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Conserved domains on  [gi|35038601|ref|NP_919268|]
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spindle assembly abnormal protein 6 homolog isoform 1 [Homo sapiens]

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 1.23e-61

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: 201.24  E-value: 1.23e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   4 VLFHQLVPLQVKCKDCEERRVSIRMSIELQSvSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKFQQGLLVDFLAF 83
Cdd:cd10142   1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35038601  84 PQKFIDLLQQCTQEHAKEIPRFLLQLVSPAailDNSPAFLNVVETNPFKHLTHLSLKLLPG 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 2.09e-16

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: 83.57  E-value: 2.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    165 LSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLEIL-- 242
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLea 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    243 ----HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVN 318
Cdd:TIGR02168  741 eveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    319 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 35038601    399 GKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 450
Cdd:TIGR02168  901 EELR-------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 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 2.79e-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: 35.72  E-value: 2.79e-03
                          10        20
                  ....*....|....*....|....*.
gi 35038601   146 DVEIKKFLAGCLKCSKEEKLSLMQSL 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 1.23e-61

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: 201.24  E-value: 1.23e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   4 VLFHQLVPLQVKCKDCEERRVSIRMSIELQSvSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKFQQGLLVDFLAF 83
Cdd:cd10142   1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35038601  84 PQKFIDLLQQCTQEHAKEIPRFLLQLVSPAailDNSPAFLNVVETNPFKHLTHLSLKLLPG 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 3.59e-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: 108.05  E-value: 3.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    44 LVIRLTDDTDPFFLYNLVISEEDFQSLKFQQGLLVDFLAFPQKFIDLLQQCTQEHAKEIprfllqlvspAAILDNSPAFL 123
Cdd:pfam16531   1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKEPNLLV----------FLIQDDGTATL 70

                          90
                  ....*....|....*...
gi 35038601   124 NVVETNPFKHLTHLSLKL 141
Cdd:pfam16531  71 VFIENNEFKNLEHLSLDF 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-450 2.09e-16

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: 83.57  E-value: 2.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    165 LSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLEIL-- 242
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLea 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    243 ----HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVN 318
Cdd:TIGR02168  741 eveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    319 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 35038601    399 GKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 450
Cdd:TIGR02168  901 EELR-------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 182-482 5.06e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.83  E-value: 5.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 182 RKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILhQQNIHQLQNRLSELEAAN 261
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAEL 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 262 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRT 341
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 342 KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 421
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 35038601 422 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNE-KLITWLNKELNENQ 482
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
249-472 2.96e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.00  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  249 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQR---TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVA 325
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  326 VLEQEIKDKDQLVLRTKE------AFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMG 399
Cdd:PRK03918 270 ELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKK 345

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35038601  400 KLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLIT 472
Cdd:PRK03918 346 KLK-------ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 250-470 1.75e-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: 54.13  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   250 LQNRLSELEAANKDLterkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLdvechekEKHVNQLQTKVAVLEQ 329
Cdd:pfam07888  32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYKRDREQWERQRREL-------ESRVAELKEELRQSRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   330 EIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 409
Cdd:pfam07888  95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35038601   410 QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 470
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
Sas6_CC pfam18594
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of ...
 146-171 2.79e-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: 35.72  E-value: 2.79e-03
                          10        20
                  ....*....|....*....|....*.
gi 35038601   146 DVEIKKFLAGCLKCSKEEKLSLMQSL 171
Cdd:pfam18594   1 DSEVKKYLADCLKSLKEEKQLLEQKL 26
TOP4c cd00187
DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), ...
 360-480 3.55e-03

DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), bacterial DNA gyrases (A subunit, GyrA),mammalian DNA toposiomerases II. DNA topoisomerases are essential enzymes that regulate the conformational changes in DNA topology by catalysing the concerted breakage and rejoining of DNA strands during normal cellular growth.


Pssm-ID: 238111 [Multi-domain]  Cd Length: 445  Bit Score: 40.24  E-value: 3.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 360 EKNQVQLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKElqdvgqslrik 439
Cdd:cd00187 341 GKAEARLHILEGLLKAILN-IDEVINLIRSSDEAKKALIEELEKLGFSEIQADAILDMRLRRLTKLERE----------- 408

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 35038601 440 eqevcKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:cd00187 409 -----KLLKELKELEAEIEDLEKILASEERPKDLWKEELDE 444
 
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 1.23e-61

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: 201.24  E-value: 1.23e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   4 VLFHQLVPLQVKCKDCEERRVSIRMSIELQSvSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKFQQGLLVDFLAF 83
Cdd:cd10142   1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35038601  84 PQKFIDLLQQCTQEHAKEIPRFLLQLVSPAailDNSPAFLNVVETNPFKHLTHLSLKLLPG 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 3.59e-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: 108.05  E-value: 3.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    44 LVIRLTDDTDPFFLYNLVISEEDFQSLKFQQGLLVDFLAFPQKFIDLLQQCTQEHAKEIprfllqlvspAAILDNSPAFL 123
Cdd:pfam16531   1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKEPNLLV----------FLIQDDGTATL 70

                          90
                  ....*....|....*...
gi 35038601   124 NVVETNPFKHLTHLSLKL 141
Cdd:pfam16531  71 VFIENNEFKNLEHLSLDF 88
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-450 2.09e-16

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: 83.57  E-value: 2.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    165 LSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLEIL-- 242
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLea 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    243 ----HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVN 318
Cdd:TIGR02168  741 eveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    319 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 35038601    399 GKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 450
Cdd:TIGR02168  901 EELR-------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 182-482 5.06e-15

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 78.83  E-value: 5.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 182 RKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILhQQNIHQLQNRLSELEAAN 261
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAEL 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 262 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRT 341
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 342 KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 421
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 35038601 422 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNE-KLITWLNKELNENQ 482
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-482 6.88e-13

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 72.01  E-value: 6.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    243 HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT 322
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    323 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEEN-------GEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK 395
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    396 TLMGKLK-LKNTVTI---QQEKLLAEKEEKLQK-EQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 470
Cdd:TIGR02168  397 SLNNEIErLEARLERledRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476

                          250
                   ....*....|..
gi 35038601    471 ITWLNKELNENQ 482
Cdd:TIGR02168  477 LDAAERELAQLQ 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 163-470 1.74e-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: 70.86  E-value: 1.74e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    163 EKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQEltNEKEKALQAQVQYQQQHEQQKKDLEil 242
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV--SELEEEIEELQKELYALANEISRLE-- 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    243 hqQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEC-------HEKEK 315
Cdd:TIGR02168  302 --QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrlEELEE 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    316 HVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLgkLEATIKSLSAELLKANEIIKKLQGDLK 395
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELE 457

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35038601    396 TLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQevckLQEQLEatvKKLEESKQLLKNNEKL 470
Cdd:TIGR02168  458 RLEEALE-------ELREELEEAEQALDAAERELAQLQARLDSLER----LQENLE---GFSEGVKALLKNQSGL 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 236-488 2.47e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 70.35  E-value: 2.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 236 KKDLEIL-HQQNIHQLQNRLSELEAANKDLTERKykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKE 314
Cdd:COG1196 219 KEELKELeAELLLLKLRELEAELEELEAELEELE----AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 315 KHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDL 394
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 395 KTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 474
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                       250
                ....*....|....
gi 35038601 475 NKELNENQLVRKQD 488
Cdd:COG1196 455 EEEEEALLELLAEL 468
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 163-471 6.99e-12

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 68.94  E-value: 6.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    163 EKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALT--NKHSQELTNEKEKALqaqvqyqqqheqqKKDLE 240
Cdd:TIGR02169  231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIKDLGEEEQLRV-------------KEKIG 297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    241 ILHQQnIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQL 320
Cdd:TIGR02169  298 ELEAE-IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK 400
Cdd:TIGR02169  377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35038601    401 LKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLrikeqevcklqEQLEATVKKLEESKQLLKNNEKLI 471
Cdd:TIGR02169  457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVL 516
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-480 3.53e-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: 66.63  E-value: 3.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    162 EEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKL---RNEWASHTAALTNKHSQELT---NEKEKALQAQVQYQQQHEQQ 235
Cdd:TIGR02169  170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLrreREKAERYQALLKEKREYEGYellKEKEALERQKEAIERQLASL 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    236 KKDLEILHQQnIHQLQNRLSELEAANKDLTER-KYKGDSTIRELKAKLSGVEEELQRT-------KQEVLSLRRENSTLD 307
Cdd:TIGR02169  250 EEELEKLTEE-ISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLersiaekERELEDAEERLAKLE 328

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    308 VECHEKEKHVNQLQTKvavLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLeatiKSLSAELLKANEII 387
Cdd:TIGR02169  329 AEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----KDYREKLEKLKREI 401

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    388 KKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNN 467
Cdd:TIGR02169  402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481

                          330
                   ....*....|...
gi 35038601    468 EKLITWLNKELNE 480
Cdd:TIGR02169  482 EKELSKLQRELAE 494
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 292-480 6.90e-11

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.85  E-value: 6.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    292 TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA 371
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    372 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 451
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834

                          170       180
                   ....*....|....*....|....*....
gi 35038601    452 ATVKKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEE 863
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 236-461 1.87e-10

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: 64.32  E-value: 1.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    236 KKDLEILHQ------QNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVE 309
Cdd:TIGR02169  687 KRELSSLQSelrrieNRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    310 CHEKEKHVNQLQTKVAVLEQEIKDkdqlvlrtkEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKK 389
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35038601    390 LQGDLKTLMGKlklKNTVTIQQEKL---LAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK 461
Cdd:TIGR02169  838 LQEQRIDLKEQ---IKSIEKEIENLngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 161-459 1.97e-10

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: 64.32  E-value: 1.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    161 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWaSHTAALTNKHSQELTNEKEKaLQAQVQYQQQHEQQKKDLE 240
Cdd:TIGR02169  687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEED-LSSLEQEIENVKSELKELE 764

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    241 ilhqQNIHQLQNRLSELEAANKDLtERKYkGDSTIRELKAKLSGVEEELQRTKQEVLSLrrenstldvechekEKHVNQL 320
Cdd:TIGR02169  765 ----ARIEELEEDLHKLEEALNDL-EARL-SHSRIPEIQAELSKLEEEVSRIEARLREI--------------EQKLNRL 824

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK 400
Cdd:TIGR02169  825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35038601    401 LKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ--EQLEATVKKLEE 459
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEE 965
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 272-511 1.23e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 60.61  E-value: 1.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 272 DSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDK-DQLVLRTKEAFdtiqe 350
Cdd:COG3883  22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERrEELGERARALY----- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 351 qkvvleengeKNQVQLGKLEATIKSLS-AELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKEL 429
Cdd:COG3883  97 ----------RSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELK-------ADKAELEAKKAELEAKLAEL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 430 QDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDVLGPSTTPPAHSSSNTIRSGI 509
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239


                ..
gi 35038601 510 SP 511
Cdd:COG3883 240 AA 241
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 273-478 5.60e-09

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: 58.62  E-value: 5.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 273 STIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQK 352
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 353 VVLEENGEK---NQVQLGKLEATIKSLSAE----LLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKE 425
Cdd:COG4942 100 EAQKEELAEllrALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 35038601 426 QKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 478
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
249-462 8.79e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 58.49  E-value: 8.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 249 QLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQE--VLSLRRENSTLdvechekEKHVNQLQTKVAV 326
Cdd:COG3206 165 NLELRREEARKALEFLEEQ-------LPELRKELEEAEAALEEFRQKngLVDLSEEAKLL-------LQQLSELESQLAE 230

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 327 LEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQV--QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-- 402
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqe 310

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 35038601 403 -------LKNTVTI--QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQ 462
Cdd:COG3206 311 aqrilasLEAELEAlqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 244-478 1.07e-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: 57.47  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 244 QQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 323
Cdd:COG4942  19 ADAAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 324 VAVLEQEIKD-KDQLVLRTKEAFDTIQEQKVVLEENGEkNQVQLGKLEATIKSLSAELlkaNEIIKKLQGDLKTLmgklk 402
Cdd:COG4942  92 IAELRAELEAqKEELAELLRALYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPAR---REQAEELRADLAEL----- 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35038601 403 lkNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 478
Cdd:COG4942 163 --AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
249-472 2.96e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.00  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  249 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQR---TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVA 325
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  326 VLEQEIKDKDQLVLRTKE------AFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMG 399
Cdd:PRK03918 270 ELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKK 345

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35038601  400 KLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLIT 472
Cdd:PRK03918 346 KLK-------ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 275-478 3.57e-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: 57.00  E-value: 3.57e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    275 IRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDK-------DQLVLRTKEAFDT 347
Cdd:TIGR02169  683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlsslEQEIENVKSELKE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    348 IQEQKVVLEENGEKNQVQLGKLEAT-----IKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiqqeKLLAEKEEkL 422
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLN----------RLTLEKEY-L 831

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 35038601    423 QKEQKELQDVGQSLRIKEQEVCKLQEQLEAtvkKLEESKQLLKNNEKLITWLNKEL 478
Cdd:TIGR02169  832 EKEIQELQEQRIDLKEQIKSIEKEIENLNG---KKEELEEELEELEAALRDLESRL 884
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 272-475 5.30e-08

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 54.16  E-value: 5.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 272 DSTIRELKAKLSGVEEELQRTKQEVLSLRREnstldveCHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 351
Cdd:COG1579  16 DSELDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 352 KVVleENGEKnqvQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtiqqEKLLAEKEEKLQKEQKELQD 431
Cdd:COG1579  89 KEY--EALQK---EIESLKRRISDLEDEILELMERIEELEEELAEL--------------EAELAELEAELEEKKAELDE 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 35038601 432 VGQSLRIKEQEvckLQEQLEATVKKLEEskQLLKNNEKLITWLN 475
Cdd:COG1579 150 ELAELEAELEE---LEAEREELAAKIPP--ELLALYERIRKRKN 188
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
157-480 5.76e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 56.23  E-value: 5.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  157 LKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTN--KHSQELTNEKEKaLQAQVQYQQQHEQ 234
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKleKEVKELEELKEE-IEELEKELESLEG 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  235 QKKDLEILHQQ---NIHQLQNRLSELEAANKDLTERKYKGDSTIR------ELKAKLSGVEEELQRTKQEVLSLRR---E 302
Cdd:PRK03918 253 SKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKAEEYIKlsefyeEYLDELREIEKRLSRLEEEINGIEErikE 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  303 NSTLDVECHEKEKHVNQLQTKVAVLE------QEIKDK-DQL-VLRTKEAFDTIQEQKVVLEE---NGEKNQVQLGKLEA 371
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKkEELeRLKKRLTGLTPEKLEKELEElekAKEEIEEEISKITA 412

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  372 TIKSL---SAELLKANEIIKKLQG------------DLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELqdvgQSL 436
Cdd:PRK03918 413 RIGELkkeIKELKKAIEELKKAKGkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL----EKV 488

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 35038601  437 RIKEQEVCKLQ---EQLEATVKKLEE-SKQLLKNNEKLITWLNKELNE 480
Cdd:PRK03918 489 LKKESELIKLKelaEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIK 536
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 157-480 6.03e-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: 55.80  E-value: 6.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   157 LKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEwashTAALTNKHSQELTNEKEKALQAQvqyqqqheqqk 236
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE----ISDLNNQKEQDWNKELKSELKNQ----------- 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   237 kdleilhQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENStldvechEKEKH 316
Cdd:TIGR04523 320 -------EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ-------SYKQE 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   317 VNQLQTKVAVLEQEIKDKDQlvlrtkeafdtiqeQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 396
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEK--------------LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   397 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQ---LEATVKKLEESKQLLKNNEKLitw 473
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEKIEK--- 528


                  ....*..
gi 35038601   474 LNKELNE 480
Cdd:TIGR04523 529 LESEKKE 535
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
187-488 6.61e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 6.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  187 EKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDleilhqqnIHQLQNRLSELEAA------ 260
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE--------IKELKKAIEELKKAkgkcpv 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  261 -NKDLTERKYKGdsTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT--KVAVLEQEIK--DKD 335
Cdd:PRK03918 441 cGRELTEEHRKE--LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKkyNLE 518

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  336 QLVLRTKEAfdtiqeqkvvleengEKNQVQLGKLEATIKSLSAELLKANEIIKKL----------QGDLKTLMGKLKLKN 405
Cdd:PRK03918 519 ELEKKAEEY---------------EKLKEKLIKLKGEIKSLKKELEKLEELKKKLaelekkldelEEELAELLKELEELG 583

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  406 TVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVR 485
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663


                 ...
gi 35038601  486 KQD 488
Cdd:PRK03918 664 LRE 666
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 161-490 1.02e-07

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: 55.41  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   161 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQEL----DKLRNEWASHTAALTNKHSQ--ELTNEKEKALQAQVQYQQQHEQ 234
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKKQNNQLkdniEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKKQLSEKQKELEQ 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   235 QKKDLEILHQQnIHQLQNRLSEL-----EAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVE 309
Cdd:TIGR04523 279 NNKKIKELEKQ-LNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   310 CHEKEKHVNQLQTKVAVLEQEIKDKDQ----LVLRTKEAFDTIQEQKVV---LEENGEKNQVQLGKLEATIKSLSAELLK 382
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQeiknLESQINDLESKIQNQEKLnqqKDEQIKKLQQEKELLEKEIERLKETIIK 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   383 ANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQE--------------VCKLQE 448
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKElkklneekkeleekVKDLTK 517

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 35038601   449 QLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDVL 490
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 160-478 1.14e-07

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: 55.03  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   160 SKEEKLSLMQS-LDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAqvqyqqqheqqkkd 238
Cdd:TIGR04523 318 NQEKKLEEIQNqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK-------------- 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   239 leilhqQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVN 318
Cdd:TIGR04523 384 ------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   319 QLQTKVAVLEQEIKD---------------KDQLVLRTKEaFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKA 383
Cdd:TIGR04523 458 NLDNTRESLETQLKVlsrsinkikqnleqkQKELKSKEKE-LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   384 NEIIKKLQGDLKTL---MGKLKLKNTVTIQQEKLL-------------AEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ 447
Cdd:TIGR04523 537 ESKISDLEDELNKDdfeLKKENLEKEIDEKNKEIEelkqtqkslkkkqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616

                         330       340       350
                  ....*....|....*....|....*....|.
gi 35038601   448 EQLEATVKKLEESKQLLKNNEKLITWLNKEL 478
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 250-470 1.75e-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: 54.13  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   250 LQNRLSELEAANKDLterkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLdvechekEKHVNQLQTKVAVLEQ 329
Cdd:pfam07888  32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYKRDREQWERQRREL-------ESRVAELKEELRQSRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   330 EIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 409
Cdd:pfam07888  95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35038601   410 QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 470
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
275-488 2.02e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 53.75  E-value: 2.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 275 IRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVV 354
Cdd:COG4372  47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 355 LEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQ 434
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 35038601 435 SLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 488
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 321-469 2.09e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 53.68  E-value: 2.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK----- 395
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 396 ---------------------TLMGKLKLKNTVTIQQEKLLAE---KEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 451
Cdd:COG3883  95 lyrsggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                       170
                ....*....|....*...
gi 35038601 452 ATVKKLEESKQLLKNNEK 469
Cdd:COG3883 175 AQQAEQEALLAQLSAEEA 192
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 286-487 2.70e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.92  E-value: 2.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    286 EEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDkdqlvlrtkeafdtIQEQKVVLEENGEKNQVQ 365
Cdd:TIGR02169  673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE--------------IEKEIEQLEQEEEKLKER 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    366 LGKLEATIKSLSAELLKANEIIKKLqgdlktlmgklklkntvtiqqEKLLAEKEEKLQKEQKELQDVGQSLRikeqevck 445
Cdd:TIGR02169  739 LEELEEDLSSLEQEIENVKSELKEL---------------------EARIEELEEDLHKLEEALNDLEARLS-------- 789

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 35038601    446 lQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 487
Cdd:TIGR02169  790 -HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 236-482 9.59e-07

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: 52.43  E-value: 9.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    236 KKDLEILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEElqrtkqevlsLRRENSTLDVECHEKEK 315
Cdd:pfam15921  255 QNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ----------ARNQNSMYMRQLSDLES 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    316 HVNQLQTKVAVLEQEIKDK-----DQLVLRTKEAFDTIQEQKVVLEENGEKNQvQLGKLEATIKSLSAELLKANEIIKKL 390
Cdd:pfam15921  325 TVSQLRSELREAKRMYEDKieeleKQLVLANSELTEARTERDQFSQESGNLDD-QLQKLLADLHKREKELSLEKEQNKRL 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    391 ----QGDLKT---LMGKLKLKNTVTIQQEKLL----AEKEEKLQKEQKELQDVGQSLrikeQEVCKLQEQLEAT------ 453
Cdd:pfam15921  404 wdrdTGNSITidhLRRELDDRNMEVQRLEALLkamkSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTkemlrk 479

                          250       260       270
                   ....*....|....*....|....*....|
gi 35038601    454 -VKKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:pfam15921  480 vVEELTAKKMTLESSERTVSDLTASLQEKE 509
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
247-483 1.49e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 51.58  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  247 IHQLQNRLSELEAANKDL---TERKYKGDSTIRELKAKLSGVEEELQRTKQEV-LSLRRENSTLDV---ECHEKEKHVNQ 319
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeAGLDDADAEAVEARREELEDRDEELRDRLEECrVAAQAHNEEAESlreDADDLEERAEE 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  320 LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG 399
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE 440

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  400 KLKlkntvtiQQEKLLA---------------------EKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVK--- 455
Cdd:PRK02224 441 RVE-------EAEALLEagkcpecgqpvegsphvetieEDRERVEELEAELED----LEEEVEEVEERLERAEDLVEaed 509

                        250       260
                 ....*....|....*....|....*...
gi 35038601  456 KLEESKQLLKNNEKLITWLNKELNENQL 483
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRE 537
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 237-488 1.55e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 51.56  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   237 KDLE---ILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDvechEK 313
Cdd:TIGR04523  57 KNLDknlNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLE----KQ 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   314 EKHVNQLQTKVAVleqEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKAN---EIIKKL 390
Cdd:TIGR04523 133 KKENKKNIDKFLT---EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKK 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   391 QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 470
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289

                         250
                  ....*....|....*...
gi 35038601   471 ITWLNKELNENQLVRKQD 488
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQD 307
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
185-398 1.55e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  185 LAEKKQELDKLRNEWASHTAALtnkhsQELTNEKEKALQAQVQYQQQHEQQKKDLEIL-HQQNIHQLQNRLSELEAANKD 263
Cdd:COG4913  612 LAALEAELAELEEELAEAEERL-----EALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDD 686

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  264 LterkykgdstiRELKAKLSGVEEELQRTKQEvlslrrenstldvechekekhVNQLQTKVAVLEQEIKDKDQLVLRTKE 343
Cdd:COG4913  687 L-----------AALEEQLEELEAELEELEEE---------------------LDELKGEIGRLEKELEQAEEELDELQD 734

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 35038601  344 AFDTIQE-QKVVLEENGEK--NQVQLGKLEATI-KSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:COG4913  735 RLEAAEDlARLELRALLEErfAAALGDAVERELrENLEERIDALRARLNRAEEELERAM 793
PTZ00121 PTZ00121
MAEBL; Provisional
 157-517 2.99e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   157 LKCSKEEKL---SLMQSLDDATKQLDFTRKTlAEKKQELDKLRNEWASHTA-----ALTNKHSQEL--TNEKEKALQAQV 226
Cdd:PTZ00121 1475 AKKKAEEAKkadEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKAEEAKKAdeakkAEEAKKADEAkkAEEKKKADELKK 1553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   227 QYQQQHEQQKKDLEILH--QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEElQRTKQEvlSLRREns 304
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAE--ELKKA-- 1628

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   305 tldvecHEKEKHVNQLQTKVavlEQEIKDKDQLvlRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKAN 384
Cdd:PTZ00121 1629 ------EEEKKKVEQLKKKE---AEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   385 EIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKqll 464
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR--- 1774

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 35038601   465 KNNEKLItwlNKELNENQLVRKQDVlgPSTTPPAHSSSNTIRSGISPNLNVVD 517
Cdd:PTZ00121 1775 KEKEAVI---EEELDEEDEKRRMEV--DKKIKDIFDNFANIIEGGKEGNLVIN 1822
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 161-401 4.32e-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: 49.38  E-value: 4.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 161 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALtnKHSQELTNEKEKALQAQVQYQQQHEQQKKDLE 240
Cdd:COG4942  47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI--AELRAELEAQKEELAELLRALYRLGRQPPLAL 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 241 ILHQQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLsgveEELQRTKQEVLSLRRenstldvechEKEKHVNQL 320
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQ-------AEELRADL----AELAALRAELEAERA----------ELEALLAEL 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEknqvqlgKLEATIKSLSAELLKANEiiKKLQGDLKTLMGK 400
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE-------ELEALIARLEAEAAAAAE--RTPAAGFAALKGK 254


                .
gi 35038601 401 L 401
Cdd:COG4942 255 L 255
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
254-474 4.58e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 4.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 254 LSELEAANKDLteRKYKGDSTIRELKaKLSGVEEELQRTKQEVLSLRRENSTLDvechEKEKHVNQLQTKVAVLEQEIKD 333
Cdd:COG4717  48 LERLEKEADEL--FKPQGRKPELNLK-ELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEK 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 334 KDQLvlrtKEAFDTIQEQKVvLEENGEKNQVQLGKLEA---TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 410
Cdd:COG4717 121 LEKL----LQLLPLYQELEA-LEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 35038601 411 QeklLAEKEEKLQKEQKELQdvgQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 474
Cdd:COG4717 196 D---LAEELEELQQRLAELE---EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
272-470 5.49e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 5.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 272 DSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 351
Cdd:COG4372  30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 352 KVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-LKNTVTIQQEKLLAEKEEKLQKEQKELQ 430
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEsLQEELAALEQELQALSEAEAEQALDELL 189

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 35038601 431 DVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 470
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
CAGE1 pfam15066
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ...
 239-472 5.52e-06

Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.


Pssm-ID: 464481  Cd Length: 528  Bit Score: 49.45  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   239 LEILHQQNiHQLQNRLSELEAANKDLTERkykgdstIRELKAKLsgveeelqrTKQEVLslrrenstLDVechekekhVN 318
Cdd:pfam15066 320 LQKLKHTN-RKQQMQIQDLQCSNLYLEKK-------VKELQMKI---------TKQQVF--------VDI--------IN 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   319 QLQTKVavlEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENgeKNQVQLGKLEATIKSLSAELLKANEIikKLQGDLKTLM 398
Cdd:pfam15066 367 KLKENV---EELIEDKYNVILEKNDINKTLQNLQEILANT--QKHLQESRKEKETLQLELKKIKVNYV--HLQERYITEM 439

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   399 GKLKLKNTVTIQQEKLLAEKEE---KLQKEQKELQDVGQSL--------RIKEQEVCKLQEQLEATVKK-LEESKQLLKN 466
Cdd:pfam15066 440 QQKNKSVSQCLEMDKTLSKKEEeveRLQQLKGELEKATTSAldllkrekETREQEFLSLQEEFQKHEKEnLEERQKLKSR 519


                  ....*.
gi 35038601   467 NEKLIT 472
Cdd:pfam15066 520 LEKLVA 525
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 183-428 5.72e-06

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 48.99  E-value: 5.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 183 KTLAEKKQELDKLRNEwashtAALTNKHSQELTNEKEKALqaqvqyqqqheqqkKDLEILhQQNIHQLQNRLSELEAANK 262
Cdd:COG4942  20 DAAAEAEAELEQLQQE-----IAELEKELAALKKEEKALL--------------KQLAAL-ERRIAALARRIRALEQELA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 263 DLTERkykgdstIRELKAKLSGVEEELQRTKQE----VLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLV 338
Cdd:COG4942  80 ALEAE-------LAELEKEIAELRAELEAQKEElaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 339 LRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKntvtIQQEKLLAEK 418
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL----QQEAEELEAL 228

                       250
                ....*....|
gi 35038601 419 EEKLQKEQKE 428
Cdd:COG4942 229 IARLEAEAAA 238
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 212-476 6.11e-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: 49.79  E-value: 6.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    212 QELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIHQlQNRLSELEAANKDLTerkykgdSTIRELKAKLSGVEEELQR 291
Cdd:pfam01576    4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEE-KNALQEQLQAETELC-------AEAEEMRARLAARKQELEE 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    292 TKQEvlslrrenstLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA 371
Cdd:pfam01576   76 ILHE----------LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    372 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 451
Cdd:pfam01576  146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225

                          250       260
                   ....*....|....*....|....*.
gi 35038601    452 ATVKKLEESK-QLLKNNEKLITWLNK 476
Cdd:pfam01576  226 ELQAQIAELRaQLAKKEEELQAALAR 251
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 186-484 7.37e-06

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 49.35  E-value: 7.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    186 AEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKAlqaqVQYQQQHEQQKKDLEILHQQNIHQ---LQNRLSELEAA-- 260
Cdd:pfam15921  252 SESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKA----SSARSQANSIQSQLEIIQEQARNQnsmYMRQLSDLESTvs 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    261 --NKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLD-------VECHEKEKHVN--QLQTK------ 323
Cdd:pfam15921  328 qlRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDdqlqkllADLHKREKELSleKEQNKrlwdrd 407

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    324 ------VAVLEQEIKDKDQLVLRTKEAFDTIQ-EQKVVLEENGEKNQVQLGKLEaTIKSLSAELLKANEIIKKLQGDLKT 396
Cdd:pfam15921  408 tgnsitIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTA 486

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    397 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ---EQLEATVKKLEESKQLLKNNEKLITW 473
Cdd:pfam15921  487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEI 566

                          330
                   ....*....|..
gi 35038601    474 LNKEL-NENQLV 484
Cdd:pfam15921  567 LRQQIeNMTQLV 578
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 244-448 8.66e-06

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


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 48.27  E-value: 8.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   244 QQNIHQLQNRLSELEAANkDLTERKYKGDST---IRELKAKLSGVEEELQRTKQEVLSLRREnstLDVECHEKEKHVNQL 320
Cdd:pfam15905 121 SASVASLEKQLLELTRVN-ELLKAKFSEDGTqkkMSSLSMELMKLRNKLEAKMKEVMAKQEG---MEGKLQVTQKNLEHS 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   321 QTKVAVLEQEIKDKDQLVLRTK----EAFDTIQEQKVVLEEnGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 396
Cdd:pfam15905 197 KGKVAQLEEKLVSTEKEKIEEKseteKLLEYITELSCVSEQ-VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSK 275

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 35038601   397 LMGKLKLK-NTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQE 448
Cdd:pfam15905 276 QIKDLNEKcKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
PRK12704 PRK12704
phosphodiesterase; Provisional
 348-459 8.76e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 8.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  348 IQEQKVVLEENGEKNQVQLGKLEAtiKSLSAE-LLKANEIIKKLQ----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEKL 422
Cdd:PRK12704  28 IAEAKIKEAEEEAKRILEEAKKEA--EAIKKEaLLEAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELL 105

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 35038601  423 QKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEE 459
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
132-487 8.84e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 8.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  132 KHLTHLSLKLLPGNDVEIKKFLAGClkcSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHS 211
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGL---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  212 ------QELTNEKEKALQAQVQYQQQHEqqKKDLEILHQQnIHQLQNRLSELEAANKDLTE--RKYKGDSTIRELKAKLS 283
Cdd:PRK03918 437 kcpvcgRELTEEHRKELLEEYTAELKRI--EKELKEIEEK-ERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLK 513

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  284 GV--------EEELQRTKQEVLSLRRENSTLDVECHEK---EKHVNQLQTKVAVLEQEIKD-KDQLVLRTKEAFDTIQEQ 351
Cdd:PRK03918 514 KYnleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAElLKELEELGFESVEELEER 593

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  352 KVVLEE-----NGEKNQVQ-LGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKE-EKLQK 424
Cdd:PRK03918 594 LKELEPfyneyLELKDAEKeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELE-------ELEKKYSEEEyEELRE 666

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 35038601  425 EQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 487
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
PRK12704 PRK12704
phosphodiesterase; Provisional
 260-427 9.15e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 9.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  260 ANKDLTERKYKGDSTIRELKAKLSGVEEE-LQRTKQEVLSLRREnstLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLV 338
Cdd:PRK12704  29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEaLLEAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  339 LRTKEAFDTiqeqkvvLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGD------LKTLMGKLKLKNTVTIQQe 412
Cdd:PRK12704 106 EKREEELEK-------KEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKE- 177

                        170
                 ....*....|....*
gi 35038601  413 kllAEKEEKLQKEQK 427
Cdd:PRK12704 178 ---IEEEAKEEADKK 189
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 243-482 1.32e-05

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: 48.58  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   243 HQQNI--HQLQNRLSELEAAN-KDLTERKYKGDSTIRELKAKLSGVEEELQR-----TKQEVLSLRRENSTLDVECHEKE 314
Cdd:pfam17380 280 HQKAVseRQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERK 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   315 KHVNQL-QTKVAVLEQEIKDKDQLVL-------RTKEAFDTIQEQKVVLEENGEKNQVQLGKLEatikSLSAELLKANEI 386
Cdd:pfam17380 360 RELERIrQEEIAMEISRMRELERLQMerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEARQR 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   387 -IKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQdvgqslriKEQEVCKLQEQLEATV--KKLEESKQL 463
Cdd:pfam17380 436 eVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--------KEKRDRKRAEEQRRKIleKELEERKQA 507

                         250
                  ....*....|....*....
gi 35038601   464 LKNNEKLITWLNKELNENQ 482
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQ 526
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
160-452 1.52e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 160 SKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAAL--TNKHSQELTNEKEKALQAQVQYQQQHEQQKK 237
Cdd:COG4372  29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELeqLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 238 DLEILHQQnIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKE--K 315
Cdd:COG4372 109 EAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldE 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 316 HVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK 395
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 35038601 396 TLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEA 452
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 244-456 1.71e-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: 1.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 244 QQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQEVLSLRREnstLDVECHEKEKHVNQLQTk 323
Cdd:COG4942  47 KKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAELAELEKEIAELRAE---LEAQKEELAELLRALYR- 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 324 vavleQEIKDKDQLVLRTKEAFDTIQEQKvVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 403
Cdd:COG4942 116 -----LGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 35038601 404 KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKK 456
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
PTZ00121 PTZ00121
MAEBL; Provisional
 157-487 3.20e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   157 LKCSKEEKlslmQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKhSQELTNEKEKALQAQVQYQQQHEQQK 236
Cdd:PTZ00121 1423 AKKKAEEK----KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKK 1497

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   237 KDLEILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIREL-KAKLSGVEEELQRTKQevlsLRRENSTLDVECHEKEK 315
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAkKAEEKKKADELKKAEE----LKKAEEKKKAEEAKKAE 1573

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   316 HVNQLQTKVAVLEQEIKDKdqlvlRTKEAFDTIQEQKVVLEENGEKNQvqlgklEATIKslsAELLKANEIIKKLQGDLK 395
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAE------EAKIK---AEELKKAEEEKKKVEQLK 1639

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   396 TLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL---EATVKKLEESKQLLKNNEKLIT 472
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAE 1719

                         330
                  ....*....|....*
gi 35038601   473 WLNKELNENQLVRKQ 487
Cdd:PTZ00121 1720 ELKKAEEENKIKAEE 1734
HD_XRCC4-like_N cd22210
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ...
 41-144 3.49e-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: 43.68  E-value: 3.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  41 RKDLVIRLTDDtdpFFLYNLVISEEDFQSLKFQQGLLVDFLAFPQKFIDLLQQCtqehAKEIPR--FLLQLVSPAAILdn 118
Cdd:cd22210  25 ERGLRLHVSDD---AFLWTGEVSESDISQLKNDQGILVDFASFPGKLRSALEKC----ILASDRftFVLTIRGDEAYL-- 95

                        90       100
                ....*....|....*....|....*.
gi 35038601 119 spaflnVVETNPFKHLTHLSLKLLPG 144
Cdd:cd22210  96 ------KLVEILDEQLPHITFALRKV 115
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
253-480 3.53e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  253 RLSELEAANKDLTErkykgdsTIRELKAKLSGVEEELQRTkQEVLSLRRENSTldvECHEKEKHVNQLQTKVAVLEQEIK 332
Cdd:PRK03918 156 GLDDYENAYKNLGE-------VIKEIKRRIERLEKFIKRT-ENIEELIKEKEK---ELEEVLREINEISSELPELREELE 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  333 DKDQLVLR---TKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQgdlktlmgKLKLKNTVTI 409
Cdd:PRK03918 225 KLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------ELKEKAEEYI 296

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35038601  410 QQEKLLAEKEEKLQKEQKELQDVgqslrikEQEVCKLQEQLeatvKKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRL-------EEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEE 356
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 312-487 3.92e-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: 46.30  E-value: 3.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 312 EKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQ 391
Cdd:COG4942  24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 392 GDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLI 471
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183

                       170
                ....*....|....*.
gi 35038601 472 TWLNKELNENQLVRKQ 487
Cdd:COG4942 184 EEERAALEALKAERQK 199
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
245-461 3.97e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  245 QNIHQLQNRLSELEAANKDLTERKYKgdstiRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEkhVNQLQTKV 324
Cdd:COG4913  225 EAADALVEHFDDLERAHEALEDAREQ-----IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  325 AVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQ-LGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgKLKL 403
Cdd:COG4913  298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAAL--GLPL 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  404 KNTVTI--QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK 461
Cdd:COG4913  376 PASAEEfaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
249-470 4.74e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 45.67  E-value: 4.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 249 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDV---ECHEKEKHVNQL----Q 321
Cdd:COG1340  47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLewrqQ 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 322 TKVAVLEQEIkdkdQLVLRTKEAFDTIQEQKVVLEENGEKN---------QVQLGKLEATIKSLSAELLKANEIIKKLQG 392
Cdd:COG1340 127 TEVLSPEEEK----ELVEKIKELEKELEKAKKALEKNEKLKelraelkelRKEAEEIHKKIKELAEEAQELHEEMIELYK 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 393 DLKTLMGKL-KLKNTVTIQQEKL--LAEKEEKLQKEQKELQDVGQSLRIKEQEVcKLQEQLEATVKKLEESKQLLKNNEK 469
Cdd:COG1340 203 EADELRKEAdELHKEIVEAQEKAdeLHEEIIELQKELRELRKELKKLRKKQRAL-KREKEKEELEEKAEEIFEKLKKGEK 281


                .
gi 35038601 470 L 470
Cdd:COG1340 282 L 282
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 237-469 6.13e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 45.98  E-value: 6.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  237 KDLEILHQQN---IHQLQNRLSELEaanKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQevlslrrENSTLDVEchEK 313
Cdd:PRK04778 129 QELLESEEKNreeVEQLKDLYRELR---KSLLANRFSFGPALDELEKQLENLEEEFSQFVE-------LTESGDYV--EA 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  314 EKHVNQLQTKVAVLEQEIKDKDQLVLRT-----------KEAFDTIQEQKVVLEENGEKNQV-----QLGKLEATIKSLs 377
Cdd:PRK04778 197 REILDQLEEELAALEQIMEEIPELLKELqtelpdqlqelKAGYRELVEEGYHLDHLDIEKEIqdlkeQIDENLALLEEL- 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  378 aELLKANEIIKKLQGDLKTLMGKL----KLKNTVTIQQEKL---LAEKEEKLQKEQKELQDVGQSLRIKEQEVCK---LQ 447
Cdd:PRK04778 276 -DLDEAEEKNEEIQERIDQLYDILerevKARKYVEKNSDTLpdfLEHAKEQNKELKEEIDRVKQSYTLNESELESvrqLE 354

                        250       260
                 ....*....|....*....|..
gi 35038601  448 EQLEATVKKLEESKQLLKNNEK 469
Cdd:PRK04778 355 KQLESLEKQYDEITERIAEQEI 376
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
190-490 6.57e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 6.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 190 QELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQ---QNIHQLQNRLSELEAANKDLTE 266
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyQELEALEAELAELPERLEELEE 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 267 RKykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTldvechEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFD 346
Cdd:COG4717 154 RL----EELRELEEELEELEAELAELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 347 TIQEQKVVLEENGEKNQV--QLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQK 424
Cdd:COG4717 224 ELEEELEQLENELEAAALeeRLKEARLLLLIAAA-LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 35038601 425 EQKELQDVGQSLRIKEQEVCKL-----------QEQLEATVKKLEESKQLLKNNEKlitwLNKELNENQLVRKQDVL 490
Cdd:COG4717 303 EAEELQALPALEELEEEELEELlaalglppdlsPEELLELLDRIEELQELLREAEE----LEEELQLEELEQEIAAL 375
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
247-470 7.30e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.21  E-value: 7.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  247 IHQLQNRLSELEaankDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAV 326
Cdd:PRK03918 171 IKEIKRRIERLE----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  327 LEQEIKDKDQLVLRTKEAFDTIQEQKVVLEEngeknqvqLGKLEATIKSLSaELLKANEIIKKLQGDLKTLMGKLKLKNT 406
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEE--------LEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLS 317

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 35038601  407 VTIQQEKLLAEKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 470
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEAKAKKEELERL 377
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 244-486 7.62e-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: 46.12  E-value: 7.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    244 QQNIHQLQNRLSELEAANKDLTERKYKgdsTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 323
Cdd:pfam02463  182 TENLAELIIDLEELKLQELKLKEQAKK---ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    324 VAVLEQEIKDKDQLVLRTKEAFDTIQE-QKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG--- 399
Cdd:pfam02463  259 EIEKEEEKLAQVLKENKEEEKEKKLQEeELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEeie 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    400 -KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 478
Cdd:pfam02463  339 eLEKELKELEIKREAEEEEEEELEKLQEKLEQL----EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414


                   ....*...
gi 35038601    479 NENQLVRK 486
Cdd:pfam02463  415 RQLEDLLK 422
46 PHA02562
endonuclease subunit; Provisional
 238-479 9.59e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 45.39  E-value: 9.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  238 DLEILH-QQNIHQLQNRLSELEAANKDLTERKykgdstirelKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH 316
Cdd:PHA02562 187 DMKIDHiQQQIKTYNKNIEEQRKKNGENIARK----------QNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  317 VNQLQTKVAVLEQEIK--DKDQLVLRT-------KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEII 387
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEqfQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  388 KKLQgDLKTLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDvgqSLRIKEQEVCKLQEQLEATVKKLEESKQ----- 462
Cdd:PHA02562 337 KKLL-ELKNKISTNK-------QSLITLVDKAKKVKAAIEELQA---EFVDNAEELAKLQDELDKIVKTKSELVKekyhr 405

                        250       260
                 ....*....|....*....|....*....
gi 35038601  463 -----LLKNN-------EKLITWLNKELN 479
Cdd:PHA02562 406 givtdLLKDSgikasiiKKYIPYFNKQIN 434
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 242-466 1.49e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    242 LHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEeelqRTKQEVLSLRREnstLDVECHEKEKHVNQLQ 321
Cdd:pfam01576  156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE----KGRQELEKAKRK---LEGESTDLQEQIAELQ 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    322 TKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKL 401
Cdd:pfam01576  229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL 308

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35038601    402 KLKNTVTIQQEKLLAEKEEKLQKEQKELQDVG-------QSLRIKE-QEVCKLQEQLEATVK---KLEESKQLLKN 466
Cdd:pfam01576  309 EDTLDTTAAQQELRSKREQEVTELKKALEEETrsheaqlQEMRQKHtQALEELTEQLEQAKRnkaNLEKAKQALES 384
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 275-471 1.65e-04

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: 44.71  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   275 IRELKAKLSGVEEELQRtkqEVLSLRRENSTLDVECHEKEkhvNQLQTKVAVLEQEIKDKDQLVLRTK---EAFDTIQEQ 351
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKE---NKMKDLTFLLEESRDKANQLEEKTKlqdENLKELIEK 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   352 KVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNT----VTIQQEKLLAEKEEKLQKEQK 427
Cdd:pfam05483 291 KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEELLRTEQQ 370

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 35038601   428 ELQDVGQSLRIKEQEVCKLQEQLEATVK-------KLEESKQLLKNNEKLI 471
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLL 421
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 239-485 1.70e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 44.92  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  239 LEILHQQNIHQLQNrLSELEAANKDLTERKYKGD-----STIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEK 313
Cdd:PRK05771  22 LEALHELGVVHIED-LKEELSNERLRKLRSLLTKlsealDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  314 EkhVNQLQTKVAVLEQEIKDKDQLVLRTK--EAFDTiqeqKVVLEENGEKNQVQLGKLEATIKS-LSAELLKANEIIKKl 390
Cdd:PRK05771 101 E--IKELEEEISELENEIKELEQEIERLEpwGNFDL----DLSLLLGFKYVSVFVGTVPEDKLEeLKLESDVENVEYIS- 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  391 qgdlktlmgKLKLKNTVTIQQEKLLAEK-EEKLQK---EQKELQDVG---QSLRIKEQEVCKLQEQLEATVKKLEESKQl 463
Cdd:PRK05771 174 ---------TDKGYVYVVVVVLKELSDEvEEELKKlgfERLELEEEGtpsELIREIKEELEEIEKERESLLEELKELAK- 243

                        250       260
                 ....*....|....*....|..
gi 35038601  464 lKNNEKLITWlnKELNENQLVR 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 ...
 181-487 1.83e-04

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.96  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    181 TRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIHQLQNRLSELEAA 260
Cdd:pfam02463  665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    261 NKDLTERKYKGDSTIRELKAKLSgvEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLR 340
Cdd:pfam02463  745 IDEEEEEEEKSRLKKEEKEEEKS--ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    341 TKEAFDTIQEQKVVLEENGEKN-QVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtvTIQQEKLLAEKE 419
Cdd:pfam02463  823 LIEQEEKIKEEELEELALELKEeQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL--ESKEEKEKEEKK 900

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 35038601    420 EKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 487
Cdd:pfam02463  901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLA 968
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 169-570 1.85e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 44.72  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    169 QSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtAALTNKHSQELTNEKE---KALQAQVQYQQQHEQQKKDLEILHQQ 245
Cdd:pfam15921  496 RTVSDLTASLQEKERAIEATNAEITKLRSR-----VDLKLQELQHLKNEGDhlrNVQTECEALKLQMAEKDKVIEILRQQ 570

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    246 --NIHQLQNR--------LSELEAANKDLTER----------KYKGDSTIRELKAKLSGVEeelqrtkqevlslrrenst 305
Cdd:pfam15921  571 ieNMTQLVGQhgrtagamQVEKAQLEKEINDRrlelqefkilKDKKDAKIRELEARVSDLE------------------- 631

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    306 ldvecHEKEKHVNQLQTKVAVLEQEIKDKDQL---VLRTKEAFDTIQEQKVVLEEN----GEKNQVQLGKLEATIKSLSA 378
Cdd:pfam15921  632 -----LEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDYEVLKRNfrnkSEEMETTTNKLKMQLKSAQS 706

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    379 ELLKANEIIKKLQGD----LKTLMGKLK-----------LKNTVTIQQEKLL-AEKEEKLQKEQKelQDVGQSLRIKEQE 442
Cdd:pfam15921  707 ELEQTRNTLKSMEGSdghaMKVAMGMQKqitakrgqidaLQSKIQFLEEAMTnANKEKHFLKEEK--NKLSQELSTVATE 784

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    443 VCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQ-LVRKQDvlgpsttppahssSNTIRSGISPNLNVVDGRlt 521
Cdd:pfam15921  785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQdIIQRQE-------------QESVRLKLQHTLDVKELQ-- 849

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|
gi 35038601    522 yptcGIGYPVSSAFAFQNTFPHSISAKNTSHPGSGTKVQF-NLQFTKPNA 570
Cdd:pfam15921  850 ----GPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFlSHHSRKTNA 895
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 247-465 2.08e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.44  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  247 IHQLQN----RLSELEAANKDLTERKYKGDSTirelkaklsGVEEELQRTKQEVLSLRRENSTLDVEchEKEKHVNQLQT 322
Cdd:PRK04778 221 LKELQTelpdQLQELKAGYRELVEEGYHLDHL---------DIEKEIQDLKEQIDENLALLEELDLD--EAEEKNEEIQE 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  323 KV----AVLEQEIKDK---DQLVLRTKEAFDTIQEQKVVLEEngEKNQVQLG-----KLEATIKSLSAELlkaNEIIKKL 390
Cdd:PRK04778 290 RIdqlyDILEREVKARkyvEKNSDTLPDFLEHAKEQNKELKE--EIDRVKQSytlneSELESVRQLEKQL---ESLEKQY 364

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 35038601  391 QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEkLQKEQKELQDVGQSLRIKEQEVcklQEQLEATVKKLEESKQLLK 465
Cdd:PRK04778 365 DEITERIAEQEIAYSELQEELEEILKQLEE-IEKEQEKLSEMLQGLRKDELEA---REKLERYRNKLHEIKRYLE 435
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 153-459 2.50e-04

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: 44.12  E-value: 2.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   153 LAGCLKcskeEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALtNKHSQELTNEKEKALQAQVQYQQQH 232
Cdd:pfam07888  36 LEECLQ----ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAEL-KEELRQSREKHEELEEKYKELSASS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   233 EQQKKDLEILHQQNIHQLQnRLSELEAANKDLTERKYKGDSTIRELK--------------AKLSGVEEELQRTKQEVLS 298
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEA-RIRELEEDIKTLTQRVLERETELERMKerakkagaqrkeeeAERKQLQAKLQQTEEELRS 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   299 LRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLR---TKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKS 375
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRDR 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   376 LSAELLKANEIIKKLQGDLKTLMGKLK------------LKNTVTIQQEKL------LAEKEEKLQKEQ----------- 426
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQLADASLALRegrarwaqeretLQQSAEADKDRIeklsaeLQRLEERLQEERmereklevelg 349

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 35038601   427 --------------KELQDVGQSLRIKEQEvcklQEQLEATVKKLEE 459
Cdd:pfam07888 350 rekdcnrvqlsesrRELQELKASLRVAQKE----KEQLQAEKQELLE 392
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 163-389 2.94e-04

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: 42.99  E-value: 2.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 163 EKLSLMQSLDDATKQLDFTRKTLaekKQELDKLRNEWASHTAALTNKhsqeltnekekalqaqvqyqqqheqqkkdleil 242
Cdd:COG1579   7 RALLDLQELDSELDRLEHRLKEL---PAELAELEDELAALEARLEAA--------------------------------- 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 243 hQQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLSGV--EEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQL 320
Cdd:COG1579  51 -KTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEEL 122

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 35038601 321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQkvvLEENGEKNQVQLGKLEATIkslSAELLKANEIIKK 389
Cdd:COG1579 123 EEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREELAAKI---PPELLALYERIRK 185
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 212-469 2.99e-04

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: 43.94  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   212 QELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQN---IHQLQNRlSELEAAN-KDLTERKYKGDSTIRELKAKLS---- 283
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESrdkANQLEEK-TKLQDENlKELIEKKDHLTKELEDIKMSLQrsms 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   284 ---GVEEELQRTKQEVLSLRRENSTLDVECHE-KEKH---VNQLQTKVAVLEQeikdkdqlVLRTkeafdtiQEQKVvle 356
Cdd:pfam05483 311 tqkALEEDLQIATKTICQLTEEKEAQMEELNKaKAAHsfvVTEFEATTCSLEE--------LLRT-------EQQRL--- 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   357 engEKNQVQLGKLEATIKSLSAELLKaneiikklqgdlktlMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSL 436
Cdd:pfam05483 373 ---EKNEDQLKIITMELQKKSSELEE---------------MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEEL 434

                         250       260       270
                  ....*....|....*....|....*....|...
gi 35038601   437 RIKEQEVCKLQEQLEATVKKLEESKQLLKNNEK 469
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
PRK12704 PRK12704
phosphodiesterase; Provisional
 361-480 3.29e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.61  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  361 KNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMGK---LKLKNtvtiQQEKLLAEKEEKLQKEQKELQDVGQSLR 437
Cdd:PRK12704  28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKE----ALLEAKeeiHKLRN----EFEKELRERRNELQKLEKRLLQKEENLD 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 35038601  438 IKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 170-436 3.42e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.86  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   170 SLDDATKQLDFTRKTLaekKQELDKLRNEWAShtaaltNKHSQEltnEKEKALQAQVQYQQQHEQQKKDLEilhqQNIHQ 249
Cdd:TIGR04523 451 VKELIIKNLDNTRESL---ETQLKVLSRSINK------IKQNLE---QKQKELKSKEKELKKLNEEKKELE----EKVKD 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   250 LQNRLSELEAANKDLTERKYKGDSTIRELKAKL---------SGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQL 320
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA----------TIKSLSAELLKANEIIKKL 390
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQevkqiketikEIRNKWPEIIKKIKESKTK 674

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 35038601   391 QGDLKTLMG----------KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSL 436
Cdd:TIGR04523 675 IDDIIELMKdwlkelslhyKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKEL 730
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 161-464 4.12e-04

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: 43.66  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   161 KEEKLSLMQS-LDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKhsQELTNEKEKALqaqvqyqqqheqqkkdl 239
Cdd:pfam10174 392 KERKINVLQKkIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL--EEALSEKERII----------------- 452

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   240 EILHQQNIHQLQNRLSELEAANKDLterkykgdstiRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQ 319
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKEN-----------KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS 521

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   320 LqtkvavlEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQvqlgkleaTIKSLSAELLKANEIIKKLQGDLKTLMG 399
Cdd:pfam10174 522 L-------EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIND--------RIRLLEQEVARYKEESGKAQAEVERLLG 586

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   400 KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEV--------------------CKLQEQLEATVKKLEE 459
Cdd:pfam10174 587 ILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMkkkgaqlleearrrednladNSQQLQLEELMGALEK 666


                  ....*
gi 35038601   460 SKQLL 464
Cdd:pfam10174 667 TRQEL 671
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 268-489 4.29e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 4.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 268 KYKgdSTIRELKAKLSGVEEELQRtkqevLSLRREnstldvechEKEKHVNQL--QTKVA----VLEQEIKDKDQLVLRT 341
Cdd:COG1196 169 KYK--ERKEEAERKLEATEENLER-----LEDILG---------ELERQLEPLerQAEKAeryrELKEELKELEAELLLL 232

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 342 KeaFDTIQEQKVVLEEngeknqvQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 421
Cdd:COG1196 233 K--LRELEAELEELEA-------ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 35038601 422 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDV 489
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 175-480 4.89e-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: 43.50  E-value: 4.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    175 TKQL-DFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEIlhqqnihQLQNR 253
Cdd:TIGR00606  572 KKQLeDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEES-------DLERL 644

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    254 LSELEAANKDLTERKYKG---DSTIRELKAKLSG----------VEEELQRTKQEVLSLRR----ENSTLDVECHEKEKH 316
Cdd:TIGR00606  645 KEEIEKSSKQRAMLAGATavySQFITQLTDENQSccpvcqrvfqTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKR 724

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    317 VNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSlSAELLKANEIIKKLQGDLKt 396
Cdd:TIGR00606  725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES-AKVCLTDVTIMERFQMELK- 802

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    397 lmgklklkntvtiqqekllaEKEEKLQKEQKELQDVGQSLRIKE--QEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 474
Cdd:TIGR00606  803 --------------------DVERKIAQQAAKLQGSDLDRTVQQvnQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862


                   ....*.
gi 35038601    475 NKELNE 480
Cdd:TIGR00606  863 KSKTNE 868
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
176-366 4.91e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 4.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 176 KQLDFTRKTLAEKKQELDKLRNE----WASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDL--------EILH 243
Cdd:COG3206 182 EQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpELLQ 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 244 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVL-SLRRENSTLDVECHEKEKHVNQLQT 322
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEA 341

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 35038601 323 KVAVL---EQEIKDKDQLVLRTKEAFDTIQE--QKVVLEENGEKNQVQL 366
Cdd:COG3206 342 RLAELpelEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 411-482 6.75e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 6.75e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 35038601 411 QEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 365-480 9.04e-04

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: 41.45  E-value: 9.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 365 QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKL-----QKE----QKELQDVGQS 435
Cdd:COG1579  25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEyealQKEIESLKRR 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 35038601 436 LRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
PTZ00121 PTZ00121
MAEBL; Provisional
 158-462 1.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   158 KCSKEEKLSLMQSLDDATKQLDFTRKtlAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKK 237
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEAKKDAEEAKK--AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK 1296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   238 DLEilHQQNIHQLQNRLSE---LEAANKDLTERKYKGDstirELKAKlsgveEELQRTKQEVLSLRRENSTLDVECHEKE 314
Cdd:PTZ00121 1297 KAE--EKKKADEAKKKAEEakkADEAKKKAEEAKKKAD----AAKKK-----AEEAKKAAEAAKAEAEAAADEAEAAEEK 1365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   315 KHVNQLQTKVAVLE-QEIKDKDQLVLRTKEAFDTIQEQKVVLEE----NGEKNQVQLGKLEATIKSLSAELLKANEIIKK 389
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAEEDKKKADElkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   390 LQGDLKTLMGKLKLKNTVTIQQEKLLAE----------KEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEA-TVKKLE 458
Cdd:PTZ00121 1446 ADEAKKKAEEAKKAEEAKKKAEEAKKADeakkkaeeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAeEAKKAD 1525


                  ....
gi 35038601   459 ESKQ 462
Cdd:PTZ00121 1526 EAKK 1529
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 247-466 1.23e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 41.76  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   247 IHQLQN----RLSELEAANKDLTERKYKGDSTirELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEchEKEKHVNQLQt 322
Cdd:pfam06160 202 YEELKTelpdQLEELKEGYREMEEEGYALEHL--NVDKEIQQLEEQLEENLALLENLELDEAEEALE--EIEERIDQLY- 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   323 kvAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEK-NQVQL-----GKLEATIKSLSAELlkaNEIIKKLQGDLKT 396
Cdd:pfam06160 277 --DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEElERVQQsytlnENELERVRGLEKQL---EELEKRYDEIVER 351

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   397 LMGKLKLKNTVTIQQEKLLaEKEEKLQKEQKELQDVGQSLRIKEQEVcklQEQLEATVKKLEESKQLLKN 466
Cdd:pfam06160 352 LEEKEVAYSELQEELEEIL-EQLEEIEEEQEEFKESLQSLRKDELEA---REKLDEFKLELREIKRLVEK 417
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 168-483 1.23e-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: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    168 MQSLDDATKQLDFTRKTLaekKQELDKLRNEwashtAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEI-LHQQN 246
Cdd:TIGR00618  565 MQEIQQSFSILTQCDNRS---KEDIPNLQNI-----TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVrLHLQQ 636

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    247 IHQ-LQNRLSELEAANKDLTERKYKGDS-TIRELKAKLSGV----EEELQRTKQEVLSLRRENSTLDVECHEKEKHV--- 317
Cdd:TIGR00618  637 CSQeLALKLTALHALQLTLTQERVREHAlSIRVLPKELLASrqlaLQKMQSEKEQLTYWKEMLAQCQTLLRELETHIeey 716

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    318 --------NQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKK 389
Cdd:TIGR00618  717 drefneieNASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREE 796

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    390 LQGDLKTLMGKlklkntvtIQQEKLLAEKEEKLQKEQ--KELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNN 467
Cdd:TIGR00618  797 DTHLLKTLEAE--------IGQEIPSDEDILNLQCETlvQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQ 868

                          330
                   ....*....|....*.
gi 35038601    468 EKLITWLNKELNENQL 483
Cdd:TIGR00618  869 AKIIQLSDKLNGINQI 884
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 140-496 1.42e-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: 41.88  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    140 KLLPGNDVEIKKFLAGCLKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnKHSQELTNEKE 219
Cdd:TIGR00618  190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK----------REAQEEQLKKQ 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    220 KALQAQVQYQQQHEQQKKDLEilHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRT------K 293
Cdd:TIGR00618  260 QLLKQLRARIEELRAQEAVLE--ETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRaahvkqQ 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    294 QEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVlrtkeafdTIQEQKVVLEENGEKNQVQLGKLEATI 373
Cdd:TIGR00618  338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH--------TLQQQKTTLTQKLQSLCKELDILQREQ 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    374 KSLSAELLKANEiikkLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ---EQL 450
Cdd:TIGR00618  410 ATIDTRTSAFRD----LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEqihLQE 485

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 35038601    451 EATVKKLEESKQLLKNNEKLITwlNKELNENQLVRKQDVLGPSTTP 496
Cdd:TIGR00618  486 TRKKAVVLARLLELQEEPCPLC--GSCIHPNPARQDIDNPGPLTRR 529
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 162-472 1.55e-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: 41.65  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   162 EEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWAshtaaltnkhsqELTNEKEKALQAQVQYQQQHEQQKKDLEI 241
Cdd:pfam05557  76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELS------------ELRRQIQRAELELQSTNSELEELQERLDL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   242 LHQqNIHQLQNRLSELEAANKDLTERKYKgdstIRELKAKLSGVE---EELQRTKQEVLSLRRENSTLDvECHEKEKHVN 318
Cdd:pfam05557 144 LKA-KASEAEQLRQNLEKQQSSLAEAEQR----IKELEFEIQSQEqdsEIVKNSKSELARIPELEKELE-RLREHNKHLN 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   319 QLQTKVAVLEQEIKDkdqlvLRTK-EAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLK----ANEIIKKLQGD 393
Cdd:pfam05557 218 ENIENKLLLKEEVED-----LKRKlEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpedlSRRIEQLQQRE 292

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 35038601   394 LkTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLIT 472
Cdd:pfam05557 293 I-VLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELT 370
PRK01156 PRK01156
chromosome segregation protein; Provisional
 236-480 1.57e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  236 KKDLEILHQQNIHQLQNRLSELEAANKDLTERKYKgDSTIRELKAKLSGVEEELQRTKQEVLSLRREN--------STLD 307
Cdd:PRK01156 503 KKRKEYLESEEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLKLEDLDSKRTSwlnalaviSLID 581

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  308 VEC-----HEKEKHVNQLQTKVAVLEQEIKD----KDQLVLRTKEAFDTIQEQKVVLEENgeknQVQLGKLEATIKSLSA 378
Cdd:PRK01156 582 IETnrsrsNEIKKQLNDLESRLQEIEIGFPDdksyIDKSIREIENEANNLNNKYNEIQEN----KILIEKLRGKIDNYKK 657

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  379 ELLKANEIIKKlqgdlktlmgklklKNTVTIQqeklLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ---EQLEATVK 455
Cdd:PRK01156 658 QIAEIDSIIPD--------------LKEITSR----INDIEDNLKKSRKALDDAKANRARLESTIEILRtriNELSDRIN 719

                        250       260
                 ....*....|....*....|....*
gi 35038601  456 KLEESKQLLKNNEKLITWLnKELNE 480
Cdd:PRK01156 720 DINETLESMKKIKKAIGDL-KRLRE 743
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 253-497 1.61e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  253 RLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRR-ENSTLDVECHEKEKHVnqlQTKVAVLEQEI 331
Cdd:PRK05771  80 SVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwGNFDLDLSLLLGFKYV---SVFVGTVPEDK 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  332 KDKDQLVLrtkeafdtiqEQKVVLEENGEKNQVQLgkLEATIKSLSAELlkaNEIIKKLQGDlktlmgKLKLKNTVTIQQ 411
Cdd:PRK05771 157 LEELKLES----------DVENVEYISTDKGYVYV--VVVVLKELSDEV---EEELKKLGFE------RLELEEEGTPSE 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  412 ekLLAEKEEKLQKEQKELQDVGQSLR----IKEQEVCKLQEQLEATVKKLEESKQLL--------------KNNEKLITW 473
Cdd:PRK05771 216 --LIREIKEELEEIEKERESLLEELKelakKYLEELLALYEYLEIELERAEALSKFLktdktfaiegwvpeDRVKKLKEL 293

                        250       260
                 ....*....|....*....|....
gi 35038601  474 LNKELNENQLVRKQDVLGPSTTPP 497
Cdd:PRK05771 294 IDKATGGSAYVEFVEPDEEEEEVP 317
COG5022 COG5022
Myosin heavy chain [General function prediction only];
267-480 1.63e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 41.99  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  267 RKYKGD--STIRELKAKLsgVEEELQRTKQEVLSLRRENSTLD--VECHEKEKHVNQLQTKVAVLeqeikdkdQLVLRTK 342
Cdd:COG5022  809 RKEYRSylACIIKLQKTI--KREKKLRETEEVEFSLKAEVLIQkfGRSLKAKKRFSLLKKETIYL--------QSAQRVE 878

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  343 EAFDTIQEQKvvlEENGEKNQVqlgkleatiKSLSAELLK-ANEIIKKLQGDLktlMGKLKLKNTVTIQQEKLLAEKEEK 421
Cdd:COG5022  879 LAERQLQELK---IDVKSISSL---------KLVNLELESeIIELKKSLSSDL---IENLEFKTELIARLKKLLNNIDLE 943

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 35038601  422 LQKE-QKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK-QLLKNNEKLITWlNKELNE 480
Cdd:COG5022  944 EGPSiEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVrEGNKANSELKNF-KKELAE 1003
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
161-312 1.87e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  161 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASH-TAALtnkhsQELTNEKEKALQAQVQYQQQHEQQKKDL 239
Cdd:COG4913  294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRL-----EQLEREIERLERELEERERRRARLEALL 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 35038601  240 EILHQQ---NIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHE 312
Cdd:COG4913  369 AALGLPlpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 415-482 1.93e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 1.93e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 35038601 415 LAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:COG3883  18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 157-488 1.96e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    157 LKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHsqELTNEkekaLQAQVQYQQQHEQQK 236
Cdd:TIGR00606  212 LKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM--KLDNE----IKALKSRKKQMEKDN 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    237 KDLEILHQQNIHQLQNRLSELEAANKdlterkykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEchekekh 316
Cdd:TIGR00606  286 SELELKMEKVFQGTDEQLNDLYHNHQ----------RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVE------- 348

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    317 VNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLgkleaTIKSLSAELLKANEIIKKLQGDLKT 396
Cdd:TIGR00606  349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTL-----VIERQEDEAKTAAQLCADLQSKERL 423

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    397 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDV---GQSLRIKEQEVCKLQEQL---EATVKKLEESKQLLKNNEKL 470
Cdd:TIGR00606  424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVikeLQQLEGSSDRILELDQELrkaERELSKAEKNSLTETLKKEV 503

                          330
                   ....*....|....*...
gi 35038601    471 ITWLNKELNENQLVRKQD 488
Cdd:TIGR00606  504 KSLQNEKADLDRKLRKLD 521
PRK12705 PRK12705
hypothetical protein; Provisional
 339-485 2.20e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.23  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  339 LRTKEAFDTIQEqkVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtIQQEKLLAEK 418
Cdd:PRK12705  30 RLAKEAERILQE--AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL-----------VQKEEQLDAR 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 35038601  419 EEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEAtvkKLEESKQLLKN--NEKLITWLNKELNENQLVR 485
Cdd:PRK12705  97 AEKLDNLENQLEEREKALSARELELEELEKQLDN---ELYRVAGLTPEqaRKLLLKLLDAELEEEKAQR 162
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 161-378 2.42e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 2.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 161 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWAShtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLE 240
Cdd:COG3883  36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---------AEAEIEERREELGERARALYRSGGSVSYLD 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 241 -ILHQQNIHQLQNR---LSELEAANKDLTErkykgdsTIRELKAKLSGVEEELQRTKQEVLSLRREnstldvechekekh 316
Cdd:COG3883 107 vLLGSESFSDFLDRlsaLSKIADADADLLE-------ELKADKAELEAKKAELEAKLAELEALKAE-------------- 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 35038601 317 vnqLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSA 378
Cdd:COG3883 166 ---LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 244-492 2.44e-03

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


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.19  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    244 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 323
Cdd:TIGR00606  856 QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS 935

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    324 VAVLEQEIKDK----DQLVLRTKEAFDTIQEQKvvleengeknQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG 399
Cdd:TIGR00606  936 NKKAQDKVNDIkekvKNIHGYMKDIENKIQDGK----------DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ 1005

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    400 KLKLKNtvtiQQEKLLAEkEEKLQKEQKELQDVGQSLRIKEQEVCKLQ-EQLEATVKKLEESKQLLKNNEKLITWLNKEL 478
Cdd:TIGR00606 1006 DIDTQK----IQERWLQD-NLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGY 1080

                          250
                   ....*....|....
gi 35038601    479 NENQLVRKQDVLGP 492
Cdd:TIGR00606 1081 EKEIKHFKKELREP 1094
Sas6_CC pfam18594
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of ...
 146-171 2.79e-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: 35.72  E-value: 2.79e-03
                          10        20
                  ....*....|....*....|....*.
gi 35038601   146 DVEIKKFLAGCLKCSKEEKLSLMQSL 171
Cdd:pfam18594   1 DSEVKKYLADCLKSLKEEKQLLEQKL 26
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 244-422 2.93e-03

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


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 39.50  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   244 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIR-------ELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH 316
Cdd:pfam15619  17 QNELAELQSKLEELRKENRLLKRLQKRQEKALGkyegtesELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   317 VNQLQTKVAVLEQEIKDKDqlVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 396
Cdd:pfam15619  97 LLRLRDQLKRLEKLSEDKN--LAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKKHKEAQEEVKI 174

                         170       180
                  ....*....|....*....|....*.
gi 35038601   397 LMGKLKLKNTvtiqqekLLAEKEEKL 422
Cdd:pfam15619 175 LQEEIERLQQ-------KLKEKEREL 193
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 376-482 3.15e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.52  E-value: 3.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 376 LSAELLKANEIIKKLQGDLKTLmgklklkntvtiQQEklLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVK 455
Cdd:COG4942  11 LALAAAAQADAAAEAEAELEQL------------QQE--IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ 76

                        90       100
                ....*....|....*....|....*..
gi 35038601 456 KLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:COG4942  77 ELAALEAELAELEKEIAELRAELEAQK 103
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
243-442 3.29e-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: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  243 HQQNIHQLQNRLSELEAANKDLteRKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH------ 316
Cdd:COG4913  260 LAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngg 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  317 --VNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQ----LGKLEATIKSLSAELLKANEIIKKL 390
Cdd:COG4913  338 drLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDL 417

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 35038601  391 QGDLKTLMGKLKL----KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQE 442
Cdd:COG4913  418 RRELRELEAEIASlerrKSNIPARLLALRDALAEALGLDEAELPFVGELIEVRPEE 473
TOP4c cd00187
DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), ...
 360-480 3.55e-03

DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), bacterial DNA gyrases (A subunit, GyrA),mammalian DNA toposiomerases II. DNA topoisomerases are essential enzymes that regulate the conformational changes in DNA topology by catalysing the concerted breakage and rejoining of DNA strands during normal cellular growth.


Pssm-ID: 238111 [Multi-domain]  Cd Length: 445  Bit Score: 40.24  E-value: 3.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 360 EKNQVQLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKElqdvgqslrik 439
Cdd:cd00187 341 GKAEARLHILEGLLKAILN-IDEVINLIRSSDEAKKALIEELEKLGFSEIQADAILDMRLRRLTKLERE----------- 408

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 35038601 440 eqevcKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:cd00187 409 -----KLLKELKELEAEIEDLEKILASEERPKDLWKEELDE 444
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 242-478 4.11e-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: 40.11  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   242 LHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQ 321
Cdd:pfam05557  80 LKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLE 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   322 TK---VAVLEQEIKD---------KDQLVLRTKEA---------------------FDTIQEQKVVLEENGEKNQVQLGK 368
Cdd:pfam05557 160 KQqssLAEAEQRIKElefeiqsqeQDSEIVKNSKSelaripelekelerlrehnkhLNENIENKLLLKEEVEDLKRKLER 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   369 LEATIKSLSAELLKANEIIKKLQGDLKTLMgklklKNTVTIQQEKLLAEKEEKLQKEQKELQ----DVGQSLRIKEQEVC 444
Cdd:pfam05557 240 EEKYREEAATLELEKEKLEQELQSWVKLAQ-----DTGLNLRSPEDLSRRIEQLQQREIVLKeensSLTSSARQLEKARR 314

                         250       260       270
                  ....*....|....*....|....*....|....
gi 35038601   445 KLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 478
Cdd:pfam05557 315 ELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV 348
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
359-490 4.24e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  359 GEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLL--AEKEEKLQKEQKELQDVGQSl 436
Cdd:COG4913  605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAS- 683

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 35038601  437 rikEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELN--ENQLVRKQDVL 490
Cdd:COG4913  684 ---SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaEEELDELQDRL 736
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 157-324 4.42e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    157 LKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHtaaltNKHSQELTNEKEKAlqaqvqyqqqheqqK 236
Cdd:TIGR02169  359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL-----KRELDRLQEELQRL--------------S 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    237 KDLEILHQQnIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH 316
Cdd:TIGR02169  420 EELADLNAA-IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498


                   ....*...
gi 35038601    317 VNQLQTKV 324
Cdd:TIGR02169  499 ARASEERV 506
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
262-480 5.38e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 5.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 262 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEikdKDQLVLRT 341
Cdd:COG1340  11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE---RDELNEKL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601 342 KEAFDTIQEQKVVLEENGEKN------QVQLGKLEATI--KSLSAEllKANEIIKKLQgDLKTLMGKLKlkntVTIQQEK 413
Cdd:COG1340  88 NELREELDELRKELAELNKAGgsidklRKEIERLEWRQqtEVLSPE--EEKELVEKIK-ELEKELEKAK----KALEKNE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 35038601 414 LLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
 247-478 5.95e-03

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 39.17  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   247 IHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENS-------TLDVECHEKEKHVNQ 319
Cdd:pfam09728   6 LMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSkailaksKLEKLCRELQKQNKK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   320 LQTKVAVLEQEIKDKDQLVlrtKEAF-DTIQEQKVVLEENGEKNQVQLG---KLEATIKSLSAELLKANEIIKKL--QGD 393
Cdd:pfam09728  86 LKEESKKLAKEEEEKRKEL---SEKFqSTLKDIQDKMEEKSEKNNKLREeneELREKLKSLIEQYELRELHFEKLlkTKE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601   394 LKTLMGKLKLKNTvTIQQEKLLAEKEeklQKEQKELQDvgQSLRIKEQEVcKLQEQLEATVKKLEESKQLLKNNEKLITW 473
Cdd:pfam09728 163 LEVQLAEAKLQQA-TEEEEKKAQEKE---VAKARELKA--QVQTLSETEK-ELREQLNLYVEKFEEFQDTLNKSNEVFTT 235


                  ....*
gi 35038601   474 LNKEL 478
Cdd:pfam09728 236 FKKEM 240
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 161-399 9.53e-03

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 39.07  E-value: 9.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  161 KEEKLSLMQSLDDATKQLDFTRKTLAEKkqeLDKLRNEWASHTAALTN----KHSQELTNEKEKAlQAQVQYQQQHEQQK 236
Cdd:PLN03229 485 QERLENLREEFSKANSQDQLMHPVLMEK---IEKLKDEFNKRLSRAPNylslKYKLDMLNEFSRA-KALSEKKSKAEKLK 560

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  237 KDLEILHQQNIHQLQNRlSELEAANKDLTERK-YKGDSTIRELKAKLSGVEEELQRTKQEVLslrrENSTLDVECHEK-- 313
Cdd:PLN03229 561 AEINKKFKEVMDRPEIK-EKMEALKAEVASSGaSSGDELDDDLKEKVEKMKKEIELELAGVL----KSMGLEVIGVTKkn 635

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601  314 -----EKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLG----KLEATIKSLSAELLKAN 384
Cdd:PLN03229 636 kdtaeQTPPPNLQEKIESLNEEINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKekieALEQQIKQKIAEALNSS 715

                        250
                 ....*....|....*...
gi 35038601  385 EIIKK---LQGDLKTLMG 399
Cdd:PLN03229 716 ELKEKfeeLEAELAAARE 733
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 249-487 9.82e-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: 39.05  E-value: 9.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    249 QLQNRL-SELEAANKDLTERKYKGDSTIRELKAKLSGV---EEELQRTKQEVLSLRRENSTLDvechEKEKHVNQLQTKV 324
Cdd:pfam12128  419 ALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQE----AANAEVERLQSEL 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    325 AVLEqeiKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKL------------EATIKSLSAELLKAN----EIIK 388
Cdd:pfam12128  495 RQAR---KRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhflrkeapdweQSIGKVISPELLHRTdldpEVWD 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 35038601    389 KLQGDLKTLMG-KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNN 467
Cdd:pfam12128  572 GSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNA 651

                          250       260
                   ....*....|....*....|.
gi 35038601    468 -EKLITWLNKELNENQLVRKQ 487
Cdd:pfam12128  652 rLDLRRLFDEKQSEKDKKNKA 672
 
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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