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Conserved domains on  [gi|76008363|ref|NP_001028846|]
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protein bicaudal D homolog 2 isoform 1 [Rattus norvegicus]

Protein Classification

protein bicaudal D homolog( domain architecture ID 12101353)

protein bicaudal D (Bic-D) homolog such as human Bic-D 2 that acts as an adapter protein linking the dynein motor complex to various cargos and converts dynein from a non-processive to a highly processive motor in the presence of dynactin

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
BicD pfam09730
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ...
83-797 0e+00

Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.


:

Pssm-ID: 462863 [Multi-domain]  Cd Length: 717  Bit Score: 1050.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    83 GQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGR 162
Cdd:pfam09730   1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   163 LRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEE 242
Cdd:pfam09730  81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   243 ALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDD-AVTAEPNNDAEALvNGFEHS--GLVKASLDNKT 319
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLDGLKFSEDeGAGTEPNNDGEAM-DGGENGggGLKNSGLDNRT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   320 STPRKDGLAPPSPSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTENLSAL 399
Cdd:pfam09730 240 STPRKSEVFPPAPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAM 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   400 RRLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILSCKYHVAVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAE 479
Cdd:pfam09730 320 RGLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   480 VQALTEKVSLLEKASHQDQELLAQLEKELRKVSDVAGETQGSLNVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 559
Cdd:pfam09730 400 AQDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   560 REGQGK-AGRTSPEGRGRRSPVLLPKGLLSTEIGRADGGtGDNSPSPSSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQ 638
Cdd:pfam09730 480 REGAGArARKSHQEPRGLRSPRLLTRGLFMGEVGTADTT-SNSPSPCSSCPGSPTSDFRREPMNIYNLVAIIRDQIKHLQ 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   639 AAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMV 718
Cdd:pfam09730 559 VAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYENEKAMV 638
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76008363   719 TETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLEL 797
Cdd:pfam09730 639 TETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLEDLEF 717
 
Name Accession Description Interval E-value
BicD pfam09730
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ...
83-797 0e+00

Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.


Pssm-ID: 462863 [Multi-domain]  Cd Length: 717  Bit Score: 1050.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    83 GQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGR 162
Cdd:pfam09730   1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   163 LRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEE 242
Cdd:pfam09730  81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   243 ALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDD-AVTAEPNNDAEALvNGFEHS--GLVKASLDNKT 319
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLDGLKFSEDeGAGTEPNNDGEAM-DGGENGggGLKNSGLDNRT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   320 STPRKDGLAPPSPSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTENLSAL 399
Cdd:pfam09730 240 STPRKSEVFPPAPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAM 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   400 RRLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILSCKYHVAVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAE 479
Cdd:pfam09730 320 RGLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   480 VQALTEKVSLLEKASHQDQELLAQLEKELRKVSDVAGETQGSLNVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 559
Cdd:pfam09730 400 AQDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   560 REGQGK-AGRTSPEGRGRRSPVLLPKGLLSTEIGRADGGtGDNSPSPSSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQ 638
Cdd:pfam09730 480 REGAGArARKSHQEPRGLRSPRLLTRGLFMGEVGTADTT-SNSPSPCSSCPGSPTSDFRREPMNIYNLVAIIRDQIKHLQ 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   639 AAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMV 718
Cdd:pfam09730 559 VAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYENEKAMV 638
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76008363   719 TETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLEL 797
Cdd:pfam09730 639 TETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLEDLEF 717
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
5-510 1.26e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   5 SEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEyglavleEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQ 84
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELEELELELEEAQAEEYE 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  85 AHTNHKKVAADGESREESLIQESASKEqyyvrkvlELQTELKQLRNVLINTQSE----NERLTSVAQELKEINQNVEIQR 160
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE--------ELEEELAELEEELEELEEEleelEEELEEAEEELEEAEAELAEAE 364
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 161 GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL 240
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 241 EEALETLKTEREQKNNLRKELShymSINDSFYTSHLQVSLDGLKFSDDAVTAEPNNDAEALVNGFEHSGLVKASLDNKTS 320
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLA---ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 321 TPRKDGLAPPSPSLVSDLLSELhiseiqkLKQQLVQMEREKVGLLATLQDTQKQLEQARGT-LSEQHEKVSRLTENLSAL 399
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAA-------LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALAR 594
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 400 RRLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILSCKYHVAVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAE 479
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
                       490       500       510
                ....*....|....*....|....*....|.
gi 76008363 480 VQALTEKVSLLEKASHQDQELLAQLEKELRK 510
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEE 705
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
23-262 1.36e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.46  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     23 RAEVKRLSHELAETTrEKIQAAEYGLAVLEEKHQ-LKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGEsREE 101
Cdd:TIGR02168  676 RREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-QLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    102 SLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    182 SELEEENISLQKQvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKEL 261
Cdd:TIGR02168  834 AATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                   .
gi 76008363    262 S 262
Cdd:TIGR02168  911 S 911
PLN02939 PLN02939
transferase, transferring glycosyl groups
20-301 2.85e-06

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 51.06  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   20 EWLRAEVKRLSHELAET-TREKIQAAEYGLAVLEEKHQLKLQfEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGES 98
Cdd:PLN02939 166 EALQGKINILEMRLSETdARIKLAAQEKIHVEILEEQLEKLR-NELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQF 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   99 REESLIQESASKEQYYVrkvLE-----LQTELKQLRNVLINTQSENERLTSVAQE-LKEINQNVEIQRGRLRDDIKEYkf 172
Cdd:PLN02939 245 LKAELIEVAETEERVFK---LEkerslLDASLRELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKA-- 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  173 reARLLQDYSELEEENISLQ---KQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKT 249
Cdd:PLN02939 320 --ALVLDQNQDLRDKVDKLEaslKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 76008363  250 EREqknnlRKELSHYMSINDSFYTSHLQVSLDGLKFSDDAvtaePNNDAEAL 301
Cdd:PLN02939 398 ESK-----KRSLEHPADDMPSEFWSRILLLIDGWLLEKKI----SNNDAKLL 440
 
Name Accession Description Interval E-value
BicD pfam09730
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ...
83-797 0e+00

Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.


Pssm-ID: 462863 [Multi-domain]  Cd Length: 717  Bit Score: 1050.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    83 GQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGR 162
Cdd:pfam09730   1 GQSVSSHKKVAADGESREESLLQESASKEAYYAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   163 LRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEE 242
Cdd:pfam09730  81 MRDEIKEYKVREARLLQDYSELEEENISLQKQVSVLKQNQVEFEGLKHEITRKEEETELLNSQLEEAIRLREIAERQLDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   243 ALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDD-AVTAEPNNDAEALvNGFEHS--GLVKASLDNKT 319
Cdd:pfam09730 161 ALETLKTEREQKNSLRKELSHYMTLNDFDYVSHLSISLDGLKFSEDeGAGTEPNNDGEAM-DGGENGggGLKNSGLDNRT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   320 STPRKDGLAPPSPSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTENLSAL 399
Cdd:pfam09730 240 STPRKSEVFPPAPSLVSDLLSELNISEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLTENLEAM 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   400 RRLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILSCKYHVAVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAE 479
Cdd:pfam09730 320 RGLQASKERQDALDSEKDRDSHEDGDYYEVDINGPEILECKYRVAVEEAGELREELKALKARYNTLEERYKEEKTRWEAE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   480 VQALTEKVSLLEKASHQDQELLAQLEKELRKVSDVAGETQGSLNVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 559
Cdd:pfam09730 400 AQDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEELANLYHHVCMCNNETPNRVMLDYY 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   560 REGQGK-AGRTSPEGRGRRSPVLLPKGLLSTEIGRADGGtGDNSPSPSSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQ 638
Cdd:pfam09730 480 REGAGArARKSHQEPRGLRSPRLLTRGLFMGEVGTADTT-SNSPSPCSSCPGSPTSDFRREPMNIYNLVAIIRDQIKHLQ 558
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   639 AAVDRTTELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKSKYENEKAMV 718
Cdd:pfam09730 559 VAVDRTTELSRQRGAALELSTESDKDKEALMEEILKLKSLLSTKREQIATLRTVLKANKQTAEVALANLKSKYENEKAMV 638
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76008363   719 TETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLELLEL 797
Cdd:pfam09730 639 TETMMKLRNELKALKEDAATFSSLRAMFATRCDEYVTQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLALTQRLEDLEF 717
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
5-510 1.26e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 71.89  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   5 SEEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEyglavleEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQ 84
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRLELEELELELEEAQAEEYE 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  85 AHTNHKKVAADGESREESLIQESASKEqyyvrkvlELQTELKQLRNVLINTQSE----NERLTSVAQELKEINQNVEIQR 160
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE--------ELEEELAELEEELEELEEEleelEEELEEAEEELEEAEAELAEAE 364
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 161 GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQL 240
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 241 EEALETLKTEREQKNNLRKELShymSINDSFYTSHLQVSLDGLKFSDDAVTAEPNNDAEALVNGFEHSGLVKASLDNKTS 320
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLA---ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 321 TPRKDGLAPPSPSLVSDLLSELhiseiqkLKQQLVQMEREKVGLLATLQDTQKQLEQARGT-LSEQHEKVSRLTENLSAL 399
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALEAA-------LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALAR 594
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 400 RRLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILSCKYHVAVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAE 479
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL 674
                       490       500       510
                ....*....|....*....|....*....|.
gi 76008363 480 VQALTEKVSLLEKASHQDQELLAQLEKELRK 510
Cdd:COG1196 675 LEAEAELEELAERLAEEELELEEALLAEEEE 705
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
23-262 1.36e-10

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 65.46  E-value: 1.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     23 RAEVKRLSHELAETTrEKIQAAEYGLAVLEEKHQ-LKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGEsREE 101
Cdd:TIGR02168  676 RREIEELEEKIEELE-EKIAELEKALAELRKELEeLEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA-QLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    102 SLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    182 SELEEENISLQKQvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKEL 261
Cdd:TIGR02168  834 AATERRLEDLEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                   .
gi 76008363    262 S 262
Cdd:TIGR02168  911 S 911
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
6-264 1.45e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363      6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREkIQAAEYGLAVLEEKH-QLKLQFEELEVDYEAIRSEMEQLK----- 79
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELEELQEELKEAEEE-LEELTAELQELEEKLeELRLEVSELEEEIEELQKELYALAneisr 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     80 -EAFGQAHTNHKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEI 158
Cdd:TIGR02168  300 lEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    159 QRGRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQ--VEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEIS 236
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeeLLKKLEEAELKELQAELEELEEELEELQEELERL 459
                          250       260
                   ....*....|....*....|....*...
gi 76008363    237 ERQLEEALETLKTEREQKNNLRKELSHY 264
Cdd:TIGR02168  460 EEALEELREELEEAEQALDAAERELAQL 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
38-261 2.96e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 2.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  38 REKIQAAEYgLAVLEEKHQLK-----LQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEq 112
Cdd:COG1196 207 RQAEKAERY-RELKEELKELEaelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE- 284
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 113 yyvrkvlELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQ 192
Cdd:COG1196 285 -------EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76008363 193 KQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKEL 261
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
6-539 7.63e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.48  E-value: 7.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   6 EEEEYARLVMEAQPEWLRAEVKRLSHELAET------TREKIQAAEYGLAVLEEK-HQLKLQFEELEVDYEAIRSEMEQL 78
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAqaeeyeLLAELARLEQDIARLEERrRELEERLEELEEELAELEEELEEL 335
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  79 KEAFGQAHTNHKKVAADGESREESLIQESASKEQyYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEI 158
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLE-AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 159 QRGRLRDDIKEykfREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAiRLKEISER 238
Cdd:COG1196 415 RLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL-LEELAEAA 490
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 239 QLEEALETLKTEREQKNNLRKELSHyMSINDSFYTSHLQVSLDGLKFSDDAVTA----------EPNNDAEALVNGFEHS 308
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALL-LAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqnivvEDDEVAAAAIEYLKAA 569
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 309 GLVKASLDNKTSTPRKDGLAPPSPSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEK 388
Cdd:COG1196 570 KAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 389 VSRLTENLSALRRLQAGKERQTSLDNEKDRDSHEdgdyyevdingpeilsckyhvAVAEAGELREQLKALHSTHEAREAQ 468
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE---------------------LAERLAEEELELEEALLAEEEEERE 708
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76008363 469 LAEEKGRYEAEVQALTEKVSLLEKASHQDQELLAQLEKELRKVSDVAGETQGSLNVAQDELVTFSEELANL 539
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5-264 1.97e-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: 55.07  E-value: 1.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363      5 SEEEEYARLVMEAQPEWLRAEVKRLSHELaETTREKIQAAEYGLAVLE-EKHQLKLQFEELEVDYEAIRSEMEQLKeafg 83
Cdd:TIGR02169  204 RREREKAERYQALLKEKREYEGYELLKEK-EALERQKEAIERQLASLEeELEKLTEEISELEKRLEEIEQLLEELN---- 278
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     84 qahtnhKKVAADGESREESL---IQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEinqNVEIQR 160
Cdd:TIGR02169  279 ------KKIKDLGEEEQLRVkekIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER---EIEEER 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    161 GRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEI--------------KRLEEETEYLNSQL 226
Cdd:TIGR02169  350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREInelkreldrlqeelQRLSEELADLNAAI 429
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 76008363    227 EDAI--------RLKEI------SERQLEEALETLKTEREQKNNLRKELSHY 264
Cdd:TIGR02169  430 AGIEakineleeEKEDKaleikkQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
22-264 2.50e-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: 54.69  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREE 101
Cdd:TIGR02169  707 LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA 786
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    102 SLiqeSASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:TIGR02169  787 RL---SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK 863
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    182 SELEEENISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNSQLEDAirlkeisERQLEEALETLKTEREQKNNLRKEL 261
Cdd:TIGR02169  864 EELEEELEELEAALRDLES---RLGDLKKERDELEAQLRELERKIEEL-------EAQIEKKRKRLSELKAKLEALEEEL 933

                   ...
gi 76008363    262 SHY 264
Cdd:TIGR02169  934 SEI 936
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
102-513 3.55e-07

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: 54.29  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    102 SLIQESASKEQYYVRKvleLQTELKqlrnvLINTQSENERLTSVAQELKEinqnveiQRGRLRddikeykfREARLLQDY 181
Cdd:TIGR02168  159 AIFEEAAGISKYKERR---KETERK-----LERTRENLDRLEDILNELER-------QLKSLE--------RQAEKAERY 215
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    182 SELEEENISLQKQVSVLRqnqvefeglkheIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKEL 261
Cdd:TIGR02168  216 KELKAELRELELALLVLR------------LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI 283
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    262 SHYMSINDSFYT--SHLQVSLDGLKFSDDAVTAEPNNDAEALVNGFEHSGLVKASLdnKTSTPRKDGLAPpspslvsdll 339
Cdd:TIGR02168  284 EELQKELYALANeiSRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL--AELEEKLEELKE---------- 351
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    340 selhisEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGtlseqheKVSRLTENLSALR-RLQAGKERQTSLDNEKDR 418
Cdd:TIGR02168  352 ------ELESLEAELEELEAELEELESRLEELEEQLETLRS-------KVAQLELQIASLNnEIERLEARLERLEDRRER 418
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    419 DSHEDGDyyevdiNGPEILSCKYHVAVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAEVQALTEKVSLLEKAShQDQ 498
Cdd:TIGR02168  419 LQQEIEE------LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ-ARL 491
                          410
                   ....*....|....*
gi 76008363    499 ELLAQLEKELRKVSD 513
Cdd:TIGR02168  492 DSLERLQENLEGFSE 506
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
22-262 1.55e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  22 LRAEVKRLSHELAETTREKIQAAEYGLAvlEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFgqahtnhkkvaadgeSREE 101
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELE--AELEELEAELEELEAELAELEAELEELRLEL---------------EELE 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 102 SLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDY 181
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 182 SELEEENISLQKQVSVLRQNQVEFEglKHEIKRLEEETEYLNSQLEDAIRLKEISERQ--LEEALETLKTEREQKNNLRK 259
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELA--EELLEALRAAAELAAQLEELEEAEEALLERLerLEEELEELEEALAELEEEEE 438

                ...
gi 76008363 260 ELS 262
Cdd:COG1196 439 EEE 441
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
116-539 2.24e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 51.31  E-value: 2.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 116 RKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQ---NVEIQRGRLRDDIKEYKFREA--RLLQDYSELEEENIS 190
Cdd:COG4717  64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEeleELEAELEELREELEKLEKLLQllPLYQELEALEAELAE 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 191 LQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIR-LKEISERQLEEALETLKTEREQKNNLRKELSHYMSIND 269
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 270 SFYTSHLQVSLDGLKFSDDAVTAEPNNDAEALVNGFEHSGLVKASLDNKTSTP------------RKDGLAPPSPSLVSD 337
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlgllalLFLLLAREKASLGKE 303
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 338 LLSELHISEIQKLKQQLVQMEREKVGLLATLQDTqkQLEQARGTLSEQHEKVSRLTENLSALRRLQAGKERQTSLDNEKD 417
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPE--ELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV 381
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 418 RDsheDGDYYEVDINGPEilsckYHVAVAEAGELREQLKALHSTHEAREAQLAEEkgRYEAEVQALTEKVSLLEKASHQD 497
Cdd:COG4717 382 ED---EEELRAALEQAEE-----YQELKEELEELEEQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEEL 451
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 76008363 498 QELLAQLEKELRKVsdvagETQGSLNVAQDELVTFSEELANL 539
Cdd:COG4717 452 REELAELEAELEQL-----EEDGELAELLQELEELKAELREL 488
PLN02939 PLN02939
transferase, transferring glycosyl groups
20-301 2.85e-06

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 51.06  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   20 EWLRAEVKRLSHELAET-TREKIQAAEYGLAVLEEKHQLKLQfEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGES 98
Cdd:PLN02939 166 EALQGKINILEMRLSETdARIKLAAQEKIHVEILEEQLEKLR-NELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQF 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   99 REESLIQESASKEQYYVrkvLE-----LQTELKQLRNVLINTQSENERLTSVAQE-LKEINQNVEIQRGRLRDDIKEYkf 172
Cdd:PLN02939 245 LKAELIEVAETEERVFK---LEkerslLDASLRELESKFIVAQEDVSKLSPLQYDcWWEKVENLQDLLDRATNQVEKA-- 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  173 reARLLQDYSELEEENISLQ---KQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKT 249
Cdd:PLN02939 320 --ALVLDQNQDLRDKVDKLEaslKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 76008363  250 EREqknnlRKELSHYMSINDSFYTSHLQVSLDGLKFSDDAvtaePNNDAEAL 301
Cdd:PLN02939 398 ESK-----KRSLEHPADDMPSEFWSRILLLIDGWLLEKKI----SNNDAKLL 440
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
346-522 3.86e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 346 EIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTENLSALRRLQAGKERQTSLDNEKDRDSHEDGD 425
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 426 YYEVDIngpEILSCKYHVAVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAEVQALTEKVSLLEKASHQDQELLAQLE 505
Cdd:COG1196 320 ELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
                       170
                ....*....|....*..
gi 76008363 506 KELRKVSDVAGETQGSL 522
Cdd:COG1196 397 ELAAQLEELEEAEEALL 413
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
52-812 5.24e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 5.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     52 EEKHQLKLQFEELEV-----DYEAIRSEMEQLKEAFGQAHTNHKkvaadgesREESLIQESASKEQYYVRKVLELQTELK 126
Cdd:TIGR02168  213 ERYKELKAELRELELallvlRLEELREELEELQEELKEAEEELE--------ELTAELQELEEKLEELRLEVSELEEEIE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    127 QLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENISLQKqvsvlrqnqvEFE 206
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE----------ELE 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    207 GLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKELshymsindsfytSHLQVSLDGLKfs 286
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL------------ERLEDRRERLQ-- 420
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    287 ddavtaepnndaealvngfehsglvkasldnktstprkdglappspSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLA 366
Cdd:TIGR02168  421 ----------------------------------------------QEIEELLKKLEEAELKELQAELEELEEELEELQE 454
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    367 TLQDTQKQLEQARGTLSEQHEKVsrltenLSALRRLQAGKERQTSLdneKDRDSHEDGDYYEV--------DINGP---- 434
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQAL------DAAERELAQLQARLDSL---ERLQENLEGFSEGVkallknqsGLSGIlgvl 525
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    435 -EILSC--KYHVAVAEAGELREQLKALHSTHEAREAQlaeekgryEAEVQALTEKVSLLEKASHQDQELLAQLEKELRKV 511
Cdd:TIGR02168  526 sELISVdeGYEAAIEAALGGRLQAVVVENLNAAKKAI--------AFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI 597
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    512 SDVAGetqgslnvAQDELVTFSEE----LANLYHHVCMCNNETPNRVMLDYYREGQ----------GKAGRTSPEGRGRR 577
Cdd:TIGR02168  598 EGFLG--------VAKDLVKFDPKlrkaLSYLLGGVLVVDDLDNALELAKKLRPGYrivtldgdlvRPGGVITGGSAKTN 669
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    578 SPVLLPKG-----------------LLSTEIGRADGGTgDNSPSPSSSLPSPLSDPRREPMNIYNLIAIIRDQIKHLQAA 640
Cdd:TIGR02168  670 SSILERRReieeleekieeleekiaELEKALAELRKEL-EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    641 VDRT-----------TELSRQRIASQELGPAVDKDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANLKS 709
Cdd:TIGR02168  749 IAQLskelteleaeiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    710 kYENEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDE-------MQRQLAAAEDEKKTLNSLLRMAI 782
Cdd:TIGR02168  829 -LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAllnerasLEEALALLRSELEELSEELRELE 907
                          810       820       830
                   ....*....|....*....|....*....|
gi 76008363    783 QQKLALTQRLELLELDHEQTRRGRNKATSK 812
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVR 937
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
6-200 5.64e-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: 5.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTReKIQAAEYGLAVLEEK-HQLKLQFEELEVDYEAIRSEM-EQLKEAFG 83
Cdd:COG4942  37 AELEKELAALKKEEKALLKQLAALERRIAALAR-RIRALEQELAALEAElAELEKEIAELRAELEAQKEELaELLRALYR 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  84 QAHTNHKKVAADGESreeslIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRL 163
Cdd:COG4942 116 LGRQPPLALLLSPED-----FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 76008363 164 RDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQ 200
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
6-247 7.75e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 7.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363      6 EEEEYARLVMEAQPEWLRAEVKRLS-HELAETTREKIQAAEYGLAVLEEKHQ-LKLQFEELEVDYEAIRSEMEQLKEAFG 83
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTlLNEEAANLRERLESLERRIAATERRLE 841
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     84 QAHTNHKKVAADGESREESLIQESASKEqyyvrkvlELQTELKQLRNVLINTQSE----NERLTSVAQELKEINQNV--- 156
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIE--------ELESELEALLNERASLEEAlallRSELEELSEELRELESKRsel 913
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    157 EIQRGRLRDDIKEYKFREARLLQDYSEL-----EEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAI- 230
Cdd:TIGR02168  914 RRELEELREKLAQLELRLEGLEVRIDNLqerlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIe 993
                          250       260
                   ....*....|....*....|....*.
gi 76008363    231 RLKEISERQ---------LEEALETL 247
Cdd:TIGR02168  994 EYEELKERYdfltaqkedLTEAKETL 1019
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
6-541 1.03e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363      6 EEEEYARLVMEAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAfGQA 85
Cdd:TIGR02168  319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IAS 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     86 HTNH----KKVAADGESREESLIQESASKEQYYVR-KVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQR 160
Cdd:TIGR02168  398 LNNEierlEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    161 GRLRDDIKEYKFREARLlqdySELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIR-----LKEI 235
Cdd:TIGR02168  478 DAAERELAQLQARLDSL----ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGgrlqaVVVE 553
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    236 SERQLEEALETLKTEREQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDDAVTAEPnnDAEALVNGFEHSGLVKASL 315
Cdd:TIGR02168  554 NLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP--KLRKALSYLLGGVLVVDDL 631
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    316 DNKTSTPRKDGLAPPSPSLVSDLL---------SELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEqh 386
Cdd:TIGR02168  632 DNALELAKKLRPGYRIVTLDGDLVrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE-- 709
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    387 ekvsrLTENLSALRRLQAGKERQTSLDNEKDRDSHEDGDYYEVDINGPEILSCKYHVAVAEAGELREQLKALHSTHEARE 466
Cdd:TIGR02168  710 -----LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76008363    467 AQLAEEKGRYEAEVQALTEKVSLLEKASHQDQELLAQLEKELRKVSDVAGETQGSLNVAQDELVTFSEELANLYH 541
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
6-271 1.05e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.30  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363      6 EEEEYARLVMEAQPEwLRAEVKRLSHELAETtREKIQAAEyglAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQa 85
Cdd:TIGR02169  781 LNDLEARLSHSRIPE-IQAELSKLEEEVSRI-EARLREIE---QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK- 854
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     86 htnhkkvaadgesREESLIQESASKEQyyvrKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRD 165
Cdd:TIGR02169  855 -------------EIENLNGKKEELEE----ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRK 917
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    166 DIKEYKFREARLLQDYSELEEENISLQKQVSvlrqNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISER---QLEE 242
Cdd:TIGR02169  918 RLSELKAKLEALEEELSEIEDPKGEDEEIPE----EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKrldELKE 993
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 76008363    243 ALETLKTER-------EQKNNLRKE--LSHYMSINDSF 271
Cdd:TIGR02169  994 KRAKLEEERkaileriEEYEKKKREvfMEAFEAINENF 1031
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
32-261 1.34e-05

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: 48.95  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    32 ELAETTREKIQAAEYGLAVLEEKHQLKL-QFEELEVDYEAIRSEMEQLKEAFGQAHT------NHKKVAADGESREESL- 103
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKIITMELQKKSsELEEMTKFKNNKEVELEELKKILAEDEKlldekkQFEKIAEELKGKEQELi 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   104 --------------IQESASK--EQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDDI 167
Cdd:pfam05483 443 fllqarekeihdleIQLTAIKtsEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDI 522
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   168 KEYKFREARLLQDYSELEEENISLQKQVSVLRQnqvEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETL 247
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVRE---EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL 599
                         250
                  ....*....|....
gi 76008363   248 KTEREQKNNLRKEL 261
Cdd:pfam05483 600 KKQIENKNKNIEEL 613
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
22-539 1.62e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   22 LRAEVKRLS-----HELAETTREKIQAAEYGLAVL------EEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTN-- 88
Cdd:COG4913  247 AREQIELLEpirelAERYAAARERLAELEYLRAALrlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREEld 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   89 --HKKVAADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDD 166
Cdd:COG4913  327 elEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  167 IKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEF-----EGLKH------------EIKRLEEETE-----YLNS 224
Cdd:COG4913  407 LAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALrdalaEALGLdeaelpfvgeliEVRPEEERWRgaierVLGG 486
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  225 Q----------LEDAIRLkeISERQLEEALETLKTEREQKNNLRKE-----LSHYMSINDSFYTSHLQVSL--------- 280
Cdd:COG4913  487 FaltllvppehYAAALRW--VNRLHLRGRLVYERVRTGLPDPERPRldpdsLAGKLDFKPHPFRAWLEAELgrrfdyvcv 564
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  281 ---DGLKFSDDAVTAEpnndaealvngfehsGLVKASLDNKTSTPRKDGLAPPspslvsdLLSELHISEIQKLKQQLVQM 357
Cdd:COG4913  565 dspEELRRHPRAITRA---------------GQVKGNGTRHEKDDRRRIRSRY-------VLGFDNRAKLAALEAELAEL 622
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  358 EREkvglLATLQDTQKQLEQARGTLSEQHEKVSRLTENLSALRRLQAGKERQTSLDNEKDRDSHEDGDyyevdingpeil 437
Cdd:COG4913  623 EEE----LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD------------ 686
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  438 sckyhvaVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAEVQALTEKVSLLEKA-----SHQDQELLAQLEKEL---- 508
Cdd:COG4913  687 -------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaeDLARLELRALLEERFaaal 759
                        570       580       590
                 ....*....|....*....|....*....|...
gi 76008363  509 --RKVSDVAGETQGSLNVAQDELVTFSEELANL 539
Cdd:COG4913  760 gdAVERELRENLEERIDALRARLNRAEEELERA 792
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
345-510 1.83e-05

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: 46.84  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 345 SEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTENLSALR-RLQAGKERQTSLDNEKDRDSHED 423
Cdd:COG1579  17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEaRIKKYEEQLGNVRNNKEYEALQK 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 424 gdyyEVDINGPEILSCKYHV--AVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAEVQALTEKVSLLEKAShqdQELL 501
Cdd:COG1579  97 ----EIESLKRRISDLEDEIleLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER---EELA 169

                ....*....
gi 76008363 502 AQLEKELRK 510
Cdd:COG1579 170 AKIPPELLA 178
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
60-510 2.04e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.23  E-value: 2.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  60 QFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAAdGESREESLIQESASKEQyyVRKVLELQTELKQLRNVLintQSEN 139
Cdd:COG4717  72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEK--LLQLLPLYQELEALEAEL---AELP 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 140 ERLTSVAQELKEInQNVEIQRGRLRDDIKEYKFREARLLQDYSELEEENIS-----LQKQVSVLRQNQVEFEGLKHEIKR 214
Cdd:COG4717 146 ERLEELEERLEEL-RELEEELEELEAELAELQEELEELLEQLSLATEEELQdlaeeLEELQQRLAELEEELEEAQEELEE 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 215 LEEETEYLNSQLEDAIRLKEISERQLEEALETLktereqknnlrkeLSHYMSINDSFYTSHLQVS---------LDGLKF 285
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAA-------------LLALLGLGGSLLSLILTIAgvlflvlglLALLFL 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 286 SDDAVTAEPNNDAEALVNGFEHSGLVKASLDNKTStpRKDGLAPPSPSLVSDLLSelHISEIQKLKQQLVQMEREKvgLL 365
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLA--ALGLPPDLSPEELLELLD--RIEELQELLREAEELEEEL--QL 365
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 366 ATLQDTQKQLEQARGTLSEQhekvsRLTENLSALRRLQAGKERQTSLdnEKDRDSHEDGDYYEVDINGPEILSckyhvav 445
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEE-----ELRAALEQAEEYQELKEELEEL--EEQLEELLGELEELLEALDEEELE------- 431
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76008363 446 AEAGELREQLKALhsthEAREAQLAEEKGRYEAEVQALtEKVSLLEKASHQDQELLAQLEKELRK 510
Cdd:COG4717 432 EELEELEEELEEL----EEELEELREELAELEAELEQL-EEDGELAELLQELEELKAELRELAEE 491
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
20-229 3.15e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 3.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  20 EWLRAEVKRLSHELAETtREKIQA--AEYGLAVLEEKHQLKL-QFEELEVDYEAIRSEMEQLKEAFGQAhtnhKKVAADG 96
Cdd:COG3206 178 EFLEEQLPELRKELEEA-EAALEEfrQKNGLVDLSEEAKLLLqQLSELESQLAEARAELAEAEARLAAL----RAQLGSG 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  97 ESREESLIQESAskEQYYVRKVLELQTELKQLRNVLintQSENERLTSVAQELKEINQNVEIQRGRLRDDIK-EYKFREA 175
Cdd:COG3206 253 PDALPELLQSPV--IQQLRAQLAELEAELAELSARY---TPNHPDVIALRAQIAALRAQLQQEAQRILASLEaELEALQA 327
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 76008363 176 RLlqdySELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDA 229
Cdd:COG3206 328 RE----ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
22-262 4.56e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.37  E-value: 4.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREE 101
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    102 SLIQESASKEQYYVRKVlELQTELKQLRNVLINTQSE--NERLTSVAQELKEINQNVEIQRGRLRD---DIKEYKFREAR 176
Cdd:TIGR02169  752 EIENVKSELKELEARIE-ELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREieqKLNRLTLEKEY 830
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    177 LLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYlnsqledairlkeiSERQLEEALETLKTEREqknN 256
Cdd:TIGR02169  831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA--------------ALRDLESRLGDLKKERD---E 893

                   ....*.
gi 76008363    257 LRKELS 262
Cdd:TIGR02169  894 LEAQLR 899
COG5022 COG5022
Myosin heavy chain [General function prediction only];
100-262 5.34e-05

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 46.99  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  100 EESLIQESASKEQYYVRKVLELQTELKQLRnvlintqsenerltSVAQELKEINQNVEIQRGRLRDDIKEYKfreaRLLQ 179
Cdd:COG5022  938 NNIDLEEGPSIEYVKLPELNKLHEVESKLK--------------ETSEEYEDLLKKSTILVREGNKANSELK----NFKK 999
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  180 DYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQ--LEDAIRLKEISERQLEEALETLKTEREQKNNL 257
Cdd:COG5022 1000 ELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILkpLQKLKGLLLLENNQLQARYKALKLRRENSLLD 1079

                 ....*
gi 76008363  258 RKELS 262
Cdd:COG5022 1080 DKQLY 1084
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
22-256 5.12e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.21  E-value: 5.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  22 LRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAhtnhkkvaadgESREE 101
Cdd:COG4942  25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-----------EKEIA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 102 SLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEykfrearLLQDY 181
Cdd:COG4942  94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76008363 182 SELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNN 256
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
54-260 5.70e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.47  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    54 KHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESL------IQESASKEQYYVRKVLELQTELKQ 127
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVkdltkkISSLKEKIEKLESEKKEKESKISD 542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   128 LRNVLINTQSENERlTSVAQELKEINQNVEiqrgRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSvlrQNQVEFEG 207
Cdd:TIGR04523 543 LEDELNKDDFELKK-ENLEKEIDEKNKEIE----ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE---EKEKKISS 614
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 76008363   208 LKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTEREQKNNLRKE 260
Cdd:TIGR04523 615 LEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
22-261 8.91e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 8.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   22 LRAEVKRLS--HELAETTREKIQAaeygLAVLEEKHQlklQFEELEVDYEAIRSEMEQLKEAFGQahtnhkKVAADGESR 99
Cdd:COG4913  230 LVEHFDDLEraHEALEDAREQIEL----LEPIRELAE---RYAAARERLAELEYLRAALRLWFAQ------RRLELLEAE 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  100 EESLIQESASKEQyyvrKVLELQTELKQLRNVLINTqsENERLTSVAQELKEINQnveiQRGRLRDDIKEYKFREARLLQ 179
Cdd:COG4913  297 LEELRAELARLEA----ELERLEARLDALREELDEL--EAQIRGNGGDRLEQLER----EIERLERELEERERRRARLEA 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  180 DYSELEEEnislqkqvsvLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTERE----QKN 255
Cdd:COG4913  367 LLAALGLP----------LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerRKS 436

                 ....*.
gi 76008363  256 NLRKEL 261
Cdd:COG4913  437 NIPARL 442
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
22-539 1.00e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   22 LRAEVKRLSHELAETTREKIQAAEY---GLAVLEEKHQLKLQFEELEVDYEAIR---SEMEQLKEAFGQAHTNHKKVAAD 95
Cdd:PRK02224 211 LESELAELDEEIERYEEQREQARETrdeADEVLEEHEERREELETLEAEIEDLRetiAETEREREELAEEVRDLRERLEE 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   96 GESREESLIQE----SASKEQYYVRKVlELQTELKQLRnvlintqsenERLTSVAQELKEINQNVEiqrgRLRDDIKEYK 171
Cdd:PRK02224 291 LEEERDDLLAEagldDADAEAVEARRE-ELEDRDEELR----------DRLEECRVAAQAHNEEAE----SLREDADDLE 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  172 FREARLLQDYSELEEEnisLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAirlkeisERQLEEALETLKTER 251
Cdd:PRK02224 356 ERAEELREEAAELESE---LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA-------EDFLEELREERDELR 425
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  252 EQKNNLRKElshymsindsfytshlqvsldgLKFSDDAVtaepnNDAEALVNgfehsglvkasldnktstprkdglAPPS 331
Cdd:PRK02224 426 EREAELEAT----------------------LRTARERV-----EEAEALLE------------------------AGKC 454
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  332 PSLVSDLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARgTLSEQHEKVSRLTENLSALRRLQAGKERQTS 411
Cdd:PRK02224 455 PECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIE 533
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  412 LDNEKDRDSHEDGDYYEVDINGPEILSCKYHVAVAEA----GELREQLKALHSTHEA--REAQLAEEKGRYEAEVQALTE 485
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAreevAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLRE 613
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 76008363  486 KVSLLEKASHQDQELLAqlEKELRKvSDVAGETQGS-LNVAQDELVTFSEELANL 539
Cdd:PRK02224 614 KREALAELNDERRERLA--EKRERK-RELEAEFDEArIEEAREDKERAEEYLEQV 665
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
131-414 1.03e-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: 42.44  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 131 VLINTQSENERLTSVAQELKEINQNVEiqrgRLRDDIKEYKFREARLLQDYSELEEENISLQKQVSVLRQNQVEFEGlkh 210
Cdd:COG4942  11 LALAAAAQADAAAEAEAELEQLQQEIA----ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA--- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 211 EIKRLEEETEYLNSQLEdaiRLKEISERQLEEAletlktereQKNNLRKELSHYMSINDSFYTSHLQVSLDGLKFSDDAV 290
Cdd:COG4942  84 ELAELEKEIAELRAELE---AQKEELAELLRAL---------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 291 TAEPNNDAEALVNgfehsglVKASLDNKTSTPRKDglappspslvsdllselhISEIQKLKQQLVQMEREKVGLLATLqd 370
Cdd:COG4942 152 AEELRADLAELAA-------LRAELEAERAELEAL------------------LAELEEERAALEALKAERQKLLARL-- 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 76008363 371 tQKQLEQARGTLSEQHEKVSRLTENLSALRRLQAGKERQTSLDN 414
Cdd:COG4942 205 -EKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
345-539 1.60e-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: 41.67  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 345 SEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTENLSAL--------RRLQAGKERQTSLDNEK 416
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALeqelaaleAELAELEKEIAELRAEL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 417 DRDSHEDGD-----YYEVDINGPEILsckyhVAVAEAGELREQLKALHSTHEAREAQLAEekgrYEAEVQALTEKVSLLE 491
Cdd:COG4942 100 EAQKEELAEllralYRLGRQPPLALL-----LSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 76008363 492 KASHQDQELLAQLEKELRKVSDVAGETQGSLNVAQDELVTFSEELANL 539
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
346-507 1.62e-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: 41.67  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 346 EIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTENLSALRRLQAgkERQTSLDNEKDR------- 418
Cdd:COG4942  35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA--ELRAELEAQKEElaellra 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 419 --------------------DSHEDGDYYEVDINGPEILSCKYHVAVAEAGELREQLKALHSTHEAREAQLAEEKGRYEA 478
Cdd:COG4942 113 lyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
                       170       180
                ....*....|....*....|....*....
gi 76008363 479 EVQALTEKVSLLEKASHQDQELLAQLEKE 507
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQE 221
PRK12704 PRK12704
phosphodiesterase; Provisional
113-265 2.36e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  113 YYVRKVLeLQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGR------LRDDIKEYKFREARLLQDYSELEE 186
Cdd:PRK12704  22 YFVRKKI-AEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRnefekeLRERRNELQKLEKRLLQKEENLDR 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76008363  187 ENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDaiRLKEISERQLEEALETLKTEREQKnnLRKELSHYM 265
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ--ELERISGLTAEEAKEILLEKVEEE--ARHEAAVLI 175
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
60-263 2.38e-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: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    60 QFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESREESLIQESASKEQyyvrKVLELQTELKQLRNVLINTQSEN 139
Cdd:pfam05557  59 LLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKN----ELSELRRQIQRAELELQSTNSEL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   140 ERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREARLlqdySELEEEnISLQKQ----VSVLRQNQVEFEGLKHEIKRL 215
Cdd:pfam05557 135 EELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRI----KELEFE-IQSQEQdseiVKNSKSELARIPELEKELERL 209
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 76008363   216 EEETEYLNSQLEDAIRLKEISErQLEEALETLKTEREQKNNLRKELSH 263
Cdd:pfam05557 210 REHNKHLNENIENKLLLKEEVE-DLKRKLEREEKYREEAATLELEKEK 256
PTZ00121 PTZ00121
MAEBL; Provisional
23-260 2.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    23 RAEVKRLSHELAETTREKIQAAEYGLAVLEEK--HQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHKKVAADGESRE 100
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKkaDEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   101 ESLIQESASKEQYyVRKVLELQT--ELK---QLRNVLINTQSENERLTSV--AQELKEINQNVEIQRGRLRDDIKEYKFR 173
Cdd:PTZ00121 1532 EAKKADEAKKAEE-KKKADELKKaeELKkaeEKKKAEEAKKAEEDKNMALrkAEEAKKAEEARIEEVMKLYEEEKKMKAE 1610
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   174 EARLLQDYSELEEE---NISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEdaiRLKEISERQLEEALETLKTE 250
Cdd:PTZ00121 1611 EAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA---KKAEEDKKKAEEAKKAEEDE 1687
                         250
                  ....*....|
gi 76008363   251 REQKNNLRKE 260
Cdd:PTZ00121 1688 KKAAEALKKE 1697
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
337-539 2.91e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 2.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 337 DLLSELHISEIQKLKQQLVQMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTENLSALR-RLQAGKERQTSLDNE 415
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELElELEEAQAEEYELLAE 296
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 416 KDRdSHEDGDYYEVDINGpeilsckYHVAVAEAGELREQLKALHSTHEAREAQLAEEKGRYEAEVQALTEKVSLLEKASH 495
Cdd:COG1196 297 LAR-LEQDIARLEERRRE-------LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 76008363 496 QDQELLAQLEKELRKVSDVAGETQGSLNVAQDELVTFSEELANL 539
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
343-539 3.65e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  343 HISEIQKLKQQLVQmEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTEnLSALRRLQAGKERQTSLDNEKDRdsHE 422
Cdd:COG4913  233 HFDDLERAHEALED-AREQIELLEPIRELAERYAAARERLAELEYLRAALRL-WFAQRRLELLEAELEELRAELAR--LE 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  423 DgdyyEVDINGPEILSCKYHVAVAEA------GELREQLKALHSTHEAREAQLAEEKGRYEAEVQALTEKVSL----LEK 492
Cdd:COG4913  309 A----ELERLEARLDALREELDELEAqirgngGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAA 384
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 76008363  493 ASHQDQELLAQLEKELRKVSDVAGETQGSLNVAQDELVTFSEELANL 539
Cdd:COG4913  385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL 431
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
348-540 3.69e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 348 QKLKQQLvqMEREKVGLLATLQDTQKQLEQARGTLSEQHEKVSRLTEnlsALRRLQAGKERQTSLDNEKDRDSHEDGDyy 427
Cdd:COG1196 216 RELKEEL--KELEAELLLLKLRELEAELEELEAELEELEAELEELEA---ELAELEAELEELRLELEELELELEEAQA-- 288
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363 428 evdingpeilscKYHVAVAEAGELREQLKALhsthEAREAQLAEEKGRYEAEVQALTEKVSLLEKASHQDQELLAQLEKE 507
Cdd:COG1196 289 ------------EEYELLAELARLEQDIARL----EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
                       170       180       190
                ....*....|....*....|....*....|...
gi 76008363 508 LRKVSDVAGETQGSLNVAQDELVTFSEELANLY 540
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
22-261 4.19e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   22 LRAEVKRLSHELA--ETTREKIQAAEYGLA-VLEEKHQLKLQFEELEVDYEAIRSEMEQLKEafgqahtnHKKVAADGES 98
Cdd:PRK03918 174 IKRRIERLEKFIKrtENIEELIKEKEKELEeVLREINEISSELPELREELEKLEKEVKELEE--------LKEEIEELEK 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   99 REESLIQESASkeqyyvrkvleLQTELKQLRNVLINTQSENERLTSVAQELKEINQNVE--IQRGRLRDDIKEYKFREAR 176
Cdd:PRK03918 246 ELESLEGSKRK-----------LEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyIKLSEFYEEYLDELREIEK 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  177 LLQDYSE----LEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAIRLKEISERQLEEALETLKTERE 252
Cdd:PRK03918 315 RLSRLEEeingIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELE 394

                 ....*....
gi 76008363  253 QKNNLRKEL 261
Cdd:PRK03918 395 ELEKAKEEI 403
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
16-198 4.58e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     16 EAQPEWLRAEVKRLSHELAETTREKIQAAEYGLAVLEEKHQLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHK--KVA 93
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyREK 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363     94 ADGESREESLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSE-NERLTSVAQELKEINQNVEiqrgRLRDDIKEYKF 172
Cdd:TIGR02169  394 LEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINElEEEKEDKALEIKKQEWKLE----QLAADLSKYEQ 469
                          170       180
                   ....*....|....*....|....*.
gi 76008363    173 REARLLQDYSELEEENISLQKQVSVL 198
Cdd:TIGR02169  470 ELYDLKEEYDRVEKELSKLQRELAEA 495
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
17-247 5.26e-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: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   17 AQPEWLRAEVKRLSHELAETtREKIQAAEYGLAVLEEkhqLKLQFEELEVDYEAIRSEMEQLKEAFGQAHTNHkkvaadg 96
Cdd:COG4913  654 AEYSWDEIDVASAEREIAEL-EAELERLDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKEL------- 722
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   97 ESREESLIQESASKEQYYVRKVLELQTELKQLRNVLINTQSENERLTSVAQELKEINQNVEIQRGRLRDDIKEYKFREAR 176
Cdd:COG4913  723 EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPA 802
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76008363  177 LLQDYSELEEENISLQKQVSVLRQN-----QVEFEGLKHEikRLEEETEYLNSQLEDAIRlkEISER--QLEEALETL 247
Cdd:COG4913  803 ETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNE--NSIEFVADLLSKLRRAIR--EIKERidPLNDSLKRI 876
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
49-259 5.74e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.30  E-value: 5.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363   49 AVLEEKHQLKL-QFEEL--EVDYEAIRSEME----------QLKEAFGQAHTNHKKVAADGESREESLIQESASKEQYYV 115
Cdd:PRK05771  20 EVLEALHELGVvHIEDLkeELSNERLRKLRSlltklsealdKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  116 RKVLELQTELKQLRNVLINTQSENERL----------------TSVAQELKEINQNVEIQRGRLRDDIKEYKFREAR--- 176
Cdd:PRK05771 100 KEIKELEEEISELENEIKELEQEIERLepwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKgyv 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363  177 --LLQDYSELEEENISLQKQVSVLRQNQVEFEGLKHEIKRLEEETEYLNSQLEDAI-RLKEISER------QLEEALETL 247
Cdd:PRK05771 180 yvVVVVLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLeELKELAKKyleellALYEYLEIE 259
                        250
                 ....*....|..
gi 76008363  248 KTEREQKNNLRK 259
Cdd:PRK05771 260 LERAEALSKFLK 271
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
630-814 6.83e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 6.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    630 IRDQIKHLQAA--VDRTTELSRQRIASQElgpavdkDKEALMEEILKLKSLLSTKREQITTLRTVLKANKQTAEVALANL 707
Cdd:TIGR02168  218 LKAELRELELAllVLRLEELREELEELQE-------ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76008363    708 KSKYeNEKAMVTETMMKLRNELKALKEDAATFSSLRAMFATRCDEYITQLDEMQRQLAAAEDEKKTLNSLLRMAIQQKLA 787
Cdd:TIGR02168  291 YALA-NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
                          170       180
                   ....*....|....*....|....*..
gi 76008363    788 LTQRLELLELDHEQTRRGRNKATSKAK 814
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIA 396
 
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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