1907152297  328 EQEIKDKDQLVLR-------TKEAFDTIQEQKVALEEngEKNQIQL 366
Cdd:TIGR02169  964 EEEIRALEPVNMLaiqeyeeVLKRLDELKEKRAKLEE--ERKAILE 1007
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
251-459 3.90e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 3.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  251 QSRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQRAKQevlslRRENCTLDTECHEKEKHINQLQTKVAVLEQE 330
Cdd:COG4913    609 RAKLAALEAELAELEEE-------LAEAEERLEALEAELDALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAE 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  331 IKDkdqlVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntVTIQ 410
Cdd:COG4913    677 LER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---------EDLA 743

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907152297  411 QEKLLAEKEEMLQKERKEsQDAGQFLRAKEQEVCRLQEQLETTVQKLEE 459
Cdd:COG4913    744 RLELRALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELER 791
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
272-492 4.70e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 272 DSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 351
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 352 KVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-LKNTVTIQQEKLLAEKEEMLQKERKESQ 430
Cdd:COG4372   110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEsLQEELAALEQELQALSEAEAEQALDELL 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907152297 431 DAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQDTLGT 492
Cdd:COG4372   190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
160-451 4.99e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 160 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASL--TNKHSQELTAEKEKALQTQVQCQQQHEQQKK 237
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELeqLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 238 ELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE--K 315
Cdd:COG4372   109 EAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 316 HINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 395
Cdd:COG4372   188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907152297 396 TLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLE 451
Cdd:COG4372   268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 183-488 7.75e-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: 7.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  183 ETLSEKMQELDKLRSEWASHTASLTNKHS-QELTAEKEKALQTQVQCQQQHEQQKKELETlHQRNIHQLQSRLSELEAAN 261
Cdd:TIGR00606  795 ERFQMELKDVERKIAQQAAKLQGSDLDRTvQQVNQEKQEKQHELDTVVSKIELNRKLIQD-QQEQIQHLKSKTNELKSEK 873

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  262 KELTERKYKGDSTVRELKAKLAGVEE---ELQRAKQEVLSLRRencTLDTECHEKEKHINQLQTKVAVLEQEIKDK---- 334
Cdd:TIGR00606  874 LQIGTNLQRRQQFEEQLVELSTEVQSlirEIKDAKEQDSPLET---FLEKDQQEKEELISSKETSNKKAQDKVNDIkekv 950

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  335 DQLVLRTKEAFDTIQEQKvaleengeknQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtvtiQQEKL 414
Cdd:TIGR00606  951 KNIHGYMKDIENKIQDGK----------DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK----IQERW 1016

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907152297  415 LAEkEEMLQKERKESQDAGQFLRAKEQEVCRLQ-EQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 488
Cdd:TIGR00606 1017 LQD-NLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKE 1090
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
254-477 8.14e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 254 LSELEAANKELteRKYKGDSTVRELKaKLAGVEEELQRAKQEVLSLRRenctLDTECHEKEKHINQLQTKVAVLEQEIKD 333
Cdd:COG4717    48 LERLEKEADEL--FKPQGRKPELNLK-ELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 334 KDQLvlrtKEAFDTIQEQKvALEENGEKNQIQLGKLEA---TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 410
Cdd:COG4717   121 LEKL----LQLLPLYQELE-ALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907152297 411 QeklLAEKEEMLQKERKEsqdagqflrakeqevcrLQEQLETTVQKLEESKQLLKNNEKLITWLNKE 477
Cdd:COG4717   196 D---LAEELEELQQRLAE-----------------LEEELEEAQEELEELEEELEQLENELEAAALE 242
PRK12704 PRK12704
phosphodiesterase; Provisional
 348-480 8.73e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 348 IQEQKVALEENGEKNQIQLGKLEAtiKSLSAE-LLKANEIIKKLQGDLKTlmgKLKLKNTVTIQQEKLLAEKEEMLqKER 426
Cdd:PRK12704   28 IAEAKIKEAEEEAKRILEEAKKEA--EAIKKEaLLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENL-DRK 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907152297 427 KESqdagqfLRAKEQEvcrLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:PRK12704  102 LEL------LEKREEE---LEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 243-482 8.90e-04

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: 42.42  E-value: 8.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 243 HQRNI--HQLQSRLSELEAAN-KELTERKYKGDSTVRELKAKLAGVEEELQR-----AKQEVLSLRRENCTLDTECHEKE 314
Cdd:pfam17380 280 HQKAVseRQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERK 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 315 KHINQL-QTKVAVLEQEIKDKDQLVL-------RTKEAFDTIQEQKVALEENGEKNQIQLGKLEatikSLSAELLKANEI 386
Cdd:pfam17380 360 RELERIrQEEIAMEISRMRELERLQMerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEARQR 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 387 -IKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQdagqflraKEQEVCRLQEQLETTV--QKLEESKQL 463
Cdd:pfam17380 436 eVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--------KEKRDRKRAEEQRRKIleKELEERKQA 507

                         250
                  ....*....|....*....
gi 1907152297 464 LKNNEKLITWLNKELNENQ 482
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQ 526
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 148-482 1.14e-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: 42.26  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  148 EIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQEL-DKLRSEWASHTASLTNKHSQELTAEKEKALQTQV 226
Cdd:TIGR00618  187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  227 QCQQQHEQQKKELETLHQR-NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCT 305
Cdd:TIGR00618  267 ARIEELRAQEAVLEETQERiNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  306 LDTeCHEKEKHINQlQTKVAVLEQEIKDKdQLVLRtkEAFDTIQEQKVALEENgeknqiqlgkleatIKSLSAELlkanE 385
Cdd:TIGR00618  347 LQT-LHSQEIHIRD-AHEVATSIREISCQ-QHTLT--QHIHTLQQQKTTLTQK--------------LQSLCKEL----D 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  386 IIKKLQGDLKTLMGKLKlkntvTIQQEKLLAEKEEMLQKERKE-----SQDAGQFLRAKEQEVCRLQEQLETTVQKLEES 460
Cdd:TIGR00618  404 ILQREQATIDTRTSAFR-----DLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478

                          330       340
                   ....*....|....*....|..
gi 1907152297  461 KQLLKNNEKLITWLNKELNENQ 482
Cdd:TIGR00618  479 EQIHLQETRKKAVVLARLLELQ 500
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 162-472 2.08e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 162 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELE- 240
Cdd:pfam05557  48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEl 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 241 --------------TLHQRNIHQLQSRLSELEAANKELTERKYKgdstVRELKAKLAGVE---EELQRAKQEVLSLRREN 303
Cdd:pfam05557 128 qstnseleelqerlDLLKAKASEAEQLRQNLEKQQSSLAEAEQR----IKELEFEIQSQEqdsEIVKNSKSELARIPELE 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 304 CTLDtECHEKEKHINQLQTKVAVLEQEIKDkdqlvLRTK-EAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLK 382
Cdd:pfam05557 204 KELE-RLREHNKHLNENIENKLLLKEEVED-----LKRKlEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 383 ----ANEIIKKLQGDLkTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLE 458
Cdd:pfam05557 278 pedlSRRIEQLQQREI-VLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERD 356

                         330
                  ....*....|....
gi 1907152297 459 ESKQLLKNNEKLIT 472
Cdd:pfam05557 357 GYRAILESYDKELT 370
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 182-464 2.10e-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: 41.35  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 182 QETLSEKMQELDKLRSEWASHTASLTNKHS-----QELTAEKEKALqtqvqcqqqheqqkkelETLHQRNIHQLQSRLSE 256
Cdd:pfam10174 407 QEQLRDKDKQLAGLKERVKSLQTDSSNTDTalttlEEALSEKERII-----------------ERLKEQREREDRERLEE 469

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 257 LEAANKELterkykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLqtkvavlEQEIKDKDQ 336
Cdd:pfam10174 470 LESLKKEN-----------KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-------EIAVEQKKE 531

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 337 LVLRTKEAFDTIQEQKVALEENGEKNQiqlgkleaTIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLA 416
Cdd:pfam10174 532 ECSKLENQLKKAHNAEEAVRTNPEIND--------RIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA 603

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152297 417 EKEEMLQKERKESQDAGQFLRAKEQEV--------------------CRLQEQLETTVQKLEESKQLL 464
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEMkkkgaqlleearrrednladNSQQLQLEELMGALEKTRQEL 671
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 236-487 2.23e-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: 41.16  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 236 KKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLR----------RENCT 305
Cdd:TIGR04523 136 NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllsnlkkkiQKNKS 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 306 LDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAEL----- 380
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlks 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 381 -------LKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETT 453
Cdd:TIGR04523 296 eisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1907152297 454 VQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 487
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 157-481 2.50e-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: 40.77  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 157 LKCSKEEKLS--LTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEkalqtQVQCQQQHEQ 234
Cdd:TIGR04523 300 LNNQKEQDWNkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE-----LEEKQNEIEK 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 235 QKKELETLHQrNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRREnctldtecheke 314
Cdd:TIGR04523 375 LKKENQSYKQ-EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE------------ 441

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 315 khINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDL 394
Cdd:TIGR04523 442 --IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 395 KTLMGKLKLKNTVTIQQEKLLAEKEEMLQK--ERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLIT 472
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599


                  ....*....
gi 1907152297 473 WLNKELNEN 481
Cdd:TIGR04523 600 DLIKEIEEK 608
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 176-422 2.50e-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: 40.98  E-value: 2.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  176 RQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL--HQRNIHQLQSR 253
Cdd:pfam12128  276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaaDQEQLPSWQSE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  254 LSELEAANKELT------ERKYKG--DSTVRELKAKLAGVEEELQRAKQE-VLSLRRENCTLDTECHEKEKHINQLQTKV 324
Cdd:pfam12128  356 LENLEERLKALTgkhqdvTAKYNRrrSKIKEQNNRDIAGIKDKLAKIREArDRQLAVAEDDLQALESELREQLEAGKLEF 435

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  325 AVLEQEIKDK-DQLVLRTKEAfdTIQEQkvaLEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 403
Cdd:pfam12128  436 NEEEYRLKSRlGELKLRLNQA--TATPE---LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510

                          250
                   ....*....|....*....
gi 1907152297  404 KNTVTIQQEKLLAEKEEML 422
Cdd:pfam12128  511 ASRRLEERQSALDELELQL 529
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
266-480 2.54e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 266 ERKYKGDSTV-RELKAKLAGVEEELQRaKQEVLSLRRENctlDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR---T 341
Cdd:PRK03918  161 ENAYKNLGEViKEIKRRIERLEKFIKR-TENIEELIKEK---EKELEEVLREINEISSELPELREELEKLEKEVKEleeL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 342 KEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKklqgDLKTLMGKLKlkntvtiQQEKLLAEKEEM 421
Cdd:PRK03918  237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK----ELKELKEKAE-------EYIKLSEFYEEY 305

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907152297 422 LQKERKESQDAGQFlrakEQEVCRLQEQLEttvqKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:PRK03918  306 LDELREIEKRLSRL----EEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEE 356
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 246-490 2.72e-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: 40.77  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 246 NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTkva 325
Cdd:TIGR04523  69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLT--- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 326 vleqEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKAN---EIIKKLQGDLKTLMGKL- 401
Cdd:TIGR04523 146 ----EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQIs 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 402 KLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVcRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNEN 481
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN-KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL 300


                  ....*....
gi 1907152297 482 QLVRKQDTL 490
Cdd:TIGR04523 301 NNQKEQDWN 309
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
237-402 2.83e-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: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  237 KELETLHQRnIHQLQSRLSELEAANKELteRKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKH 316
Cdd:COG4913    255 EPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  317 INQ--------LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQ----LGKLEATIKSLSAELLKAN 384
Cdd:COG4913    332 IRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAE 411

                          170
                   ....*....|....*...
gi 1907152297  385 EIIKKLQGDLKTLMGKLK 402
Cdd:COG4913    412 AALRDLRRELRELEAEIA 429
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 283-469 3.01e-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: 3.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  283 AGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKN 362
Cdd:pfam02463  162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  363 QIQLGKLE-ATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQ 441
Cdd:pfam02463  242 LQELLRDEqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321

                          170       180
                   ....*....|....*....|....*...
gi 1907152297  442 EVCRLQEQLETTVQKLEESKQLLKNNEK 469
Cdd:pfam02463  322 EKKKAEKELKKEKEEIEELEKELKELEI 349
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
169-476 3.28e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 169 RSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLT--NKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQrN 246
Cdd:PRK02224  272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE-D 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 247 IHQLQSRL-----------SELEAANKELTERKYKG---DSTVRELKAKLAGVEEELQRAkQEVLSLRRENctlDTECHE 312
Cdd:PRK02224  351 ADDLEERAeelreeaaeleSELEEAREAVEDRREEIeelEEEIEELRERFGDAPVDLGNA-EDFLEELREE---RDELRE 426

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 313 KEKhinQLQTKVAVLEQEIKDKDQLVLRTK-----------EAFDTIQEQKVALEENGEknqiQLGKLEATIKSLSAELL 381
Cdd:PRK02224  427 REA---ELEATLRTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEA----ELEDLEEEVEEVEERLE 499

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 382 KANEIiKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESK 461
Cdd:PRK02224  500 RAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578

                         330
                  ....*....|....*
gi 1907152297 462 QLLKNNEKLITWLNK 476
Cdd:PRK02224  579 SKLAELKERIESLER 593
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
219-361 3.39e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 40.61  E-value: 3.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 219 EKALQTQVQCQQQHEQQKKELETLH-QRNIHQLQSRLSELEAANKELteRKYkgdstVRELKAKLAGVEEELQRAKQEVL 297
Cdd:COG2433   379 EEALEELIEKELPEEEPEAEREKEHeERELTEEEEEIRRLEEQVERL--EAE-----VEELEAELEEKDERIERLERELS 451

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907152297 298 SLRREnctLDTEcHEKEKHINQLQTKVAVLEQEIKDKDQlvlRTKEAFDTIQEQK--VALEENGEK 361
Cdd:COG2433   452 EARSE---ERRE-IRKDREISRLDREIERLERELEEERE---RIEELKRKLERLKelWKLEHSGEL 510
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
317-489 3.50e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  317 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKN---------QIQLGKLEATIKSL---SAELLKAN 384
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLdasSDDLAALE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  385 EIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEvcRLQEQLETTVQKlEESKQLL 464
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD-AVERELR 768

                          170       180
                   ....*....|....*....|....*..
gi 1907152297  465 KNNEKLITWLNKELN--ENQLVRKQDT 489
Cdd:COG4913    769 ENLEERIDALRARLNraEEELERAMRA 795
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
183-475 4.58e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 183 ETLSEKMQELDKLRSEWAS---HTASLTNKHsqeltaEKEKALQTQVQCQQQHEQQKKELETLhqrnIHQLQSRLSELEA 259
Cdd:PRK02224  468 ETIEEDRERVEELEAELEDleeEVEEVEERL------ERAEDLVEAEDRIERLEERREDLEEL----IAERRETIEEKRE 537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 260 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTEchekekhINQLQTKVAVLEqEIKDKDQLVL 339
Cdd:PRK02224  538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER-------IESLERIRTLLA-AIADAEDEIE 609

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 340 RTKEAFDTIQEQ----KVALEENGEKNQIQLGKL-EATIKSLSAELLKANEIIKKLQGDLKTLMGKL-KLKNTVTIQQEK 413
Cdd:PRK02224  610 RLREKREALAELnderRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEIGAVENE 689

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907152297 414 LlaEKEEMLQKERKESQDAGQFLRAKEQEVcrlqEQLETTVQKLE-ESKQllKNNEKLITWLN 475
Cdd:PRK02224  690 L--EELEELRERREALENRVEALEALYDEA----EELESMYGDLRaELRQ--RNVETLERMLN 744
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 189-399 4.99e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 39.84  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 189 MQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQheqqKKELETLHQRNIHQLQSRLSELEAANKELTERK 268
Cdd:PLN03229  534 KYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEI----KEKMEALKAEVASSGASSGDELDDDLKEKVEKM 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 269 YKgdstvrELKAKLAGVeeeLQRAKQEVLSLRRENCTLDTECHEKEkhinqLQTKVAVLEQEIKDKDQLVLRTKEAFDTI 348
Cdd:PLN03229  610 KK------EIELELAGV---LKSMGLEVIGVTKKNKDTAEQTPPPN-----LQEKIESLNEEINKKIERVIRSSDLKSKI 675

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 349 QEQKVALEENG------EKNQIQlgKLEATIKSLSAELLKANEIIKK---LQGDLKTLMG 399
Cdd:PLN03229  676 ELLKLEVAKASktpdvtEKEKIE--ALEQQIKQKIAEALNSSELKEKfeeLEAELAAARE 733
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
249-470 5.06e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 249 QLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDT---ECHEKEKHINQL----Q 321
Cdd:COG1340    47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLewrqQ 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 322 TKVAVLEQEIkdkdQLVLRTKEAFDTIQEQKVALEENGEKNQI---------QLGKLEATIKSLSAELLKANEIIKKLQG 392
Cdd:COG1340   127 TEVLSPEEEK----ELVEKIKELEKELEKAKKALEKNEKLKELraelkelrkEAEEIHKKIKELAEEAQELHEEMIELYK 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 393 DLKTLMGKL-KLKNTVTIQQEKLLAEKEEM--LQKERKESQDAGQFLRAKEQEVcRLQEQLETTVQKLEESKQLLKNNEK 469
Cdd:COG1340   203 EADELRKEAdELHKEIVEAQEKADELHEEIieLQKELRELRKELKKLRKKQRAL-KREKEKEELEEKAEEIFEKLKKGEK 281


                  .
gi 1907152297 470 L 470
Cdd:COG1340   282 L 282
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 157-479 5.19e-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: 40.09  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 157 LKCSKEEKLSLTRSLDDVTRQLH---ITQETLSEKMQeldklrsewashtasLTNKHSQELTAEKEKALQTQVQCQQQHE 233
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQrsmSTQKALEEDLQ---------------IATKTICQLTEEKEAQMEELNKAKAAHS 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 234 QQKKELETLH--------------QRNIHQLQSRLSELEAANKELTE-RKYKGDSTVR--ELKAKLAGVEEELQRAKQ-- 294
Cdd:pfam05483 349 FVVTEFEATTcsleellrteqqrlEKNEDQLKIITMELQKKSSELEEmTKFKNNKEVEleELKKILAEDEKLLDEKKQfe 428

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 295 ---EVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKeaFDTIQEQKVALEENGEKNQIQLGKLEA 371
Cdd:pfam05483 429 kiaEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE--LEKEKLKNIELTAHCDKLLLENKELTQ 506

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 372 TIKSLSAELLKANEII-------KKLQGDLKTLMGK-LKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQF-------- 435
Cdd:pfam05483 507 EASDMTLELKKHQEDIinckkqeERMLKQIENLEEKeMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIeyevlkke 586

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1907152297 436 --LRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELN 479
Cdd:pfam05483 587 kqMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 160-469 5.25e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.10  E-value: 5.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  160 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTnkhsqeltaEKEKALQTQVQCQQQHEQ----Q 235
Cdd:pfam15921  459 SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ---------EKERAIEATNAEITKLRSrvdlK 529

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  236 KKELETLHQRNIHqLQSRLSELEAANKELTERkykgDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHE--- 312
Cdd:pfam15921  530 LQELQHLKNEGDH-LRNVQTECEALKLQMAEK----DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDrrl 604

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  313 -----------KEKHINQLQTKVAVLEQE--------------IKD----KDQL---VLRTKEAFDTIQEQKVALEEN-- 358
Cdd:pfam15921  605 elqefkilkdkKDAKIRELEARVSDLELEkvklvnagserlraVKDikqeRDQLlneVKTSRNELNSLSEDYEVLKRNfr 684

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  359 --GEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGD----LKTLMGKLKlKNTVTIQQEKLLAEKEEMLQKERKESQDA 432
Cdd:pfam15921  685 nkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdghaMKVAMGMQK-QITAKRGQIDALQSKIQFLEEAMTNANKE 763

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1907152297  433 GQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEK 469
Cdd:pfam15921  764 KHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 161-471 5.60e-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: 39.95  E-value: 5.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  161 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKE-- 238
Cdd:pfam02463  222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKse 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  239 ---LETLHQRNIHQLQSRLSELEAANKELTERKykgdstvrELKAKLAGVEEELQRAKQEVLslrrenctldtechEKEK 315
Cdd:pfam02463  302 llkLERRKVDDEEKLKESEKEKKKAEKELKKEK--------EEIEELEKELKELEIKREAEE--------------EEEE 359

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  316 HINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLK-ANEIIKKLQGDL 394
Cdd:pfam02463  360 ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKeELEILEEEEESI 439

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907152297  395 KTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLI 471
Cdd:pfam02463  440 ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALI 516
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 147-480 6.14e-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: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  147 VEIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSE-------KMQELDKLRSEWASHTASLTNK-----HSQEL 214
Cdd:TIGR00606  496 TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQmemltkdKMDKDEQIRKIKSRHSDELTSLlgyfpNKKQL 575

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  215 TAEKEKALQTQVQCQQQHEQQKKELETLHQrNIHQLQSRLSELEAANKELTERKYKGDSTvRELKAKLAGVEEELQRAKQ 294
Cdd:TIGR00606  576 EDWLHSKSKEINQTRDRLAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSK 653

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  295 E--------------VLSLRREN---CTLDTECHEKEKHINQ----LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKV 353
Cdd:TIGR00606  654 QramlagatavysqfITQLTDENqscCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP 733

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  354 ALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKN------TVTIQQEKLLAEKEEMLQKERK 427
Cdd:TIGR00606  734 GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAA 813

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907152297  428 ESQDAGQFLRAKE--QEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:TIGR00606  814 KLQGSDLDRTVQQvnQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 190-331 6.21e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.75  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 190 QELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQK-----------KELETLhQRNIHQLQSRLSELE 258
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvrnnKEYEAL-QKEIESLKRRISDLE 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907152297 259 AANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEvlslrrenctLDTECHEKEKHINQLQTKVAVLEQEI 331
Cdd:COG1579   110 DEILELMERIEELEEELAELEAELAELEAELEEKKAE----------LDEELAELEAELEELEAEREELAAKI 172
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 170-385 6.97e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 6.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 170 SLDDVTRQLHITQETLSEKMQELDKLRSEWashtasltnkhsQELTAEKEKAlqtqvqcqqqheqqKKELETLhQRNIHQ 249
Cdd:COG3883    24 ELSELQAELEAAQAELDALQAELEELNEEY------------NELQAELEAL--------------QAEIDKL-QAEIAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 250 LQSRLSELEAANKELTERKYKGDSTVRELKA------------KLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHI 317
Cdd:COG3883    77 AEAEIEERREELGERARALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907152297 318 NQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANE 385
Cdd:COG3883   157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 237-470 7.72e-03

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: 39.39  E-value: 7.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  237 KELETLhQRNIHQLQSRLSELEAANKELTerkykgdSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKH 316
Cdd:pfam01576  798 KQLKKL-QAQMKDLQRELEEARASRDEIL-------AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADE 869

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  317 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATI---KSLSAELLKANEIIKKLQGD 393
Cdd:pfam01576  870 IASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaeRSTSQKSESARQQLERQNKE 949

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297  394 LKTLMGKL------KLKNTVTIQQEKLlAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESK-QLLKN 466
Cdd:pfam01576  950 LKAKLQEMegtvksKFKSSIAALEAKI-AQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKdQAEKG 1028


                   ....
gi 1907152297  467 NEKL 470
Cdd:pfam01576 1029 NSRM 1032
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 286-407 7.85e-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: 38.89  E-value: 7.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907152297 286 EEELQRAKQEVLSLrrenctLDTEchekEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVAL--EENGEKNQ 363
Cdd:cd22656   109 DEELEEAKKTIKAL------LDDL----LKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLltDEGGAIAR 178

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1907152297 364 IQLGKLEATIKSLSAELL-KANEIIKKLQGDLKTLMGKLKLKNTV 407
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 8.01e-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: 34.18  E-value: 8.01e-03
                          10        20
                  ....*....|....*....|....*.
gi 1907152297 146 DVEIKKFLAGCLKCSKEEKLSLTRSL 171
Cdd:pfam18594   1 DSEVKKYLADCLKSLKEEKQLLEQKL 26
 
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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